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Identification Of Proteins That Contribute To Yeast Heat Stress By Lysine Acetylation, Weijia Shi
Identification Of Proteins That Contribute To Yeast Heat Stress By Lysine Acetylation, Weijia Shi
Biological Sciences Undergraduate Honors Theses
Evidence is emerging that protein lysine acetylation may be a novel type of post-translational modification (PTM) contributing to the mechanisms of yeast heat stress responses. Proteomics studies including ours have identified over 1,000 acetylated proteins in the yeast proteomes that are composed of about 6,000 proteins. Our lab recently identified 596 proteins that underwent acetylation changes during heat shock by mass spectrometry. However, the role of lysine acetylation on specific residues of specific proteins in yeast thermotolerance remains largely unknown. This study selected 43 proteins from our lab’s previous work and examined their possible contributions to yeast heat stress responses. …
How Acetylation Regulates Metabolic Enzyme Function During Environmental Shifts, Jared Canonigo
How Acetylation Regulates Metabolic Enzyme Function During Environmental Shifts, Jared Canonigo
Biological Sciences Undergraduate Honors Theses
Organisms such as Saccharomyces cerevisiae can regulate the mechanisms of proteins through post-translational modification. These modifications play a vital role in functional proteomic activity because they can regulate protein activity, localization, and interaction with other cellular molecules. Such modifications include phosphorylation, methylation, and acetylation. The metabolic mechanisms of yeast became of keen interest to our lab because our lab noticed many stress defense proteins were being acetylated during stress heat shock. Notably, Adh1p and Adh2p showed both an increase and a decrease in acetylation at two lysine residues (K315 and K314) overtime during heat shock respectively, though the exact function …