subject:(Rhodanese)

University of Groningen

1. Lijk, Leendert Joost. X-ray crystallographic studies on bovine liver rhodanese.

Degree: Faculty of Science and Engineering, 1981, University of Groningen

URL: https://www.rug.nl/research/portal/en/publications/xray-crystallographic-studies-on-bovine-liver-rhodanese(83403dd4-04eb-4089-9aa7-af64e5cfbf00).html ; urn:nbn:nl:ui:11-dbi/484c451d28a90 ; 83403dd4-04eb-4089-9aa7-af64e5cfbf00 ; 11370/83403dd4-04eb-4089-9aa7-af64e5cfbf00 ; urn:nbn:nl:ui:11-dbi/484c451d28a90 ; https://www.rug.nl/research/portal/en/publications/xray-crystallographic-studies-on-bovine-liver-rhodanese(83403dd4-04eb-4089-9aa7-af64e5cfbf00).html

► The crystal structure of the enzyme rhodanese was determined some years ago by X-ray analysis at a resolution of 2.5 A (Ploegman et al, 1978… (more)

Subjects/Keywords: Rhodanese; RÒntgendiffractie; Structuur Proefschriften (vo

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APA (6^th Edition):

Lijk, L. J. (1981). X-ray crystallographic studies on bovine liver rhodanese. (Doctoral Dissertation). University of Groningen. Retrieved from https://www.rug.nl/research/portal/en/publications/xray-crystallographic-studies-on-bovine-liver-rhodanese(83403dd4-04eb-4089-9aa7-af64e5cfbf00).html ; urn:nbn:nl:ui:11-dbi/484c451d28a90 ; 83403dd4-04eb-4089-9aa7-af64e5cfbf00 ; 11370/83403dd4-04eb-4089-9aa7-af64e5cfbf00 ; urn:nbn:nl:ui:11-dbi/484c451d28a90 ; https://www.rug.nl/research/portal/en/publications/xray-crystallographic-studies-on-bovine-liver-rhodanese(83403dd4-04eb-4089-9aa7-af64e5cfbf00).html

Chicago Manual of Style (16^th Edition):

Lijk, Leendert Joost. “X-ray crystallographic studies on bovine liver rhodanese.” 1981. Doctoral Dissertation, University of Groningen. Accessed January 24, 2021. https://www.rug.nl/research/portal/en/publications/xray-crystallographic-studies-on-bovine-liver-rhodanese(83403dd4-04eb-4089-9aa7-af64e5cfbf00).html ; urn:nbn:nl:ui:11-dbi/484c451d28a90 ; 83403dd4-04eb-4089-9aa7-af64e5cfbf00 ; 11370/83403dd4-04eb-4089-9aa7-af64e5cfbf00 ; urn:nbn:nl:ui:11-dbi/484c451d28a90 ; https://www.rug.nl/research/portal/en/publications/xray-crystallographic-studies-on-bovine-liver-rhodanese(83403dd4-04eb-4089-9aa7-af64e5cfbf00).html.

MLA Handbook (7^th Edition):

Lijk, Leendert Joost. “X-ray crystallographic studies on bovine liver rhodanese.” 1981. Web. 24 Jan 2021.

Vancouver:

Lijk LJ. X-ray crystallographic studies on bovine liver rhodanese. [Internet] [Doctoral dissertation]. University of Groningen; 1981. [cited 2021 Jan 24]. Available from: https://www.rug.nl/research/portal/en/publications/xray-crystallographic-studies-on-bovine-liver-rhodanese(83403dd4-04eb-4089-9aa7-af64e5cfbf00).html ; urn:nbn:nl:ui:11-dbi/484c451d28a90 ; 83403dd4-04eb-4089-9aa7-af64e5cfbf00 ; 11370/83403dd4-04eb-4089-9aa7-af64e5cfbf00 ; urn:nbn:nl:ui:11-dbi/484c451d28a90 ; https://www.rug.nl/research/portal/en/publications/xray-crystallographic-studies-on-bovine-liver-rhodanese(83403dd4-04eb-4089-9aa7-af64e5cfbf00).html.

Council of Science Editors:

Lijk LJ. X-ray crystallographic studies on bovine liver rhodanese. [Doctoral Dissertation]. University of Groningen; 1981. Available from: https://www.rug.nl/research/portal/en/publications/xray-crystallographic-studies-on-bovine-liver-rhodanese(83403dd4-04eb-4089-9aa7-af64e5cfbf00).html ; urn:nbn:nl:ui:11-dbi/484c451d28a90 ; 83403dd4-04eb-4089-9aa7-af64e5cfbf00 ; 11370/83403dd4-04eb-4089-9aa7-af64e5cfbf00 ; urn:nbn:nl:ui:11-dbi/484c451d28a90 ; https://www.rug.nl/research/portal/en/publications/xray-crystallographic-studies-on-bovine-liver-rhodanese(83403dd4-04eb-4089-9aa7-af64e5cfbf00).html

Virginia Tech

2. Cheng, Hui. Characterization of PspE, a Secreted Sulfurtransferase of Escherichia coli.

Degree: MS, Biochemistry, 2003, Virginia Tech

URL: http://hdl.handle.net/10919/32364

► PspE, encoded by the last gene of the phage shock protein operon, is one of the nine proteins of Escherichia coli that contain a rhodanese… (more)

▼ PspE, encoded by the last gene of the phage shock protein operon, is one of the nine proteins of Escherichia coli that contain a rhodanese homology domain. PspE is synthesized as a precursor with a 19-amino acid signal sequence and secreted to the periplasm. Mature PspE is the smallest rhodanese of E. coli (85 amino acids) and catalyzes the transfer of sulfur from thiosulfate to cyanide forming thiocyanate and sulfite. Cation exchange chromatography of a freeze-thaw extract of a PspE-overexpressing strain yielded two major peaks of active, homogeneous PspE. The two peaks contained two forms of PspE (PspE1 and PspE2) of distinct size and/or charge that were distinguished by native polyacrylamide gel electrophoresis and gel chromatography. PspE2 was converted to the more compact PspE1 by treatment with thiosulfate, which suggested that PspE1 is the persulfide form. One equivalent of cyanizable sulfur was associated with PspE1, with much less present in PspE2. Consistent with the conclusion that the single active site cysteine of PspE1 contains a persulfide sulfur was the observation that this form was much more tolerant to chemical inactivation by thiol-specific modifying reagent DTNB (5,5â -dithiobis(2-nitrobenzoic acid)). Rhodanese activity was subject to inhibition by anions (sulfite, sulfate, chloride, phosphate and arsenate), suggesting PspE has a cationic site for substrate binding. Kinetic analysis revealed that PspE employs a double-displacement mechanism, as is the case for other rhodaneses. The Kms for SSO32- and CN- were 3.0 and 43 mM, respectively. PspE exhibited a kcat of 72 s-1. To aid in understanding the physiological role of PspE, a strain with a pspE gene disruption was constructed. Comparison of rhodanese activity in extracts of wild-type and mutant strains revealed that PspE is a major contributor of rhodanese activity in E. coli. The pspE mutant displayed no obvious growth defect or auxotrophies, and was capable of molybdopterin biosynthesis, indicating that pspE is not essential for production of sulfur-containing amino acid or cofactors. Growth of wild-type and mutant strains deficient in pspE and other sulfurtransferase paralogs in medium with cyanide or cadmium was compared. The results indicated that neither PspE nor other E. coli rhodanese paralogs play roles in cyanide or cadmium detoxification. The physiological role of PspE remains to be determined. Advisors/Committee Members: Larson, Timothy J. (committeechair), Popham, David L. (committee member), Dean, Dennis R. (committee member).

