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You searched for subject:(proteolytic maturation). Showing records 1 – 3 of 3 total matches.

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Cornell University

1. Rowland, Elden Ernest. PROTEOLYTIC MATURATION AND PROTEIN DEGRADATION IN ARABIDOPSIS THALIANA CHLOROPLASTS.

Degree: PhD, Plant Biology, 2017, Cornell University

Proteolysis is crucial for the maturation, regulation and recycling of the chloroplast proteome. Although several dozen chloroplast proteases are known, information concerning their substrates and functions is limited. In particular, little is known about the structural features of substrates that trigger their proteolysis. Most chloroplast proteins are nuclear encoded and are targeted through an N-terminal chloroplast transit peptide (cTP) that is removed by stromal processing peptidase (SPP). To better understand proteolytic maturation, the soluble N-terminal proteome of the Arabidopsis thaliana chloroplast was characterized. A cTP cleavage motif was observed that suggests other peptidases, in addition to SPP, are involved in chloroplast protein maturation. There was a clear preference for small uncharged amino acids at the processed protein N-terminus suggesting the existence of a chloroplast specific ‘N-end rule’. The soluble chloroplast peptidases PREP and OOP have been shown to degrade small polypeptides in vitro and are thought to be responsible for removal of cTP fragments and other degradation products. The CLP protease system can degrade intact protein substrates with the aid of ATP dependent (AAA+) CLPC chaperones that unfold and feed substrates into the CLP proteolytic core. An array of proteomic tools were used to compare Arabidopsis mutants deficient in the above peptidases with wild type. Degradation products, including cTPs, were found to accumulate in peptidase mutants indicative, of rate-limited or blocked degradation pathways. Incomplete or altered N-terminal maturation for chloroplast proteins was dependent on the type and severity of the peptidase deficiency. These results provide molecular details to help explain dwarf, chlorotic mutant phenotypes and demonstrate the interplay between protein import, proteolytic processing and the downstream degradation of damaged or unwanted proteins in the chloroplast. Substrate and sequence cleavage specificity was determined for soluble chloroplast glutamyl-endopeptidase (CGEP) and the plastoglobule localized metallopeptidase PGM48. Structural models were used to predict peptidase substrate binding mechanisms. Advisors/Committee Members: Van Wijk, Klaas (chair), Hanson, Maureen R. (committee member), Owens, Thomas G. (committee member), Cilia, Michelle (committee member).

Subjects/Keywords: Plant sciences; Biochemistry; Arabidopsis; chloroplast; N-terminal proteome; protease; proteolytic degradation; proteolytic maturation

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

APA (6th Edition):

Rowland, E. E. (2017). PROTEOLYTIC MATURATION AND PROTEIN DEGRADATION IN ARABIDOPSIS THALIANA CHLOROPLASTS. (Doctoral Dissertation). Cornell University. Retrieved from http://hdl.handle.net/1813/58987

Chicago Manual of Style (16th Edition):

Rowland, Elden Ernest. “PROTEOLYTIC MATURATION AND PROTEIN DEGRADATION IN ARABIDOPSIS THALIANA CHLOROPLASTS.” 2017. Doctoral Dissertation, Cornell University. Accessed November 29, 2020. http://hdl.handle.net/1813/58987.

MLA Handbook (7th Edition):

Rowland, Elden Ernest. “PROTEOLYTIC MATURATION AND PROTEIN DEGRADATION IN ARABIDOPSIS THALIANA CHLOROPLASTS.” 2017. Web. 29 Nov 2020.

Vancouver:

Rowland EE. PROTEOLYTIC MATURATION AND PROTEIN DEGRADATION IN ARABIDOPSIS THALIANA CHLOROPLASTS. [Internet] [Doctoral dissertation]. Cornell University; 2017. [cited 2020 Nov 29]. Available from: http://hdl.handle.net/1813/58987.

Council of Science Editors:

Rowland EE. PROTEOLYTIC MATURATION AND PROTEIN DEGRADATION IN ARABIDOPSIS THALIANA CHLOROPLASTS. [Doctoral Dissertation]. Cornell University; 2017. Available from: http://hdl.handle.net/1813/58987

2. Demoures, Béatrice. Maturation protéolytique par les proprotéines convertases (PCs) dans l'angiogenèse, l'oncogenèse et l'infection virale : identification et étude de deux substrats des PCs : Proteolytic maturation by Proprotein Convertases (PCs) in angiogenesis, oncogenesis and viral infection : iIdentification and study of two PCs substrates.

