Investigation of the kinetically stable sub-proteomes of Vibrio cholerae and Vibrio harveyi
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Authors
Church, Jennifer
Issue Date
2017-08
Type
Electronic thesis
Thesis
Thesis
Language
ENG
Keywords
Chemistry
Alternative Title
Abstract
The structural properties of the KSPs in Vibrio were similar to those of E. coli, suggesting a bias of KSPs towards topological complexity and oligomeric structures. Functional analysis revealed several outer membrane proteins (OMPs), oxidoreductases, metabolic enzymes and essential proteins involved in translation and transcription, suggesting biological roles for kinetic stability in cellular metabolism, essential processes and protection from environmental stress. Additionally, three KSPs – OmpU, OmpT and long-chain-fatty-acid-CoA ligase – were identified and traced back to the virulence pathways of V. cholerae, thereby also implicating kinetic stability in Vibrio bacteria virulence. This work strongly supports a link between topological complexity and oligomeric structure with kinetic stability, and advances the long-term goal of predicting kinetic stability from a protein’s three-dimensional structure. In addition, certain biological functions or pathways in bacteria seem to require kinetic stability, in particular those linked to stress response and virulence. Finally, the high overlap of KSPs in V. cholerae and E. coli suggest the abundance and type of KSPs present in bacteria may correlate with their ability to adapt and survive in harsher environments.
Description
August 2017
School of Science
School of Science
Full Citation
Publisher
Rensselaer Polytechnic Institute, Troy, NY