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 journalJournal articleResearchpeer-review

Harvard

Weinert, BT, Iesmantavicius, V, Wagner, SA, Schölz, C, Gummesson, B, Beli, P, Nyström, T & Choudhary, CR 2013, 'Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli', Molecular Cell, vol. 51, no. 2, pp. 265-272. https://doi.org/10.1016/j.molcel.2013.06.003

APA

Weinert, B. T., Iesmantavicius, V., Wagner, S. A., Schölz, C., Gummesson, B., Beli, P., ... Choudhary, C. R. (2013). Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Molecular Cell, 51(2), 265-272. https://doi.org/10.1016/j.molcel.2013.06.003

Vancouver

Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P et al. Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Molecular Cell. 2013 Jul 25;51(2):265-272. https://doi.org/10.1016/j.molcel.2013.06.003

Author

Weinert, Brian T ; Iesmantavicius, Vytautas ; Wagner, Sebastian A ; Schölz, Christian ; Gummesson, Bertil ; Beli, Petra ; Nyström, Thomas ; Choudhary, Chuna Ram. / Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. In: Molecular Cell. 2013 ; Vol. 51, No. 2. pp. 265-272.

Bibtex

@article{fdf7d289decb4ce5b226bed55e7d51d6,
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.",
author = "Weinert, {Brian T} and Vytautas Iesmantavicius and Wagner, {Sebastian A} and Christian Sch{\"o}lz and Bertil Gummesson and Petra Beli and Thomas Nystr{\"o}m and Choudhary, {Chuna Ram}",
note = "Copyright {\circledC} 2013 Elsevier Inc. All rights reserved.",
year = "2013",
month = "7",
day = "25",
doi = "10.1016/j.molcel.2013.06.003",
language = "English",
volume = "51",
pages = "265--272",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "2",

}

RIS

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

VL - 51

SP - 265

EP - 272

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 2

ER -

ID: 47460488