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PMID: 18723842 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.

Molecular & cellular proteomics : MCP ·Vol. 8 ·No. 2 ·2009-02-00 ·Pages 215-25

Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y

Abstract

Lysine acetylation and its regulatory enzymes are known to have pivotal roles in mammalian cellular physiology. However, the extent and function of this modification in prokaryotic cells remain largely unexplored, thereby presenting a hurdle to further functional study of this modification in prokaryotic systems. Here we report the first global screening of lysine acetylation, identifying 138 modification sites in 91 proteins from Escherichia coli. None of the proteins has been previously associated with this modification. Among the identified proteins are transcriptional regulators, as well as others with diverse functions. Interestingly, more than 70% of the acetylated proteins are metabolic enzymes and translation regulators, suggesting an intimate link of this modification to energy metabolism. The new dataset suggests that lysine acetylation could be abundant in prokaryotic cells. In addition, these results also imply that functions of lysine acetylation beyond regulation of gene expression are evolutionarily conserved from bacteria to mammals. Furthermore, we demonstrate that bacterial lysine acetylation is regulated in response to stress stimuli.

MeSH Terms
Acetylation Amino Acid Motifs Animals Blotting, Western Citric Acid Cycle Computational Biology Conserved Sequence Escherichia coli/metabolism Escherichia coli Proteins/metabolism Evolution, Molecular Glycolysis Lysine/metabolism Protein Biosynthesis Protein Processing, Post-Translational Proteomics Stress, Physiological Substrate Specificity Transcription, Genetic
Chemicals
Escherichia coli Proteins Lysine
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Zhang Junmei
Department of Biochemistry, Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Sprung Robert
Pei Jimin
Tan Xiaohong
Kim Sungchan
Zhu Heng
Liu Chuan-Fa
Grishin Nick V
Zhao Yingming
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Article Info
Journal
Molecular & cellular proteomics : MCP
Abbr.
Mol Cell Proteomics
ISSN
1535-9484
Published
2009-02-00
Epub
2008-00-23
Pages
215-25
Language
English
Region
United States
NLM ID
101125647
PMCID
PMC2634580
Subset
IM
Grants
NCRR NIH HHS · U54 RR020839 · United States
NCRR NIH HHS · U45 RR020839 · United States
NCI NIH HHS · CA107943 · United States
NCI NIH HHS · R33 CA107943 · United States
NCI NIH HHS · R21 CA107943 · United States
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