Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli

Brian T Weinert; Vytautas Iesmantavicius; Sebastian A Wagner; Christian Schölz; Bertil Gummesson; Petra Beli; Thomas Nyström; Chuna Ram Choudhary

doi:10.1016/j.molcel.2013.06.003

Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli

Brian T Weinert, Vytautas Iesmantavicius, Sebastian A Wagner, Christian Schölz, Bertil Gummesson, Petra Beli, Thomas Nyström, Chuna Ram Choudhary

Novo Nordisk Foundation Center for Protein Research

252 Citations (Scopus)

Abstract

Lysine acetylation is a frequently occurring posttranslational modification in bacteria; however, little is known about its origin and regulation. Using the model bacterium Escherichia coli (E. coli), we found that most acetylation occurred at a low level and accumulated in growth-arrested cells in a manner that depended on the formation of acetyl-phosphate (AcP) through glycolysis. Mutant cells unable to produce AcP had significantly reduced acetylation levels, while mutant cells unable to convert AcP to acetate had significantly elevated acetylation levels. We showed that AcP can chemically acetylate lysine residues in vitro and that AcP levels are correlated with acetylation levels in vivo, suggesting that AcP may acetylate proteins nonenzymatically in cells. These results uncover a critical role for AcP in bacterial acetylation and indicate that most acetylation in E. coli occurs at a low level and is dynamically affected by metabolism and cell proliferation in a global, uniform manner.

Original language	English
Journal	Molecular Cell
Volume	51
Issue number	2
Pages (from-to)	265-272
Number of pages	8
ISSN	1097-2765
DOIs	https://doi.org/10.1016/j.molcel.2013.06.003
Publication status	Published - 25 Jul 2013

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title = "Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli",

abstract = "Lysine acetylation is a frequently occurring posttranslational modification in bacteria; however, little is known about its origin and regulation. Using the model bacterium Escherichia coli (E. coli), we found that most acetylation occurred at a low level and accumulated in growth-arrested cells in a manner that depended on the formation of acetyl-phosphate (AcP) through glycolysis. Mutant cells unable to produce AcP had significantly reduced acetylation levels, while mutant cells unable to convert AcP to acetate had significantly elevated acetylation levels. We showed that AcP can chemically acetylate lysine residues in vitro and that AcP levels are correlated with acetylation levels in vivo, suggesting that AcP may acetylate proteins nonenzymatically in cells. These results uncover a critical role for AcP in bacterial acetylation and indicate that most acetylation in E. coli occurs at a low level and is dynamically affected by metabolism and cell proliferation in a global, uniform manner.",

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T1 - Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli

AU - Weinert, Brian T

AU - Iesmantavicius, Vytautas

AU - Wagner, Sebastian A

AU - Schölz, Christian

AU - Gummesson, Bertil

AU - Beli, Petra

AU - Nyström, Thomas

AU - Choudhary, Chuna Ram

PY - 2013/7/25

Y1 - 2013/7/25

N2 - Lysine acetylation is a frequently occurring posttranslational modification in bacteria; however, little is known about its origin and regulation. Using the model bacterium Escherichia coli (E. coli), we found that most acetylation occurred at a low level and accumulated in growth-arrested cells in a manner that depended on the formation of acetyl-phosphate (AcP) through glycolysis. Mutant cells unable to produce AcP had significantly reduced acetylation levels, while mutant cells unable to convert AcP to acetate had significantly elevated acetylation levels. We showed that AcP can chemically acetylate lysine residues in vitro and that AcP levels are correlated with acetylation levels in vivo, suggesting that AcP may acetylate proteins nonenzymatically in cells. These results uncover a critical role for AcP in bacterial acetylation and indicate that most acetylation in E. coli occurs at a low level and is dynamically affected by metabolism and cell proliferation in a global, uniform manner.

AB - Lysine acetylation is a frequently occurring posttranslational modification in bacteria; however, little is known about its origin and regulation. Using the model bacterium Escherichia coli (E. coli), we found that most acetylation occurred at a low level and accumulated in growth-arrested cells in a manner that depended on the formation of acetyl-phosphate (AcP) through glycolysis. Mutant cells unable to produce AcP had significantly reduced acetylation levels, while mutant cells unable to convert AcP to acetate had significantly elevated acetylation levels. We showed that AcP can chemically acetylate lysine residues in vitro and that AcP levels are correlated with acetylation levels in vivo, suggesting that AcP may acetylate proteins nonenzymatically in cells. These results uncover a critical role for AcP in bacterial acetylation and indicate that most acetylation in E. coli occurs at a low level and is dynamically affected by metabolism and cell proliferation in a global, uniform manner.

U2 - 10.1016/j.molcel.2013.06.003

DO - 10.1016/j.molcel.2013.06.003

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SN - 1097-2765

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SP - 265

EP - 272

JO - Molecular Cell

JF - Molecular Cell

IS - 2

ER -

Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli

Abstract

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