Subjects/Keywords: sulfurtransferase; PspE; Escherichia coli; rhodanese

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Cheng, H. (2003). Characterization of PspE, a Secreted Sulfurtransferase of Escherichia coli. (Masters Thesis). Virginia Tech. Retrieved from http://hdl.handle.net/10919/32364

Chicago Manual of Style (16^th Edition):

Cheng, Hui. “Characterization of PspE, a Secreted Sulfurtransferase of Escherichia coli.” 2003. Masters Thesis, Virginia Tech. Accessed January 24, 2021. http://hdl.handle.net/10919/32364.

MLA Handbook (7^th Edition):

Cheng, Hui. “Characterization of PspE, a Secreted Sulfurtransferase of Escherichia coli.” 2003. Web. 24 Jan 2021.

Vancouver:

Cheng H. Characterization of PspE, a Secreted Sulfurtransferase of Escherichia coli. [Internet] [Masters thesis]. Virginia Tech; 2003. [cited 2021 Jan 24]. Available from: http://hdl.handle.net/10919/32364.

Council of Science Editors:

Cheng H. Characterization of PspE, a Secreted Sulfurtransferase of Escherichia coli. [Masters Thesis]. Virginia Tech; 2003. Available from: http://hdl.handle.net/10919/32364

3. W. Remelli. FRAMING THE ROLE OF RHODANESE-LIKE PROTEINS IN CELL REDOX BALANCE IN TWO BACTERIAL MODEL SYSTEMS.

Degree: 2012, Università degli Studi di Milano

URL: http://hdl.handle.net/2434/170507

► A key component of the host’s ability to survive bacterial challenge consist in the innate ability of macrophages to ingest and destroy the invading organism… (more)

▼ A key component of the host’s ability to survive bacterial challenge consist in the innate ability of macrophages to ingest and destroy the invading organism via various mechanisms which the most thoroughly studied is oxidative burst (Hanna et al., 1994). In response pathogens have evolved different approaches to survive the severe oxidative stress generated by the host. Genome analysis have clustered more than 14000 sequences coding for putative rhodanese like proteins. These sequences contain domains structurally similar to those of the extensively studied bovine rhodanese, and were found in more than 2100 species homogeneously distributed in all life's phyla. Proteins belonging to the rhodanese like superfamily (PFAM accession number: PF00581) are characterized by having more than 140 different architectures of the rhodanese domain, that can be present mostly alone or in tandem with another rhodanese domain, or fused to other functional domains. Although only few amino acid residues are conserved among rhodanese-like proteins, their most distinctive structural feature is the active site configuration, that contains an electronegative residue (generally cysteine) surrounded by positively charged residues. This particular architecture allows rhodanese-like proteins to bear a low pKa catalytic residue that can be the clue to explain their biological activity (Bordo et al 2001). Although the in vitro reported sulfurtransferase activity for the few characterized rhodanese-like proteins is the transfer of sulfur atom from a sulfur donor (e.g. thiosulfate) to a thiophilic acceptor (e.g. cyanide) (E.C. 2.8.1.x), in the last two decades the scientific community has started to indicate biological roles different from cyanide detoxification for rhodanese like proteins. Proposed roles for rhodanese like proteins can be summarized in two different but complementary fields. Rhodanese-like proteins can function as source of bioactive sulfur equivalents by the formation of a persulfide sulfur on a cysteine residue (R-SSH) (Cartini et al 2011), or can be involved in maintaining redox homeostasis acting as a direct or indirect scavengers of reactive oxygen species (ROS). My PhD research project was devoted to unravel the biological roles of rhodanese-like proteins using two prokaryotic model systems: the Azotobacter vinelandii and the Bacillus subtilis system. A. vinelandii is a Gram negative bacterium of the Pseudomonadaceae family in which redox balance must be carefully controlled due to its ability to fix molecular nitrogen via the molybdenum-iron-sulfur cluster enzyme nitrogenase (Setubal et al., 2009). The A. vinelandii genome possesses 14 ORFs coding for rhodanese like proteins with the tandem domain rhodanese-like protein RhdA (Gene ID: 7759697) being responsible for more than 80% of the crude extract thiosulfate:cyanide sulfurtransferase (TST) activity (Cartini et al., 2011). RhdA was widely studied in our lab from both structural and functional point of views. Starting from the evidence that the rhdA null-mutant… Advisors/Committee Members: tutor: F. Bonomi, supervisore: F. Forlani, coordinatore: F. Bonomi, BONOMI, FRANCESCO, FORLANI, FABIO, BONOMI, FRANCESCO.

Subjects/Keywords: rhodanese-like proteins; thiyl radical; redox homeostasis; glutathione; hydroxil radical; bacteria; Settore BIO/10 - Biochimica

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Remelli, W. (2012). FRAMING THE ROLE OF RHODANESE-LIKE PROTEINS IN CELL REDOX BALANCE IN TWO BACTERIAL MODEL SYSTEMS. (Thesis). Università degli Studi di Milano. Retrieved from http://hdl.handle.net/2434/170507

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Remelli, W.. “FRAMING THE ROLE OF RHODANESE-LIKE PROTEINS IN CELL REDOX BALANCE IN TWO BACTERIAL MODEL SYSTEMS.” 2012. Thesis, Università degli Studi di Milano. Accessed January 24, 2021. http://hdl.handle.net/2434/170507.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Remelli, W.. “FRAMING THE ROLE OF RHODANESE-LIKE PROTEINS IN CELL REDOX BALANCE IN TWO BACTERIAL MODEL SYSTEMS.” 2012. Web. 24 Jan 2021.

Vancouver:

Remelli W. FRAMING THE ROLE OF RHODANESE-LIKE PROTEINS IN CELL REDOX BALANCE IN TWO BACTERIAL MODEL SYSTEMS. [Internet] [Thesis]. Università degli Studi di Milano; 2012. [cited 2021 Jan 24]. Available from: http://hdl.handle.net/2434/170507.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Remelli W. FRAMING THE ROLE OF RHODANESE-LIKE PROTEINS IN CELL REDOX BALANCE IN TWO BACTERIAL MODEL SYSTEMS. [Thesis]. Università degli Studi di Milano; 2012. Available from: http://hdl.handle.net/2434/170507

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Freie Universität Berlin

4. Krueger, Katharina. Characterization of the antioxidant enzymes rhodanese and superoxide dismutase 1 in chronic renal failure.

