Advanced search options

Advanced Search Options 🞨

Browse by author name (“Author name starts with…”).

Find ETDs with:

in
/  
in
/  
in
/  
in

Written in Published in Earliest date Latest date

Sorted by

Results per page:

Sorted by: relevance · author · university · dateNew search

Dates: Last 2 Years

You searched for +publisher:"Cornell University" +contributor:("Hanson, Maureen R"). Showing records 1 – 2 of 2 total matches.

Search Limiters

Last 2 Years | English Only

No search limiters apply to these results.

▼ Search Limiters


Cornell University

1. Hines, Kevin Matthew. THE ROLE OF CHLOROPLAST CARBONIC ANHYDRASES IN THE DEVELOPMENT OF C3 PHOTOSYNTHESIZING PLANTS.

Degree: PhD, Biochemistry, Molecular and Cell Biology, 2019, Cornell University

Carbonic anhydrase (CA, EC: 4.2.1.1) is a zinc-bond metalloenzyme that rapidly catalyzes the reversable hydration between carbon dioxide and water with bicarbonate. C3 photosynthesizing plants contain very highly expressed CAs in their chloroplasts, which can represent over 2% of all soluble protein. However, no single role has been assigned to CA and its activity in the stroma, although they are proposed to have a myriad of duties, from oxidative stress tolerance and plant defense to macromolecule biosynthesis and pH buffering. Previous research exploring the function of chloroplast CA have focused largely on deactivating or deleting βCA1, the most highly expressed CA and the first to be identified in the chloroplast. However, no study has completely removed all CA enzymes from the chloroplast stroma and observed the effects. Using the model Nicotiana tabacum (tobacco), I identified two stromal CAs, βCA1 and βCA5, and produced CRISPR/Cas9 mutants targeting both genes. While the single knockout lines Δβca1 and Δβca5 had no striking phenotypic differences compared to WT plants, Δβca1ca5 leaves developed large necrotic lesions. Leaf development of Δβca1ca5 plants normalized at the high CO2 concentration of 9000ppm. High CO2-grown Δβca1ca5 mutants had no measurable defect in photosynthetic capacity when measured at ambient CO2 Δβca1ca5 seedling germination and development is negatively affected when seedling development occurs at ambient CO2. A series of complementation experiments using altered forms of βCA1 were carried out in Δβca1ca5 plants. Constructs expressing full length βCA1 and βCA5 proteins complemented the Δβca1ca5 mutation, but inactivated (ΔZn-βCA1) and cytoplasm-localized (Δ62-βCA1) forms of βCA1 failed to reverse the mutant phenotype. When infected with tobacco mosaic virus (TMV) Δβca1 and Δβca1ca5 tobacco failed to show the hypersensitive response (HR), while expression of ΔZn-βCA1 restored the response. Thus, stromal CAs play major roles in plant development and defense. Advisors/Committee Members: Hanson, Maureen R. (chair), Owens, Thomas (committee member), van Wijk, Klaas (committee member).

Subjects/Keywords: Carbonic anhydrase; Chloroplast; CRISPR; Nicotiana; Photosynthesis; Plant Development

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

APA (6th Edition):

Hines, K. M. (2019). THE ROLE OF CHLOROPLAST CARBONIC ANHYDRASES IN THE DEVELOPMENT OF C3 PHOTOSYNTHESIZING PLANTS. (Doctoral Dissertation). Cornell University. Retrieved from http://hdl.handle.net/1813/70137

Chicago Manual of Style (16th Edition):

Hines, Kevin Matthew. “THE ROLE OF CHLOROPLAST CARBONIC ANHYDRASES IN THE DEVELOPMENT OF C3 PHOTOSYNTHESIZING PLANTS.” 2019. Doctoral Dissertation, Cornell University. Accessed December 05, 2020. http://hdl.handle.net/1813/70137.

MLA Handbook (7th Edition):

Hines, Kevin Matthew. “THE ROLE OF CHLOROPLAST CARBONIC ANHYDRASES IN THE DEVELOPMENT OF C3 PHOTOSYNTHESIZING PLANTS.” 2019. Web. 05 Dec 2020.

Vancouver:

Hines KM. THE ROLE OF CHLOROPLAST CARBONIC ANHYDRASES IN THE DEVELOPMENT OF C3 PHOTOSYNTHESIZING PLANTS. [Internet] [Doctoral dissertation]. Cornell University; 2019. [cited 2020 Dec 05]. Available from: http://hdl.handle.net/1813/70137.

