Mechanisms, Detection, and Relevance of Protein Acetylation in Prokaryotes.

Abstract:

:Posttranslational modification of a protein, either alone or in combination with other modifications, can control properties of that protein, such as enzymatic activity, localization, stability, or interactions with other molecules. N-ε-Lysine acetylation is one such modification that has gained attention in recent years, with a prevalence and significance that rival those of phosphorylation. This review will discuss the current state of the field in bacteria and some of the work in archaea, focusing on both mechanisms of N-ε-lysine acetylation and methods to identify, quantify, and characterize specific acetyllysines. Bacterial N-ε-lysine acetylation depends on both enzymatic and nonenzymatic mechanisms of acetylation, and recent work has shed light into the regulation of both mechanisms. Technological advances in mass spectrometry have allowed researchers to gain insight with greater biological context by both (i) analyzing samples either with stable isotope labeling workflows or using label-free protocols and (ii) determining the true extent of acetylation on a protein population through stoichiometry measurements. Identification of acetylated lysines through these methods has led to studies that probe the biological significance of acetylation. General and diverse approaches used to determine the effect of acetylation on a specific lysine will be covered.

journal_name

mBio

journal_title

mBio

authors

Christensen DG,Baumgartner JT,Xie X,Jew KM,Basisty N,Schilling B,Kuhn ML,Wolfe AJ

doi

10.1128/mBio.02708-18

subject

Has Abstract

pub_date

2019-04-09 00:00:00

issue

2

issn

2150-7511

pii

mBio.02708-18

journal_volume

10

pub_type

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