Degree: Docteur es, Biologie Cellulaire et Physiopathologie, 2016, Bordeaux

Les proprotéines convertases (PCs) sont des enzymes impliquées de nombreux processus pathologiques. Nous avons étudié deux substrats des PCs: l'apeline et la glycoprotéine B (gB) du virus d'Epstein Barr (EBV), et le rôle de cette maturation protéolytique dans la médiation de leurs fonctions. L'apeline est surexprimée dans plusieurs cancers dont le cancer colorectal (CCR), et nous avons montré que la furine, un membre des PCs, clive l’apeline. Pour déterminer le rôle de ce clivage dans le CCR métastatique, nous avons généré un mutant non clivable (apeline-DM). In vitro, ce mutant inhibe la croissance de cellules cancéreuses du côlonet ne les protège pas de l'apoptose, contrairement à l'apeline sauvage. In vivo, l'apeline-DM diminue drastiquement la croissance tumorale et la formation de métastases hépatiques chez la souris. Les mêmes résultats sont obtenus dans des modèles de souris déficientes pour l’apeline, démontrant l'intérêt d'utiliser l'apeline-DM ou des dérivés comme potentiels agents anticancéreux dans le traitement des CCR métastatiques. La gB du virus EBV, virus impliqué dans certains cancers lymphoïdes et épithéliaux chez l'homme, permet l'entrée du virus dans la cellule lors de l'infection. Nous avons montré que les PCs, et notamment la furine, clivent la gB. In vitro, l'induction de la protéine virale LMP1 augmente l'expression de la furine, qui se traduit par une augmentation de l'infection par EBV. Ces résultats suggèrent l'existence d'une boucle de régulation entre la furine et LMP1 permettant d'améliorer la propagation cellulaire du virus. L'utilisation d'inhibiteurs de l'activité des PCs permettrait donc de bloquer l'infection par EBV.

Proprotein convertases (PCs) are enzymes involved in many pathological processes. We have identified two novel substrates of the PCs: apelin and glycoprotein B (gB) of Epstein Barr Virus (EBV), and studied the role of PC-mediated proteolytic maturation in their functions. Apelin is overexpressed in some cancers including colorectal cancer (CRC), and we demonstrated that furin, one of the PCs member, cleaves apelin in two peptides. To determine the role of apelin cleavage by furin in the metastatic CRC, we generated a non-cleavable mutant (apelin-DM). This mutant inhibited the growth of colon cancer cells in vitro and could not protect against apoptosis, unlike the wild-type apelin. In vivo, apelin-DM drastically reduces tumor growth and the formation of hepatic metastases in mice. These results were confirmed in apelin deficient mouse models thus demonstrating the potential interest of using apelin-DM, or its derivatives, as anticancer agents in the treatment of metastatic CRC. The gB of EBV, a virus involved in some lymphoid and epithelial cancers in humans, is involved in the entry of the virus into the cell during infection. We have shown that PCs, especially furin, cleave gB. In vitro,induction of the LMP1 viral protein increases furin expression, which results in an increase in EBV infection. These results suggest the existence of a regulatory loop between…

Advisors/Committee Members: Khatib, Abdel-Majid (thesis director).

Subjects/Keywords: Apeline; Cancer colorectal; Epstein-Barr Virus; GlycoprotéineB; Maturation protéolytique; Métastases; Proprotéines convertases; Apelin; Colorectal cancer; Epstein-Barr Virus; Glycoprotein B; Proteolytic maturation; Metastases; Proprotein convertases

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

APA (6th Edition):

Demoures, B. (2016). Maturation protéolytique par les proprotéines convertases (PCs) dans l'angiogenèse, l'oncogenèse et l'infection virale : identification et étude de deux substrats des PCs : Proteolytic maturation by Proprotein Convertases (PCs) in angiogenesis, oncogenesis and viral infection : iIdentification and study of two PCs substrates. (Doctoral Dissertation). Bordeaux. Retrieved from http://www.theses.fr/2016BORD0446

Chicago Manual of Style (16th Edition):

Demoures, Béatrice. “Maturation protéolytique par les proprotéines convertases (PCs) dans l'angiogenèse, l'oncogenèse et l'infection virale : identification et étude de deux substrats des PCs : Proteolytic maturation by Proprotein Convertases (PCs) in angiogenesis, oncogenesis and viral infection : iIdentification and study of two PCs substrates.” 2016. Doctoral Dissertation, Bordeaux. Accessed November 29, 2020. http://www.theses.fr/2016BORD0446.

MLA Handbook (7th Edition):

Demoures, Béatrice. “Maturation protéolytique par les proprotéines convertases (PCs) dans l'angiogenèse, l'oncogenèse et l'infection virale : identification et étude de deux substrats des PCs : Proteolytic maturation by Proprotein Convertases (PCs) in angiogenesis, oncogenesis and viral infection : iIdentification and study of two PCs substrates.” 2016. Web. 29 Nov 2020.

Vancouver:

Demoures B. Maturation protéolytique par les proprotéines convertases (PCs) dans l'angiogenèse, l'oncogenèse et l'infection virale : identification et étude de deux substrats des PCs : Proteolytic maturation by Proprotein Convertases (PCs) in angiogenesis, oncogenesis and viral infection : iIdentification and study of two PCs substrates. [Internet] [Doctoral dissertation]. Bordeaux; 2016. [cited 2020 Nov 29]. Available from: http://www.theses.fr/2016BORD0446.