Council of Science Editors:

Hines KM. THE ROLE OF CHLOROPLAST CARBONIC ANHYDRASES IN THE DEVELOPMENT OF C3 PHOTOSYNTHESIZING PLANTS. [Doctoral Dissertation]. Cornell University; 2019. Available from: http://hdl.handle.net/1813/70137

2. Liao, Juiyun. SUBSTRATES, STRUCTURES, AND FUNCTIONS OF THE CHLOROPLAST CLP PROTEASE SYSTEM IN ARABIDOPSIS THALIANA.

Degree: PhD, Plant Biology, 2019, Cornell University

The caseinolytic proteolytic machinery (CLP) is an essential and abundant protease of the chloroplast protease network. It is composed of multiple components (a proteolytic core CLPP/R/T, chaperones CLPC1/C2/D, and adaptors CLPS1/F). Mostly based on functional and structural information from bacterial Clp systems, it is postulated that these chloroplast CLP chaperones are aided by the CLP adaptors to select and deliver substrates to the proteolytic chamber (protease core) for degradation. The chloroplast CLPPRT proteolytic core is different and far more complex than the bacterial or mitochondria Clp core. The chloroplast CLP core is a hetero-oligomeric tetradecamer that is associated with additional accessory proteins unique to higher plants. Furthermore, the chloroplast CLPP and CLPR subunits have C-terminal extensions with unknown functions. It is unclear why chloroplast CLP core shows such high complexity and how these different CLP subunits contribute to the proteolytic system. Finally, relatively few chloroplast CLP substrates have been identified. To better understand the chloroplast CLP protease system, I applied an in vivo trapping approach for substrate identification and crosslinking (XL) mass spectrometry (MS) for investigation of the proximity and possible protein-protein interactions between these CLP components. Functional complementation showed that CLPP5 is crucial for CLP catalysis, whereas CLPP3 plays an essential role in CLP structure but its catalytic activity is dispensable. However, in vivo trapping using CLPPRT complexes with a reduced number of catalytic triads through the presence of one or more catalytically inactivated CLPP3/5 subunits did not identify proteins trapped in these CLPPRT complexes. This suggests that reduced proteolytic capacity within CLP cores does not result in a bottleneck for protein degradation in vivo. XL-MS of affinity-purified CLP core complexes or affinity purified CLPC-TRAP complexes identified several putative domains and motifs involved in the CLP protein-protein interactions. The newly established workflow of in vitro DSSO crosslinking using plant proteins paves the way for a more detailed exploration of the 3D structure and possible regulation of the chloroplast CLP machinery. Advisors/Committee Members: Van Wijk, Klaas (chair), Hanson, Maureen R. (committee member), Qian, Shu-Bing (committee member).

Subjects/Keywords: CLP; subtrate; trapping; Proteolysis; Biochemistry; Botany; protease; Plant sciences

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

APA (6th Edition):

Liao, J. (2019). SUBSTRATES, STRUCTURES, AND FUNCTIONS OF THE CHLOROPLAST CLP PROTEASE SYSTEM IN ARABIDOPSIS THALIANA. (Doctoral Dissertation). Cornell University. Retrieved from http://hdl.handle.net/1813/67299

Chicago Manual of Style (16th Edition):

Liao, Juiyun. “SUBSTRATES, STRUCTURES, AND FUNCTIONS OF THE CHLOROPLAST CLP PROTEASE SYSTEM IN ARABIDOPSIS THALIANA.” 2019. Doctoral Dissertation, Cornell University. Accessed December 05, 2020. http://hdl.handle.net/1813/67299.

MLA Handbook (7th Edition):

Liao, Juiyun. “SUBSTRATES, STRUCTURES, AND FUNCTIONS OF THE CHLOROPLAST CLP PROTEASE SYSTEM IN ARABIDOPSIS THALIANA.” 2019. Web. 05 Dec 2020.

Vancouver:

Liao J. SUBSTRATES, STRUCTURES, AND FUNCTIONS OF THE CHLOROPLAST CLP PROTEASE SYSTEM IN ARABIDOPSIS THALIANA. [Internet] [Doctoral dissertation]. Cornell University; 2019. [cited 2020 Dec 05]. Available from: http://hdl.handle.net/1813/67299.

Council of Science Editors:

Liao J. SUBSTRATES, STRUCTURES, AND FUNCTIONS OF THE CHLOROPLAST CLP PROTEASE SYSTEM IN ARABIDOPSIS THALIANA. [Doctoral Dissertation]. Cornell University; 2019. Available from: http://hdl.handle.net/1813/67299

.