|Title||The regulation, function, and detection of protein acetylation in bacteria.|
|Publication Type||Journal Article|
|Year of Publication||2017|
|Authors||Carabetta, VJ, Cristea, IM|
|Date Published||2017 Apr 24|
N(ε)-lysine acetylation is now recognized as an abundant post-translational modification (PTM) that influences many essential biological pathways. Advancements in mass spectrometry-based proteomics have led to the discovery that bacteria contain hundreds of acetylated proteins, contrary to the prior notion of rare acetylation events in bacteria. Although the mechanisms that regulate protein acetylation are still not fully defined, it is understood that this modification is finely-tuned via both enzymatic and non-enzymatic mechanisms. The opposing actions of Gcn5-related N-acetyltransferases (GNATs) and deacetylases, including sirtuins, provide the enzymatic control of lysine acetylation. A non-enzymatic mechanism of acetylation has also been demonstrated, and proven prominent, in bacteria, as well as in mitochondria. The functional consequences of the vast majority of the identified acetylation sites remain unknown. From studies in mammalian systems, acetylation of critical lysine residues was shown to impact protein function by altering its structure, sub-cellular localization, and interactions. It is becoming apparent that the same diversity of functions can be found in bacteria. Here, we review the current knowledge of the mechanisms and the functional consequences of acetylation in bacteria. Additionally, we discuss the methods available for detecting acetylation sites, including quantitative mass spectrometry-based methods, which promise to promote this field of research. We conclude with possible future directions and broader implications of the study of protein acetylation in bacteria.
|Alternate Journal||J. Bacteriol.|