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

Research output: Contribution to journalJournal articleResearchpeer-review

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

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 languageEnglish
JournalMolecular Cell
Volume51
Issue number2
Pages (from-to)265-272
Number of pages8
ISSN1097-2765
DOIs
Publication statusPublished - 25 Jul 2013

ID: 47460488