Protein acetylation in prokaryotes

• Published in: Proteomics (Weinheim) Vol. 11; no. 15; pp. 3012 - 3022
• Main Authors: Jones, Joshua D., O'Connor, C. David
• Format: Journal Article
• Language: English
• Published: Weinheim WILEY-VCH Verlag 01.08.2011; WILEY‐VCH Verlag; Wiley Subscription Services, Inc
• Subjects: Acetylation; Acetyltransferase; Acetyltransferases - metabolism; Archaea; Archaea - enzymology; Archaea - metabolism; Archaeal Proteins - metabolism; Bacteria - enzymology; Bacteria - metabolism; Bacterial Proteins - metabolism; Deacetylase; epigenetics; Lysine; Lysine - metabolism; Metabolic Networks and Pathways; Metabolism; Microbiology; Phosphorylation; Prokaryotes; Protein turnover; Proteins; proteomics; Regulation; Transcription; Translation
• ISSN: 1615-9853; 1615-9861
• DOI: 10.1002/pmic.201000812

Protein acetylation plays a critical regulatory role in eukaryotes but until recently its significance and function in bacteria and the archaea were obscure. It is now clear, however, that prokaryotes have the capacity to acetylate both the α‐amino groups of N‐terminal residues and the ε‐amino groups of lysine side chains. In this review, we bring together information indicating that such acetylation is widespread and that it is likely to regulate fundamental cellular processes. We particularly focus on lysine acetylation, which recent studies show can occur in proteins involved in transcription, translation, pathways associated with central metabolism and stress responses. Intriguingly, specific acetylated lysine residues map to critical regions in the three‐dimensional structures of key proteins, e.g. to active sites or to surfaces that dock with other major cellular components. Like phosphorylation, acetylation appears to be an ancient reversible modification that can be present at multiple sites in proteins, thereby potentially producing epigenetic combinatorial complexity. It may be particularly important in regulating central metabolism in prokaryotes due to the requirement for acetyl‐CoA and NAD+ for protein acetyltransferases and Sir2‐type deacetylases, respectively.