Investigation of biological roles of protein kinetic stability in extremophiles
Authors
Sen, Jayeeta
ORCID
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Other Contributors
Colón, Wilfredo
Barquera, Blanca L.
Linhardt, Robert J.
Bystroff, Christopher, 1960-
Barquera, Blanca L.
Linhardt, Robert J.
Bystroff, Christopher, 1960-
Issue Date
2018-05
Keywords
Chemistry
Degree
PhD
Terms of Use
This electronic version is a licensed copy owned by Rensselaer Polytechnic Institute, Troy, NY. Copyright of original work retained by author.
Full Citation
Abstract
For a more comprehensive analysis, and contrast with a mesophilic organism, the KSPs identified from the extremophiles were compared to the 50 KSPs previously identified from E. coli. Interestingly, only four of the 180 KSPs overlapped in all the three organisms. These proteins are involved in life-sustaining functions such as stress response (superoxide dismutase, thioredoxin reductase), translation (elongation factor thermo unstable) and metabolism (purine nucleoside phosphorylase), thus implying a potential role of kinetic stability in preserving or performing these protein functions. Under metabolism, which was the main biological pathway linked to the KSPs, carbohydrate metabolism was found to be the most common function among the KSPs of all organisms, while amino acid metabolism was more frequent in thermophiles than E. coli, putatively due to the nutrient-poor and hostile nature of their thermophilic environment. Overall, certain biological functions, particularly metabolism and stress response, appear to have a greater necessity for protein kinetic stability. The identification of hyperstable proteins in different organisms could be beneficial in fundamental research to understand mechanisms of defense and survival in extreme conditions, as well as in biotechnology applications.
Description
May 2018
School of Science
School of Science
Department
Dept. of Chemistry and Chemical Biology
Publisher
Rensselaer Polytechnic Institute, Troy, NY
Relationships
Rensselaer Theses and Dissertations Online Collection
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