Acetyl-Phosphate is a Critical Determinant of Lysine Acetylation in E. coli
Lysine acetylation is a frequently occurring posttranslational modification in bacteria; however, little is known about its origin and regulation.
Using the model bacterium E. coli, a research team led by Professor Chuna Ram Choudhary has identified more than 8000 unique acetylation sites. 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.
The researchers found that AcP could chemically acetylate lysine residues in vitro and that AcP levels were correlated with acetylation levels in vivo, suggesting that AcP may acetylate proteins non-enzymatically 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.
Title: Acetyl-Phosphate is a Critical Determinant of Lysine Acetylation in E. coli
Authors: Brian T. Weinert, Vytautas Iesmantavicius, Sebastian A. Wagner, Christian Schölz, Bertil Gummesson, Petra Beli, Thomas Nyström, and Chuna Ram Choudhary