Council of Science Editors:

Demoures B. Maturation protéolytique par les proprotéines convertases (PCs) dans l'angiogenèse, l'oncogenèse et l'infection virale : identification et étude de deux substrats des PCs : Proteolytic maturation by Proprotein Convertases (PCs) in angiogenesis, oncogenesis and viral infection : iIdentification and study of two PCs substrates. [Doctoral Dissertation]. Bordeaux; 2016. Available from: http://www.theses.fr/2016BORD0446

3. Mailler, Élodie. Structural rearrangements of the HIV-1 genomic RNA during maturation of the viral particle : Etude des remaniements structuraux de l'ARN génomique du VIH-1 lors de la maturation des particules virales.

Degree: Docteur es, Aspects moléculaires et cellulaires de la biologie, 2017, Université de Strasbourg

Le VIH-1 bourgeonne sous forme immature et doit subir l’étape de maturation afin d’acquérir son caractère infectieux. La maturation protéolytique du précurseur Pr55Gag induit le réarrangement morphologique de la particule alors que le dimère d’ARNg acquiert une compaction optimale. Ces réarrangements conformationnels restent encore inconnus et sont facilités par l’activité chaperonne de la protéine NCp7. Notre but a été de déterminer les différentes étapes menant à l’obtention d’un dimère d’ARNg mature. Nous avons donc étudié la structure des 550 premiers nucléotides du génome par cartographie chimique, à la fois 1. in vitro en présence des protéines Pr55Gag, GagΔp6, intermédiaires contenant le domaine NC et NCp7 et 2. in viro par l’approche hSHAPE-Seq que nous avons développé. Les particules matures et bloquées aux différentes étapes de maturation de Pr55Gag ont été analysées ainsi que des particules matures et totalement immatures traitées avec l’éjecteur de zinc AT-2. Ce traitement permet d’identifier les sites de protection de Pr55Gag et NCp7 ainsi que leur activité déstabilisatrice.

The HIV-1 particle buds from the infected cell as an immature particle and has to undergo a maturation process to become infectious. Proteolytic processing of Pr55Gag triggers morphological rearrangements of the particle whereas the gRNA dimer becomes more stable. Genomic rearrangements remain poorly understood and are facilitated by the RNA chaperone activity of the NCp7 protein. Our goal was to determining the different steps leading to the formation of the mature dimeric gRNA. To this end, the structure of the first 550 nucleotides of the HIV-1 genome was assessed by chemical probing 1. in vitro with Pr55Gag, GagΔp6, NC-containing intermediates and NCp7 proteins and 2. in viro with the hSHAPE-Seq approach we developed. Wild type and mutant viruses mimicking the sequential processing of Pr55Gag were analysed, as well as immature PR- and mature particles treated with the AT-2 zinc ejector, in order to identify the Pr55Gag and NCp7 binding sites and their gRNA destabilising activity.

Advisors/Committee Members: Marquet, Roland (thesis director), Vivet-Boudou, Valérie (thesis director).

Subjects/Keywords: VIH-1; Maturation protéique; Maturation génomique; Cartographie chimique de l’ARN; Séquençage à haut débit; Structure secondaire de l’ARN; Activité chaperonne de l’ARN; HIV-1; Proteolytic processing; Genomic maturation; RNA chemical probing; High-throughput sequencing; RNA secondary structure; RNA chaperone activity; 572.8; 616.97

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

APA (6th Edition):

Mailler, E. (2017). Structural rearrangements of the HIV-1 genomic RNA during maturation of the viral particle : Etude des remaniements structuraux de l'ARN génomique du VIH-1 lors de la maturation des particules virales. (Doctoral Dissertation). Université de Strasbourg. Retrieved from http://www.theses.fr/2017STRAJ055

Chicago Manual of Style (16th Edition):

Mailler, Élodie. “Structural rearrangements of the HIV-1 genomic RNA during maturation of the viral particle : Etude des remaniements structuraux de l'ARN génomique du VIH-1 lors de la maturation des particules virales.” 2017. Doctoral Dissertation, Université de Strasbourg. Accessed November 29, 2020. http://www.theses.fr/2017STRAJ055.

MLA Handbook (7th Edition):

Mailler, Élodie. “Structural rearrangements of the HIV-1 genomic RNA during maturation of the viral particle : Etude des remaniements structuraux de l'ARN génomique du VIH-1 lors de la maturation des particules virales.” 2017. Web. 29 Nov 2020.

Vancouver:

Mailler E. Structural rearrangements of the HIV-1 genomic RNA during maturation of the viral particle : Etude des remaniements structuraux de l'ARN génomique du VIH-1 lors de la maturation des particules virales. [Internet] [Doctoral dissertation]. Université de Strasbourg; 2017. [cited 2020 Nov 29]. Available from: http://www.theses.fr/2017STRAJ055.

Council of Science Editors:

Mailler E. Structural rearrangements of the HIV-1 genomic RNA during maturation of the viral particle : Etude des remaniements structuraux de l'ARN génomique du VIH-1 lors de la maturation des particules virales. [Doctoral Dissertation]. Université de Strasbourg; 2017. Available from: http://www.theses.fr/2017STRAJ055

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