Degree: 2011, Freie Universität Berlin

URL: http://dx.doi.org/10.17169/refubium-10077

► Patients with chronic kidney disease (CKD), including dialysis patients (HD), have a high incidence of premature cardiovascular disease. It is the leading cause of mortality… (more)

▼ Patients with chronic kidney disease (CKD), including dialysis patients (HD), have a high incidence of premature cardiovascular disease. It is the leading cause of mortality in these patients. In the present study the antioxidant emzymes rhodanese and superoxide dismutase 1 were analyzed in monocytes of patients with CKD. The mRNA expression was determined by quantitative real- time PCR, the protein expression was determined by Immunoblotting and in-cell Western assay. Reactive oxygen species were measured by fluorescence spectrometry. Monocytes of hemodialysis patients showed a significant decrease in rhodanese protein and mRNA expression compared to healthy subjects. At the same time they showed an increased whole cell reactive oxygen species production. Furthermore, the level of mitochondrial superoxide production was significantly correlated with rhodanese protein expression in monocytes. Survival of hemodialysis patients was significantly shorter when patients monocytes expressed a low rhodanese mRNA. The analysis of proteomic profiles in monocytes of patients with CKD, including HD patients, and control subjects by two-dimensional electrophoresis (2-DE) indicated differences in spot pattern. The SOD1 protein, which was identified by MS/MS mass spectrometry and immunoblotting, was reduced in kidney disease. The characterization of SOD1 protein by in-cell Western assay showed a significant decrease of SOD1 protein in HD patients compared to CKD patients and healthy subjects. SOD1 gene expression was significantly higher in HD patients compared to CKD patients, or control subjects. Furthermore, the immunostaining of 2-DE gel blot membranes with SOD1 antibody revealed six immunoreactive spots, suggesting the appearance of different SOD1 protein species. A further study showed the importance of SOD1 within the antioxidant defence. The incubation of monocytes with high glucose concentration induced an increase of reactive oxygen species production. The effect of glucose was blocked by the SOD1 mimetic Tempol. Advisors/Committee Members: w (gender), Prof. Dr. med. M. Tepel (firstReferee), Prof. Dr. med. M. van der Giet (furtherReferee), Priv.-Doz. Dr. med. B. Henning (furtherReferee).

Subjects/Keywords: oxidative stress; chronic renal failure; rhodanese; superoxide dismutase 1; 600 Technik, Medizin, angewandte Wissenschaften::610 Medizin und Gesundheit

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Krueger, K. (2011). Characterization of the antioxidant enzymes rhodanese and superoxide dismutase 1 in chronic renal failure. (Thesis). Freie Universität Berlin. Retrieved from http://dx.doi.org/10.17169/refubium-10077

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Krueger, Katharina. “Characterization of the antioxidant enzymes rhodanese and superoxide dismutase 1 in chronic renal failure.” 2011. Thesis, Freie Universität Berlin. Accessed January 24, 2021. http://dx.doi.org/10.17169/refubium-10077.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Krueger, Katharina. “Characterization of the antioxidant enzymes rhodanese and superoxide dismutase 1 in chronic renal failure.” 2011. Web. 24 Jan 2021.

Vancouver:

Krueger K. Characterization of the antioxidant enzymes rhodanese and superoxide dismutase 1 in chronic renal failure. [Internet] [Thesis]. Freie Universität Berlin; 2011. [cited 2021 Jan 24]. Available from: http://dx.doi.org/10.17169/refubium-10077.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Krueger K. Characterization of the antioxidant enzymes rhodanese and superoxide dismutase 1 in chronic renal failure. [Thesis]. Freie Universität Berlin; 2011. Available from: http://dx.doi.org/10.17169/refubium-10077

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

University of Florida

5. Hepowit, Nathaniel L. Activation, Thiocarboxylation, and Deconjugation of Archaeal Ubiquitin-like Proteins.

Degree: PhD, Microbiology and Cell Science, 2014, University of Florida

URL: https://ufdc.ufl.edu/UFE0047496

► Many cellular processes in eukarytic system are dynamically regulated by posttranslational covalent attachment of modifier proteins, such as ubiquitin (Ub) and ubiquitin-like proteins (Ubls). Recent… (more)

▼ Many cellular processes in eukarytic system are dynamically regulated by posttranslational covalent attachment of modifier proteins, such as ubiquitin (Ub) and ubiquitin-like proteins (Ubls). Recent findings show that the ubiquitin-like small archaeal modifier proteins (SAMPs) is central in Archaea, and is evolutionarily unique of having dual functions: protein conjugation (sampylation) and sulfur mobilization. In particular, this study focuses on understanding the underlying molecular mechanisms that explain how archaea manage to regulate and modulate sampylation and sulfur mobilization systems. Here, we found that the contributing factors that influence the dual function of SAMP include the residues at the binding interface between SAMP and UbaA (SAMP-activating enzyme), the conserved residues proximal to the ATP-binding pocket of UbaA, and the protein associates of UbaA, such as the rhodanese-like UbaC and the catalytic subunit of molybdopterin synthase, MoaE. Our results show that the conserved diglycine motif of the Ub-fold proteins and ATP are found essential for association of the dual function E1-like UbaA with the Ub-fold SAMPs in vivo and in vitro. Likewise, ATP hydrolysis is required for SAMP adenylation, which marks as the point where the pathways for sampylation and sulfur transfer diverge. Similar to ubiquitylation, we propose that the formation of the thiol-dependent activation intermediate complex of UbaA and SAMP is the mechanistic switch that readies SAMP1 for isopeptide-based conjugation. In contrast, subsequent association of the adenyated SAMP1 with the rhodanese-like protein UbaC prepares SAMP1 for MoCo biosynthesis. While UbaA which is required for global sampylation, UbaC is required only in SAMP1-MoaE conjugate formation at the active site K240 and K247 of MoaE, suggesting the possible regulatory role of sampylation in sulfur relay. Moreover, it is proposed that the proteolytic function of the JAMM/MPN+ domain metalloprotease (HvJAMM1) is antagonistic on global sampylation but has possible modulatory roles in sulfur relay by possibly reactivating MPT function for MoCo biosynthesis. ( en ) Advisors/Committee Members: MAUPIN,JULIE A (committee chair), LORCA,GRACIELA L (committee member), GONZALEZ,CLAUDIO F (committee member), CHEN,SIXUE (committee member).

Subjects/Keywords: Amino acids; Biosynthesis; DNA; Enzymes; Plasmids; Polymerase chain reaction; Proteins; Sulfur; Transfer RNA; Ubiquitins; archaea – desampylation – molybdopterin – proteasome – rhodanese – sampylation – ubiquitin

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Hepowit, N. L. (2014). Activation, Thiocarboxylation, and Deconjugation of Archaeal Ubiquitin-like Proteins. (Doctoral Dissertation). University of Florida. Retrieved from https://ufdc.ufl.edu/UFE0047496

Chicago Manual of Style (16^th Edition):

Hepowit, Nathaniel L. “Activation, Thiocarboxylation, and Deconjugation of Archaeal Ubiquitin-like Proteins.” 2014. Doctoral Dissertation, University of Florida. Accessed January 24, 2021. https://ufdc.ufl.edu/UFE0047496.

