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Title: Global Lysine Acetylation in Escherichia coli Results from Growth Conditions That Favor Acetate Fermentation

Journal Article · · Journal of Bacteriology
 [1];  [2]; ORCiD logo [3];  [2];  [4];  [3];  [4]
  1. Buck Inst. for Research on Aging, Novato, CA (United States); DOE/OSTI
  2. Buck Inst. for Research on Aging, Novato, CA (United States)
  3. Loyola Univ. Chicago, Maywood, IL (United States)
  4. Univ. of Illinois at Urbana-Champaign, IL (United States)
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Lysine acetylation is thought to provide a mechanism for regulating metabolism in diverse bacteria. Indeed, many studies have shown that the majority of enzymes involved in central metabolism are acetylated and that acetylation can alter enzyme activity. However, the details regarding this regulatory mechanism are still unclear, specifically with regard to the signals that induce lysine acetylation. To better understand this global regulatory mechanism, we profiled changes in lysine acetylation during growth of Escherichia coli on the hexose glucose or the pentose xylose at both high and low sugar concentrations using label-free mass spectrometry. The goal was to see whether lysine acetylation differed during growth on these two different sugars. No significant differences, however, were observed. Rather, the initial sugar concentration was the principal factor governing changes in lysine acetylation, with higher sugar concentrations causing more acetylation. These results suggest that acetylation does not target specific metabolic pathways but rather simply targets accessible lysines, which may or may not alter enzyme activity. They further suggest that lysine acetylation principally results from conditions that favor accumulation of acetyl phosphate, the principal acetate donor in E. coli.

Research Organization:
Univ. of Illinois at Urbana-Champaign, IL (United States)
Sponsoring Organization:
USDOE Office of Science (SC)
Grant/Contract Number:
SC0012443
OSTI ID:
1611803
Journal Information:
Journal of Bacteriology, Journal Name: Journal of Bacteriology Journal Issue: 9 Vol. 201; ISSN 0021-9193
Publisher:
American Society for MicrobiologyCopyright Statement
Country of Publication:
United States
Language:
English

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Cited By (5)

Mechanisms, Detection, and Relevance of Protein Acetylation in Prokaryotes journal April 2019
Post-translational Protein Acetylation: An Elegant Mechanism for Bacteria to Dynamically Regulate Metabolic Functions journal July 2019
The Impact of ackA, pta, and ackA-pta Mutations on Growth, Gene Expression and Protein Acetylation in Escherichia coli K-12 journal February 2020
Mechanisms, Detection, and Relevance of Protein Acetylation in Prokaryotes journal April 2019
Post-translational Protein Acetylation: An Elegant Mechanism for Bacteria to Dynamically Regulate Metabolic Functions journal July 2019

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59 BASIC BIOLOGICAL SCIENCES
Escherichia coli
Microbiology
acetyl phosphate
acetylation
acetylome
fermentation
mass spectrometry