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.
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U2 - 10.1074/mcp.M800187-MCP200
DO - 10.1074/mcp.M800187-MCP200
M3 - Article
C2 - 18723842
AN - SCOPUS:61649089277
SN - 1535-9476
VL - 8
SP - 215
EP - 225
JO - Molecular and Cellular Proteomics
JF - Molecular and Cellular Proteomics
IS - 2
ER -