MLA Handbook (7^th Edition):

Hepowit, Nathaniel L. “Activation, Thiocarboxylation, and Deconjugation of Archaeal Ubiquitin-like Proteins.” 2014. Web. 24 Jan 2021.

Vancouver:

Hepowit NL. Activation, Thiocarboxylation, and Deconjugation of Archaeal Ubiquitin-like Proteins. [Internet] [Doctoral dissertation]. University of Florida; 2014. [cited 2021 Jan 24]. Available from: https://ufdc.ufl.edu/UFE0047496.

Council of Science Editors:

Hepowit NL. Activation, Thiocarboxylation, and Deconjugation of Archaeal Ubiquitin-like Proteins. [Doctoral Dissertation]. University of Florida; 2014. Available from: https://ufdc.ufl.edu/UFE0047496

University of Georgia

6. Liu, Yuchen. Adaptations of Methanococcus maripaludis to its unique lifestyle.

Degree: 2014, University of Georgia

URL: http://hdl.handle.net/10724/26702

► Methanococcus maripaludis is an obligate anaerobic, methane-producing archaeon. In addition to the unique methanogenesis pathway, unconventional biochemistry is present in this organism in adaptation to… (more)

▼ Methanococcus maripaludis is an obligate anaerobic, methane-producing archaeon. In addition to the unique methanogenesis pathway, unconventional biochemistry is present in this organism in adaptation to its unique lifestyle. The Sac10b homolog in M. maripaludis, Mma10b, is not abundant and constitutes only ~ 0.01% of the total cellular protein. It binds to DNA with sequence-specificity. Disruption of mma10b resulted in poor growth of the mutant in minimal medium. These results suggested that the physiological role of Mma10b in the mesophilic methanococci is greatly diverged from the homologs in thermophiles, which are highly abundant and associate with DNA without sequence-specificity. M. maripaludis synthesizes lysine through the DapL pathway, which uses diaminopimelate aminotransferase (DapL) to catalyze the direct transfer of an amino group from L-glutamate to L-tetrahydrodipicolinate (THDPA), forming LL-diaminopimelate (LL-DAP). This is different from the conventional acylation pathway in many bacteria that convert THDPA to LL-DAP in three steps: succinylation or acetylation, transamination, and desuccinylation or deacetylation. The DapL pathway eliminates the expense of using succinyl-CoA or acetyl-CoA and may represent a thriftier mode for lysine biosynthesis. Methanogens synthesize cysteine primarily on tRNACys via the two-step SepRS/SepCysS pathway. In the first step, tRNACys is aminoacylated with O-phosphoserine (Sep) by O-phosphoseryl-tRNA synthetase (SepRS). In the second step, the Sep moiety on Sep-tRNACys is converted to cysteine with a sulfur source to form Cys-tRNACys by Sep-tRNA:Cys-tRNA synthase (SepCysS). The nature of the physiological sulfur donor for the tRNA-dependent cysteine biosynthesis is unknown. Based upon activity assays in M. maripaludis cell extracts, a rhodanese-like, protein-mediated sulfur transfer is proposed to be involved in the sulfur assimilation for cysteine biosynthesis. This is different from cysteine biosynthesis in enteric bacteria and plants, which use direct sulfhydrylation with sulfide. Finally, M. maripaludis does not use cysteine as the sulfur source for Fe-S cluster biosynthesis. Instead, the sulfur in Fe-S clusters is derived predominantly from exogenous sulfide. This challenges the concept that cysteine is always the sulfur source for Fe-S cluster biosynthesis. The unique sulfur metabolism in M. maripaludis may be an adaptation to sulfide-rich living environments.

Subjects/Keywords: archaea; methanogens; Methanococcus maripaludis; DNA-binding protein; lysine biosynthesis; cysteine biosynthesis; iron-sulfur cluster; methionine biosynthesis; rhodanese

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Liu, Y. (2014). Adaptations of Methanococcus maripaludis to its unique lifestyle. (Thesis). University of Georgia. Retrieved from http://hdl.handle.net/10724/26702

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Liu, Yuchen. “Adaptations of Methanococcus maripaludis to its unique lifestyle.” 2014. Thesis, University of Georgia. Accessed January 24, 2021. http://hdl.handle.net/10724/26702.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Liu, Yuchen. “Adaptations of Methanococcus maripaludis to its unique lifestyle.” 2014. Web. 24 Jan 2021.

Vancouver:

Liu Y. Adaptations of Methanococcus maripaludis to its unique lifestyle. [Internet] [Thesis]. University of Georgia; 2014. [cited 2021 Jan 24]. Available from: http://hdl.handle.net/10724/26702.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Liu Y. Adaptations of Methanococcus maripaludis to its unique lifestyle. [Thesis]. University of Georgia; 2014. Available from: http://hdl.handle.net/10724/26702

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Virginia Tech

7. Ahmed, Farzana. Characterization of two novel proteins containing the rhodanese homology domain: YgaP and YbbB of Escherichia coli.

Degree: PhD, Biochemistry, 2003, Virginia Tech

URL: http://hdl.handle.net/10919/11233

► Rhodanese homology domains are ubiquitous structural modules found in eubacteria, eukaryotes and archaea. The rhodanese homology domain may comprise the entire structure of a protein.… (more)

▼ Rhodanese homology domains are ubiquitous structural modules found in eubacteria, eukaryotes and archaea. The rhodanese homology domain may comprise the entire structure of a protein. Alternatively it is found as tandemly repeated modules in which the C-terminal domain displays the properly structured active site. Finally it is found as a member of many multidomain proteins. Although some members of this family of proteins show sulfurtransferase activity in vitro, their specific physiological functions remain largely undefined. Fusion of a rhodanese domain to different protein domains of known or unknown functions provides important clues to the diverse roles for these proteins. Nine proteins containing the rhodanese homology domain are predicted in Escherichia coli. In this work, two of these proteins: YgaP and YbbB were characterized using bioinformatics, biochemical and genetic approaches. YgaP is a single domain rhodanese that is predicted to contain an amino-terminal rhodanese domain (118 amino acids) and a hydrophobic carboxy-terminal domain (56 amino acids). The ygaP gene was cloned into a vector that directed overexpression of a membrane-associated rhodanese activity. The cellular location of YgaP was determined by using sucrose density layer ultracentrifugation. YgaP and rhodanese activity co-sedimented with the cytoplasmic membrane marker D-lactate dehydrogenase, and was not present in the outer membrane fractions, indicating YgaP is a cytoplasmic membrane protein. A polyhistidine-tagged variant of YgaP was subsequently solubilized from the membrane by detergent extraction and purified by metal chelate chromatography. Similar to the other characterized rhodaneses, purified YgaP-His6 as well as the membrane-associated native form of the protein displayed a double displacement (ping-pong) mechanism. YgaP is unique in that it is the first membrane-associated rhodanese to be described. To understand the physiological role of YgaP, a strain with ygaP gene disruption was constructed. No obvious phenotype resulted from deletion of ygaP. The ybbB gene of E. coli has an interesting genome organization in several Gram-negative bacteria including Pseudomonas aeruginosa and Azotobacter vinelandii where it is predicted to be in the same operon with selD, encoding selenophosphate synthetase. Thus the role of YbbB in selenium metabolism was investigated. A strain with ybbB gene deletion was constructed and tested for its ability to incorporate 75Se into tRNA and protein. It was shown that the disruption of ybbB prevented specific incorporation of selenium into tRNA but not into proteins in vivo. The modified nucleoside missing in tRNAs of the DybbB strain was identified as 5-methylaminomethyl-2-selenouridine (mnm5se2U), which has previously been shown to be present in the wobble position of the anticodon of E. coli tRNAsLys, Glu and Gln. Data from HPLC analysis showed that the deletion of ybbB did not affect the production of 5-methylaminomethyl-2-thiouridine (mnm5s2U), the precursor to mnm5se2U,… Advisors/Committee Members: Larson, Timothy J. (committeechair), Popham, David L. (committee member), Bevan, David R. (committee member), Chen, Jiann-Shin (committee member), Dean, Dennis R. (committee member).

