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 g...

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Autores principales:	D. G. Christensen, J. T. Baumgartner, X. Xie, K. M. Jew, N. Basisty, B. Schilling, M. L. Kuhn, A. J. Wolfe
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2019
Materias:	acetylation acetylome bacteria lysine acetyltransferase mass spectrometry proteomics Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/30bacc2232d844efaf7405ffc8200334
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spelling	oai:doaj.org-article:30bacc2232d844efaf7405ffc82003342021-11-15T15:55:26ZMechanisms, Detection, and Relevance of Protein Acetylation in Prokaryotes10.1128/mBio.02708-182150-7511https://doaj.org/article/30bacc2232d844efaf7405ffc82003342019-04-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.02708-18https://doaj.org/toc/2150-7511ABSTRACT 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.D. G. ChristensenJ. T. BaumgartnerX. XieK. M. JewN. BasistyB. SchillingM. L. KuhnA. J. WolfeAmerican Society for Microbiologyarticleacetylationacetylomebacterialysine acetyltransferasemass spectrometryproteomicsMicrobiologyQR1-502ENmBio, Vol 10, Iss 2 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	acetylation acetylome bacteria lysine acetyltransferase mass spectrometry proteomics Microbiology QR1-502
spellingShingle	acetylation acetylome bacteria lysine acetyltransferase mass spectrometry proteomics Microbiology QR1-502 D. G. Christensen J. T. Baumgartner X. Xie K. M. Jew N. Basisty B. Schilling M. L. Kuhn A. J. Wolfe Mechanisms, Detection, and Relevance of Protein Acetylation in Prokaryotes
description	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.
format	article
author	D. G. Christensen J. T. Baumgartner X. Xie K. M. Jew N. Basisty B. Schilling M. L. Kuhn A. J. Wolfe
author_facet	D. G. Christensen J. T. Baumgartner X. Xie K. M. Jew N. Basisty B. Schilling M. L. Kuhn A. J. Wolfe
author_sort	D. G. Christensen
title	Mechanisms, Detection, and Relevance of Protein Acetylation in Prokaryotes
title_short	Mechanisms, Detection, and Relevance of Protein Acetylation in Prokaryotes
title_full	Mechanisms, Detection, and Relevance of Protein Acetylation in Prokaryotes
title_fullStr	Mechanisms, Detection, and Relevance of Protein Acetylation in Prokaryotes
title_full_unstemmed	Mechanisms, Detection, and Relevance of Protein Acetylation in Prokaryotes
title_sort	mechanisms, detection, and relevance of protein acetylation in prokaryotes
publisher	American Society for Microbiology
publishDate	2019
url	https://doaj.org/article/30bacc2232d844efaf7405ffc8200334
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Mechanisms, Detection, and Relevance of Protein Acetylation in Prokaryotes

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