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

Junmei Zhang, Robert Sprung, Jimin Pei, Xiaohong Tan, Sungchan Kim, Heng Zhu, Chuan Fa Liu, Nick V. Grishin, Ying Zhao

Research output: Contribution to journalArticle

322 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)215-225
Number of pages11
JournalMolecular and Cellular Proteomics
Volume8
Issue number2
DOIs
StatePublished - Feb 2009

Fingerprint

Acetylation
Escherichia coli
Lysine
Prokaryotic Cells
Proteins
Mammals
Escherichia coli Proteins
Physiology
Gene Expression Regulation
Enzymes
Gene expression
Energy Metabolism
Bacteria
Screening

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Analytical Chemistry

Cite this

Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli. / Zhang, Junmei; Sprung, Robert; Pei, Jimin; Tan, Xiaohong; Kim, Sungchan; Zhu, Heng; Liu, Chuan Fa; Grishin, Nick V.; Zhao, Ying.

In: Molecular and Cellular Proteomics, Vol. 8, No. 2, 02.2009, p. 215-225.

Research output: Contribution to journalArticle

Zhang, Junmei ; Sprung, Robert ; Pei, Jimin ; Tan, Xiaohong ; Kim, Sungchan ; Zhu, Heng ; Liu, Chuan Fa ; Grishin, Nick V. ; Zhao, Ying. / Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli. In: Molecular and Cellular Proteomics. 2009 ; Vol. 8, No. 2. pp. 215-225.
@article{4c5f3dc615474a2eafea23a64b6b8131,
title = "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli",
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.",
author = "Junmei Zhang and Robert Sprung and Jimin Pei and Xiaohong Tan and Sungchan Kim and Heng Zhu and Liu, {Chuan Fa} and Grishin, {Nick V.} and Ying Zhao",
year = "2009",
month = "2",
doi = "10.1074/mcp.M800187-MCP200",
language = "English (US)",
volume = "8",
pages = "215--225",
journal = "Molecular and Cellular Proteomics",
issn = "1535-9476",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "2",

}

TY - JOUR

T1 - Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli

AU - Zhang, Junmei

AU - Sprung, Robert

AU - Pei, Jimin

AU - Tan, Xiaohong

AU - Kim, Sungchan

AU - Zhu, Heng

AU - Liu, Chuan Fa

AU - Grishin, Nick V.

AU - Zhao, Ying

PY - 2009/2

Y1 - 2009/2

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=61649089277&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=61649089277&partnerID=8YFLogxK

U2 - 10.1074/mcp.M800187-MCP200

DO - 10.1074/mcp.M800187-MCP200

M3 - Article

C2 - 18723842

AN - SCOPUS:61649089277

VL - 8

SP - 215

EP - 225

JO - Molecular and Cellular Proteomics

JF - Molecular and Cellular Proteomics

SN - 1535-9476

IS - 2

ER -