Subjects/Keywords: seleno-tRNA; YgaP; YbbB; 2-selenouridine; rhodanese

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APA (6^th Edition):

Ahmed, F. (2003). Characterization of two novel proteins containing the rhodanese homology domain: YgaP and YbbB of Escherichia coli. (Doctoral Dissertation). Virginia Tech. Retrieved from http://hdl.handle.net/10919/11233

Chicago Manual of Style (16^th Edition):

Ahmed, Farzana. “Characterization of two novel proteins containing the rhodanese homology domain: YgaP and YbbB of Escherichia coli.” 2003. Doctoral Dissertation, Virginia Tech. Accessed January 24, 2021. http://hdl.handle.net/10919/11233.

MLA Handbook (7^th Edition):

Ahmed, Farzana. “Characterization of two novel proteins containing the rhodanese homology domain: YgaP and YbbB of Escherichia coli.” 2003. Web. 24 Jan 2021.

Vancouver:

Ahmed F. Characterization of two novel proteins containing the rhodanese homology domain: YgaP and YbbB of Escherichia coli. [Internet] [Doctoral dissertation]. Virginia Tech; 2003. [cited 2021 Jan 24]. Available from: http://hdl.handle.net/10919/11233.

Council of Science Editors:

Ahmed F. Characterization of two novel proteins containing the rhodanese homology domain: YgaP and YbbB of Escherichia coli. [Doctoral Dissertation]. Virginia Tech; 2003. Available from: http://hdl.handle.net/10919/11233

Virginia Tech

8. Jutabha, Promjit. Biochemical and genetic characterization of mercaptopyruvate sulfurtransferase and paralogous putative sulfurtransferases of Escherichia coli.

Degree: PhD, Biochemistry, 2001, Virginia Tech

URL: http://hdl.handle.net/10919/28109

► Sulfurtransferases, including mercaptopyruvate sulfurtransferase and rhodanese, are widely distributed in living organisms. Mercaptopyruvate sulfurtransferase and rhodanese catalyze the transfer of sulfur from mercaptopyruvate and thiosulfate,… (more)

▼ Sulfurtransferases, including mercaptopyruvate sulfurtransferase and rhodanese, are widely distributed in living organisms. Mercaptopyruvate sulfurtransferase and rhodanese catalyze the transfer of sulfur from mercaptopyruvate and thiosulfate, respectively, to sulfur acceptors such as thiols or cyanide. There is evidence to suggest that rhodanese can mobilize sulfur from thiosulfate for in vitro formation of iron-sulfur clusters. Additionally, primary sequence analysis reveals that MoeB from some organisms, as well as ThiI of Escherichia coli, contain a C-terminal sulfurtransferase domain. MoeB is required for molybdopterin biosynthesis, whereas ThiI is necessary for biosynthesis of thiamin and 4-thiouridine in transfer ribonucleic acid. These observations led to the hypothesis that sulfurtransferases might be involved in sulfur transfer for biosynthesis of some sulfur-containing cofactors (e.g., biotin, lipoic acid, thiamin and molybdopterin). Results of a BLAST search revealed that E. coli has at least eight potential sulfurtransferases, besides ThiI. Previously, a glpE-encoded rhodanese of E. coli was characterized in our laboratory. In this dissertation, a mercaptopyruvate sulfurtransferase and corresponding gene (sseA) of E. coli were identified. In addition, the possibility that mercaptopyruvate sulfurtransferase could participate or work in concert with a cysteine desulfurase, IscS, in the biosynthesis of cofactors was examined. Cloning of the sseA gene and biochemical characterization of the corresponding protein were used to show that SseA is a mercaptopyruvate sulfurtransferase of E. coli. A strain with a chromosomal insertion mutation in sseA was constructed in order to characterize the physiological function of mercaptopyruvate sulfurtransferase. However, the lack of SseA did not result in a discernable phenotypic change. Redundancy of sulfurtransferases in E. coli may prevent the appearance of a phenotypic change due to the loss of a single sulfurtransferase. Subsequently, other paralogous genes for putative sulfurtransferases, including ynjE and yceA, were cloned. Strains with individual deletions of the chromosomal ynjE and yceA genes were also constructed. Finally, strains with multiple deficiency in potential sulfurtransferase genes, including sseA, ynjE and glpE, as well as iscS, were created. However, no phenotype associated with combinations of sseA, glpE and/or ynjE deficiency was identified. Therefore, the physiological functions of mercaptopyruvate sulfurtransferase and related sulfurtransferases remain unknown. Advisors/Committee Members: Larson, Timothy J. (committeechair), Popham, David L. (committee member), Stevens, Ann M. (committee member), Dean, Dennis R. (committee member), Chen, Jiann-Shin (committee member).

Subjects/Keywords: Mercaptopyruvate sulfurtransferase; Escherichia coli; sulfurtransferase ortholog; rhodanese

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Jutabha, P. (2001). Biochemical and genetic characterization of mercaptopyruvate sulfurtransferase and paralogous putative sulfurtransferases of Escherichia coli. (Doctoral Dissertation). Virginia Tech. Retrieved from http://hdl.handle.net/10919/28109

Chicago Manual of Style (16^th Edition):

Jutabha, Promjit. “Biochemical and genetic characterization of mercaptopyruvate sulfurtransferase and paralogous putative sulfurtransferases of Escherichia coli.” 2001. Doctoral Dissertation, Virginia Tech. Accessed January 24, 2021. http://hdl.handle.net/10919/28109.

MLA Handbook (7^th Edition):

Jutabha, Promjit. “Biochemical and genetic characterization of mercaptopyruvate sulfurtransferase and paralogous putative sulfurtransferases of Escherichia coli.” 2001. Web. 24 Jan 2021.

