PgmNr Y3011: The role of protein acetylation in stress defense.

Authors:
Jeffrey Lewis 1 ; Rebecca Sides 1 ; Aaron Storey 2 ; Alan Tackett 2


Institutes
1) University of Arkansas, Fayetteville, AR; 2) University of Arkansas for Medical Sciences, Little Rock, AR.


Keyword: Cell Cycle/Growth Control/Metabolism

Abstract:

Cells face a staggering array of environmental challenges during their lifetimes. Not surprisingly, cells have evolved sophisticated rapid-response mechanisms to deal with acute environmental changes. Our focus has been on post-translational lysine acetylation, which was originally discovered as a histone modification over fifty years ago. Recent proteomic studies have identified thousands of acetylated proteins in diverse organisms, rivaling phosphorylation in terms of number of targets. While the sheer size of the “acetylome” points to its importance, we have little idea how acetylation affects protein function for the vast majority of targets. The striking enrichment of stress defense proteins as acetylation targets suggested an underappreciated role for protein acetylation in stress defense. We now provide evidence that protein acetylation plays a key role in stress defense. First, we have identified a post-translational mechanism for thermotolerance that requires properly coordinated protein acetylation. Second, through quantitative proteomics we observe extensive acetylome remodeling during acute heat stress. Intriguingly, we find increased acetylation of choline kinase (Cki1p) during heat shock, which in turn regulates Cki1p activity. Because Cki1p plays a known role in cell membrane turnover, this provides an exciting new link between protein acetylation and cell membrane metabolism during heat stress.



Yeast Database Genetic Index
1. gene symbol: CKI1; systematic name: YLR133W