Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli
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Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. / Weinert, Brian T; Iesmantavicius, Vytautas; Wagner, Sebastian A; Schölz, Christian; Gummesson, Bertil; Beli, Petra; Nyström, Thomas; Choudhary, Chuna Ram.
In: Molecular Cell, Vol. 51, No. 2, 25.07.2013, p. 265-272.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
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
N1 - Copyright © 2013 Elsevier Inc. All rights reserved.
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
M3 - Journal article
C2 - 23830618
VL - 51
SP - 265
EP - 272
JO - Molecular Cell
JF - Molecular Cell
SN - 1097-2765
IS - 2
ER -
ID: 47460488