Vancouver:

Jutabha P. Biochemical and genetic characterization of mercaptopyruvate sulfurtransferase and paralogous putative sulfurtransferases of Escherichia coli. [Internet] [Doctoral dissertation]. Virginia Tech; 2001. [cited 2021 Jan 24]. Available from: http://hdl.handle.net/10919/28109.

Council of Science Editors:

Jutabha P. Biochemical and genetic characterization of mercaptopyruvate sulfurtransferase and paralogous putative sulfurtransferases of Escherichia coli. [Doctoral Dissertation]. Virginia Tech; 2001. Available from: http://hdl.handle.net/10919/28109

Virginia Tech

9. Hunt, Jeremy Paul. Genetic and biochemical characterization of YrkF, a novel two-domain sulfurtransferase in Bacillus subtilis.

Degree: MS, Biochemistry, 2004, Virginia Tech

URL: http://hdl.handle.net/10919/34714

► Sulfur-containing compounds such as thiamin, biotin, molybdopterin, lipoic acid, and [Fe-S] clusters are essential for life. Sulfurtransferases are present in eukaryotes, eubacteria, and archaea… (more)

▼ Sulfur-containing compounds such as thiamin, biotin, molybdopterin, lipoic acid, and [Fe-S] clusters are essential for life. Sulfurtransferases are present in eukaryotes, eubacteria, and archaea and are believed to play important roles in mobilizing sulfur necessary for biosynthesis of these compounds and for normal cellular functions. The rhodanese homology domain is a ubiquitous structural module containing a characteristic active site cysteine residue. Some proteins containing a rhodanese domain display thiosulfate:cyanide sulfurtransferase activity in vitro. However, the physiological functions of rhodaneses remain largely unknown. YrkF, the first rhodanese to be characterized from Bacillus subtilis, is a unique protein containing two domains, an N-terminal Ccd1 domain and a C-terminal rhodanese domain. Ccd1 (conserved cysteine domain 1) is a ubiquitous structural module characterized by a Cys-Pro-X-Pro sequence motif. Thus, YrkF contains two cysteine residues (Cys¹⁵ and Cys¹⁴⁹), one in each domain. Biochemical, genetic, and bioinformatic approaches were used in order to characterize YrkF. First, YrkF was overexpressed and assayed for rhodanese activity to show that the protein is a functional rhodanese. A variant protein, YrkF^C15A, containing a cysteine to alanine substitution in the Ccd1 domain was created to determine if the Ccd1 cysteine is essential for rhodanese activity. The variant protein was overexpressed and rhodanese assays showed that YrkF^C15A is also a functional rhodanese. Inherent structural and catalytic differences were observed when comparing YrkF and YrkF^C15A, which may reflect the importance of the Ccd1 cysteine residue to normal enzymatic function and structural stability. Initial kinetic studies identified differences in activity between YrkF and YrkF^C15A. Cross-linking experiments showed a propensity for the formation of inter- and intramolecular disulfide bonds between the two cysteine residues and indicated that Cys¹⁵ and Cys¹⁴⁹ are located near one another in the 3-dimensional structure of the protein. Analysis of the proteins by mass spectrometry suggested YrkF contains a stable persulfide sulfur, whereas YrkF^C15A showed no evidence of a stable persulfide sulfur and was prone to oxidation and other active site modifications. A homology model of YrkF was created using structures of a rhodanese homolog and a Ccd1 homolog as templates. The model was used to predict the structure of YrkF based on the results of the cross-linking experiments. A strain containing a yrkF chromosomal deletion could be constructed, indicating YrkF is not essential for survival. Phenotypic analysis of the yrkF mutant revealed that YrkF is not needed for biosynthesis of sulfur-containing cofactors (thiamin, biotin, molybdopterin, or lipoic acid) or amino acids. The characterization of YrkF could lead to the discovery of novel physiological roles for rhodaneses and may… Advisors/Committee Members: Larson, Timothy J. (committeechair), Dean, Dennis R. (committee member), Winkel, Brenda S. J. (committee member).

Subjects/Keywords: disulfide cross-linking; YrkF; rhodanese; Ccd1; persulfide sulfur

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Hunt, J. P. (2004). Genetic and biochemical characterization of YrkF, a novel two-domain sulfurtransferase in Bacillus subtilis. (Masters Thesis). Virginia Tech. Retrieved from http://hdl.handle.net/10919/34714

Chicago Manual of Style (16^th Edition):

Hunt, Jeremy Paul. “Genetic and biochemical characterization of YrkF, a novel two-domain sulfurtransferase in Bacillus subtilis.” 2004. Masters Thesis, Virginia Tech. Accessed January 24, 2021. http://hdl.handle.net/10919/34714.

MLA Handbook (7^th Edition):

Hunt, Jeremy Paul. “Genetic and biochemical characterization of YrkF, a novel two-domain sulfurtransferase in Bacillus subtilis.” 2004. Web. 24 Jan 2021.

Vancouver:

Hunt JP. Genetic and biochemical characterization of YrkF, a novel two-domain sulfurtransferase in Bacillus subtilis. [Internet] [Masters thesis]. Virginia Tech; 2004. [cited 2021 Jan 24]. Available from: http://hdl.handle.net/10919/34714.

Council of Science Editors:

Hunt JP. Genetic and biochemical characterization of YrkF, a novel two-domain sulfurtransferase in Bacillus subtilis. [Masters Thesis]. Virginia Tech; 2004. Available from: http://hdl.handle.net/10919/34714

Universidade Nova

10. Gutierres, André Luís Teixeira. Structural and functional studies on human enzymes involved in hydrogen sulfide breakdown.

Degree: 2017, Universidade Nova

URL: http://www.rcaap.pt/detail.jsp?id=oai:run.unl.pt:10362/19981

► In human physiology, hydrogen sulfide (H2S), a small gaseous molecule that diffuses across aqueous and hydrophobic milieu, has been shown to team up with NO… (more)

