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Recent Contributions of Proteomics to Our Understanding of Reversible N ε -Lysine Acylation in Bacteria.

Authors :
Popova L
Carr RA
Carabetta VJ
Source :
Journal of proteome research [J Proteome Res] 2024 Aug 02; Vol. 23 (8), pp. 2733-2749. Date of Electronic Publication: 2024 Mar 05.
Publication Year :
2024

Abstract

Post-translational modifications (PTMs) have been extensively studied in both eukaryotes and prokaryotes. Lysine acetylation, originally thought to be a rare occurrence in bacteria, is now recognized as a prevalent and important PTM in more than 50 species. This expansion in interest in bacterial PTMs became possible with the advancement of mass spectrometry technology and improved reagents such as acyl-modification specific antibodies. In this Review, we discuss how mass spectrometry-based proteomic studies of lysine acetylation and other acyl modifications have contributed to our understanding of bacterial physiology, focusing on recently published studies from 2018 to 2023. We begin with a discussion of approaches used to study bacterial PTMs. Next, we discuss newly characterized acylomes, including acetylomes, succinylomes, and malonylomes, in different bacterial species. In addition, we examine proteomic contributions to our understanding of bacterial virulence and biofilm formation. Finally, we discuss the contributions of mass spectrometry to our understanding of the mechanisms of acetylation, both enzymatic and nonenzymatic. We end with a discussion of the current state of the field and possible future research avenues to explore.

Details

Language :
English
ISSN :
1535-3907
Volume :
23
Issue :
8
Database :
MEDLINE
Journal :
Journal of proteome research
Publication Type :
Academic Journal
Accession number :
38442041
Full Text :
https://doi.org/10.1021/acs.jproteome.3c00912