Format

Send to

Choose Destination
Annu Rev Microbiol. 2019 Sep 8;73:111-132. doi: 10.1146/annurev-micro-020518-115526. Epub 2019 May 15.

Protein Acetylation in Bacteria.

Author information

1
Department of Microbiology, University of Georgia, Athens, Georgia 30602, USA; email: jcescala@uga.edu.

Abstract

Acetylation is a posttranslational modification conserved in all domains of life that is carried out by N-acetyltransferases. While acetylation can occur on Nα-amino groups, this review will focus on Nε-acetylation of lysyl residues and how the posttranslational modification changes the cellular physiology of bacteria. Up until the late 1990s, acetylation was studied in eukaryotes in the context of chromatin maintenance and gene expression. At present, bacterial protein acetylation plays a prominent role in central and secondary metabolism, virulence, transcription, and translation. Given the diversity of niches in the microbial world, it is not surprising that the targets of bacterial protein acetyltransferases are very diverse, making their biochemical characterization challenging. The paradigm for acetylation in bacteria involves the acetylation of acetyl-CoA synthetase, whose activity must be tightly regulated to maintain energy charge homeostasis. While this paradigm has provided much mechanistic detail for acetylation and deacetylation, in this review we discuss advances in the field that are changing our understanding of the physiological role of protein acetylation in bacteria.

KEYWORDS:

acetyltransferases; deacetylases; enzymatic and abiotic lysine acetylation; lysine acetylation

Supplemental Content

Full text links

Icon for Atypon Icon for PubMed Central
Loading ...
Support Center