▼ In human physiology, hydrogen sulfide (H2S), a small gaseous molecule that diffuses across aqueous and hydrophobic milieu, has been shown to team up with NO and CO as the third ‘gasotransmitter’. The still growing number of physiological processes shown to be regulated by H2S includes blood flow, cellular stress response, inflammation, immune defense, apoptosis and energy metabolism. Consequently, disturbed H2S metabolism is associated with numerous human pathologies, from cardiovascular and inflammatory disorders, to neurodegeneration and cancer. As any other reactive signaling molecule, H2S homeostasis requires a fine balance between its synthesis and breakdown. One of the enzymes involved in the synthesis of H2S in humans is cystathionine β-synthase (CBS), one key enzyme of the transsulfuration pathway. H2S breakdown relies on a mitochondrial pathway involving a sulfide:quinone oxidoreductase (SQR), a sulfur dioxygenase, Rhodanese, and a sulfite oxidase. O2-dependent H2S consumption may be primarily controlled by its efficient catabolism via SQR, which may be a key regulator in switching off H2S signaling by consuming it. Although numerous studies have focused on the functional analysis of H2S catabolism components, there is a paucity of structural data to support i) the understanding of functional/physiological data, and ii) the discovery and design of modulatory compounds with potential pharmacological interest. The aim of this dissertation was to characterize from a structural and functional viewpoint human enzymes involved in H2S metabolism, employing different biophysical methodologies. Recombinant human Rhodanese was expressed in Escherichia coli and purified with a yield of 2mg/L of culture. By a combination of DSF (Differential Scanning Fluorimetry), CD (Circular Dichroism) and SAXS (Small Angle X-ray Scattering) studies, it was observed that cysteine, thiosulfate and alliin affects Rhodanese structure. This information was used into crystallization trials but without getting any Rhodanese crystals. The recombinant human SQR expression and purification was unsuccessful, precluding any further studies, and being still under development. In parallel with work on the sulfide oxidizing unit, structural studies were carried out with recombinant human cystathionine β-synthase. In particular, the crystallographic structure of the disease-causing variant CBS P49L was obtained at 2.8 Å resolution, showing very subtle differences from the WT CBS structure. However, these do not completely explain the functional impact of this mutation and its pathogenicity. Advisors/Committee Members: Vicente, João, Archer, Margarida, Brito, José.

Subjects/Keywords: Hydrogen Sulfide (H2S); Sulfide:quinone Oxidoreductase (SQR); Rhodanese (Rhod); Cystathionine β-synthase (CBS); X-ray crystallography; Small Angle X-ray Scattering (SAXS); Domínio/Área Científica::Engenharia e Tecnologia::Engenharia Química

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APA (6^th Edition):

Gutierres, A. L. T. (2017). Structural and functional studies on human enzymes involved in hydrogen sulfide breakdown. (Thesis). Universidade Nova. Retrieved from http://www.rcaap.pt/detail.jsp?id=oai:run.unl.pt:10362/19981

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Gutierres, André Luís Teixeira. “Structural and functional studies on human enzymes involved in hydrogen sulfide breakdown.” 2017. Thesis, Universidade Nova. Accessed January 24, 2021. http://www.rcaap.pt/detail.jsp?id=oai:run.unl.pt:10362/19981.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Gutierres, André Luís Teixeira. “Structural and functional studies on human enzymes involved in hydrogen sulfide breakdown.” 2017. Web. 24 Jan 2021.

Vancouver:

Gutierres ALT. Structural and functional studies on human enzymes involved in hydrogen sulfide breakdown. [Internet] [Thesis]. Universidade Nova; 2017. [cited 2021 Jan 24]. Available from: http://www.rcaap.pt/detail.jsp?id=oai:run.unl.pt:10362/19981.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Gutierres ALT. Structural and functional studies on human enzymes involved in hydrogen sulfide breakdown. [Thesis]. Universidade Nova; 2017. Available from: http://www.rcaap.pt/detail.jsp?id=oai:run.unl.pt:10362/19981

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

11. Aussignargues, Clement. Optimisation du métabolisme énergétique du soufre chez la bactérie hyperthermophile Aquifex aeolicus. : Prediction of the compliance of packaging materials using deformulation methods and partition coefficients modelling.

Degree: Docteur es, Microbiologie, 2012, Aix Marseille Université

URL: http://www.theses.fr/2012AIXM4709

►

Le soufre est utilisé à des fins bioénergétiques par des micro-organismes tels que la bactérie hyperthermophile Aquifex aeolicus qui nécessite pour sa croissance de l'oxygène,… (more)

▼

Le soufre est utilisé à des fins bioénergétiques par des micro-organismes tels que la bactérie hyperthermophile Aquifex aeolicus qui nécessite pour sa croissance de l'oxygène, de l'hydrogène et un composé soufré indispensable. Une soufre réductase réduisant des chaînes de soufre, une Sulfure Quinone Oxydoréductase (SQR) oxydant l'H2S et une Soufre Oxygénase Réductase (SOR) oxydant et réduisant simultanément des chaînes de soufre ont été caractérisées chez cette bactérie. L'organisation de certaines de ces enzymes dans des supercomplexes membranaires a également été démontrée.Nous avons montré qu'Aq_477, précédemment caractérisée comme une soufre transférase de la famille des rhodanèses, est capable (i) de « charger » des chaînes de soufre ; (ii) d'interagir avec deux partenaires (la soufre réductase et la SOR) ; (iii) de leur présenter ce substrat. Ceci conduit à une optimisation du métabolisme. Nous avons ainsi démontré l'implication directe d'Aq_477, rebaptisée SbdP pour Sulfur -binding -donating Protein, dans le métabolisme énergétique du soufre de la bactérie. Une analyse poussée du génome nous a permis de construire un nouveau modèle suggérant notamment un recyclage des composés soufrés entre différents systèmes enzymatiques. La recherche de l'existence d'un niveau d'organisation des complexes respiratoires supérieur aux supercomplexes chez Aquifex aeolicus nous a conduits à développer de nouvelles méthodes d'étude permettant de proposer plusieurs pistes de recherche. Enfin, nous avons montré l'existence d'un nanocompartiment protéique constitué de l'encapsuline Aq_1760, dans lequel vient s'ancrer la ferritine atypique à domaines en tandem Aq_331.

Sulfur can be used in energy metabolism by microorganisms as electron donor and acceptor. The hyperthermophilic bacterium Aquifex aeolicus, which need oxygen, hydrogen and an essential sulfur compound for its growth presents sulfur reduction and oxidation pathways linked to the energy synthesis. A sulfur reductase (reduction of sulfur chains), a Sulfide Quinone Oxidoreductase (SQR, oxidation of H2S) and a Sulfur Oxygenase Reductase (SOR, simultaneous oxidation and reduction of sulfur chains) have been characterized in this bacterium. It has also been shown that some of these enzymes are organized in membrane-bound supercomplexes.We have demonstrated that Aq_477, previously characterized as a sulfurtransferase belonging to the rhodanese superfamily, can load long sulfur chains and acts as a sulfur donor for its partners (sulfur reductase and SOR) which use these sulfur chains as substrate, thus optimizing the metabolism. These results show that Aq_477, renamed SbdP for Sulfur -binding -donating Protein, is involved in the sulfur energy metabolism of Aquifex aeolicus. The identification in the genome of some new proteins potentially involved in this metabolism permitted us to propose a new model which suggests a recycling of sulfur compounds between different enzymatic systems. We also looked for an organization level of respiratory complexes higher than…

Advisors/Committee Members: Giudici-Orticoni, Marie-Thérèse (thesis director).

Subjects/Keywords: Métabolisme énergétique du soufre; Transfert de soufre; Enzymes membranaires respiratoires; Aquifex aeolicus; Rhodanèse; Sulfur energy metabolism; Sulfur transfer; Respiratory enzymes; Aquifex aeolicus; Rhodanese

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Aussignargues, C. (2012). Optimisation du métabolisme énergétique du soufre chez la bactérie hyperthermophile Aquifex aeolicus. : Prediction of the compliance of packaging materials using deformulation methods and partition coefficients modelling. (Doctoral Dissertation). Aix Marseille Université. Retrieved from http://www.theses.fr/2012AIXM4709

Chicago Manual of Style (16^th Edition):

Aussignargues, Clement. “Optimisation du métabolisme énergétique du soufre chez la bactérie hyperthermophile Aquifex aeolicus. : Prediction of the compliance of packaging materials using deformulation methods and partition coefficients modelling.” 2012. Doctoral Dissertation, Aix Marseille Université. Accessed January 24, 2021. http://www.theses.fr/2012AIXM4709.

MLA Handbook (7^th Edition):

Aussignargues, Clement. “Optimisation du métabolisme énergétique du soufre chez la bactérie hyperthermophile Aquifex aeolicus. : Prediction of the compliance of packaging materials using deformulation methods and partition coefficients modelling.” 2012. Web. 24 Jan 2021.

Vancouver:

Aussignargues C. Optimisation du métabolisme énergétique du soufre chez la bactérie hyperthermophile Aquifex aeolicus. : Prediction of the compliance of packaging materials using deformulation methods and partition coefficients modelling. [Internet] [Doctoral dissertation]. Aix Marseille Université 2012. [cited 2021 Jan 24]. Available from: http://www.theses.fr/2012AIXM4709.

Council of Science Editors:

Aussignargues C. Optimisation du métabolisme énergétique du soufre chez la bactérie hyperthermophile Aquifex aeolicus. : Prediction of the compliance of packaging materials using deformulation methods and partition coefficients modelling. [Doctoral Dissertation]. Aix Marseille Université 2012. Available from: http://www.theses.fr/2012AIXM4709

University of Texas – Austin

12. Luo, Liming, 1967-. Genetic mapping of nuclear suppressors of splicing-deficient chloroplast introns, and a novel rhodanese-domain protein required for chloroplast translation in Chlamydomonas.

Degree: PhD, Plant Biology, 2010, University of Texas – Austin

URL: http://hdl.handle.net/2152/ETD-UT-2010-12-2200

► Although many group I (GI) introns can self-splice in vitro, their splicing is promoted by proteins in vivo. Only a few splicing factors that specifically… (more)

▼ Although many group I (GI) introns can self-splice in vitro, their splicing is promoted by proteins in vivo. Only a few splicing factors that specifically promote GI intron splicing have been identified, however, none are from chloroplasts, which is the subject of this study. In previous work from our lab, a strategy was developed to identify splicing factors for chloroplast GI introns of Chlamydomonas by using suppressor genetics. A mutant with reduced splicing of the chloroplast 23S rRNA intron (Cr.LSU) was generated. Then, 3 nuclear suppressors (7120, 71N1 and 7151) with substantially restored splicing of Cr.LSU were isolated and partially characterized. However, the suppressor gene(s) were not identified. In this study, I have used genetic mapping to make a renewed attempt to isolate these genes. Using polymorphisms between the 137C strain that was used for suppressor isolation, and a new strain of C.reinhardtii (S1D2), the nuclear suppressor mutations in 7120 and 71N1 were mapped to a region on chromosome III that is essentially devoid of recombination. Based on the recombination maps, the suppressor gene in 7120 is located within a ~418-kb region from bp 2,473,064 to 2,891,232, whereas the suppressor in 71N1 is likely located within a ~236-kb subregion from bp 2,473,064 to 2,709,377. It is possible that these mutations are in the same gene; however, the maps could not be refined further due to the lack of recombination in this 418-kb region. I also attempted to compare the genomic sequence of the 7120 suppressor, which was obtained by next-generation sequencing, with the Chlamydomonas reference genome (JGI, v.4). Next-generation sequencing of 7120 revealed the existence of abundant repetitive sequences and transposable elements clustered in a ~40-kb subregion of the recombinationally suppressed 418-kb region on chromosome III. I suggest that the high frequency of repetitive sequences and transposable elements in this region may be the reason for the suppressed recombination. Searching for candidate genes in the mapped region led me to examine a novel protein that was predicted to have a putative chloroplast transit-peptide, and an RNA binding domain. Further bioinformatic analysis revealed a single rhodanese domain with an active-site cysteine. The protein was expressed in E.coli as the full-length and predicted mature forms, plus a small His-tag. The purified mature protein had rhodanese catalytic activity, based on the fact that it was able to transfer sulfur from thiosulfate to cyanide. Also, western blot analysis with a polyclonal antibody produced in rabbits showed that the cellular protein migrated on SDS gels close to the mature protein and faster than the full-length protein, indicative of an organelle-targeted protein. The antibody also showed that the cellular protein co-fractionated with chloroplasts. To gain insight into its in vivo function, the gene was knocked down using the tandem RNAi system (Rohr et al., 2004), which produced strains (5) with reductions of 31% to 76% in the mRNA level, and… Advisors/Committee Members: Herrin, David L. (advisor), Roux, Stan J. (committee member), La Claire, John (committee member), Jansen, Robert K. (committee member), Browning, Karen (committee member).

Subjects/Keywords: RNA splicing; Genetic mapping; Rhodanese, chloroplast; Chlamydomonas; Splicing factors; Suppressor genes; Chloroplast

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Luo, Liming, 1. (2010). Genetic mapping of nuclear suppressors of splicing-deficient chloroplast introns, and a novel rhodanese-domain protein required for chloroplast translation in Chlamydomonas. (Doctoral Dissertation). University of Texas – Austin. Retrieved from http://hdl.handle.net/2152/ETD-UT-2010-12-2200

Chicago Manual of Style (16^th Edition):

Luo, Liming, 1967-. “Genetic mapping of nuclear suppressors of splicing-deficient chloroplast introns, and a novel rhodanese-domain protein required for chloroplast translation in Chlamydomonas.” 2010. Doctoral Dissertation, University of Texas – Austin. Accessed January 24, 2021. http://hdl.handle.net/2152/ETD-UT-2010-12-2200.

MLA Handbook (7^th Edition):

Luo, Liming, 1967-. “Genetic mapping of nuclear suppressors of splicing-deficient chloroplast introns, and a novel rhodanese-domain protein required for chloroplast translation in Chlamydomonas.” 2010. Web. 24 Jan 2021.

Vancouver:

Luo, Liming 1. Genetic mapping of nuclear suppressors of splicing-deficient chloroplast introns, and a novel rhodanese-domain protein required for chloroplast translation in Chlamydomonas. [Internet] [Doctoral dissertation]. University of Texas – Austin; 2010. [cited 2021 Jan 24]. Available from: http://hdl.handle.net/2152/ETD-UT-2010-12-2200.

Council of Science Editors:

Luo, Liming 1. Genetic mapping of nuclear suppressors of splicing-deficient chloroplast introns, and a novel rhodanese-domain protein required for chloroplast translation in Chlamydomonas. [Doctoral Dissertation]. University of Texas – Austin; 2010. Available from: http://hdl.handle.net/2152/ETD-UT-2010-12-2200

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