Publication: Regulation of bacterial physiology by lysine acetylation of proteins
Authors
Bernal Sánchez, Vicente ; Castaño Cerezo, Sara ; Écija Conesa, Ana ; Iborra Pastor, José Luis ; Cánovas Díaz, Manuel ; Diego Puente, Teresa de ; Gallego Jara, Julia
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Publisher
Elsevier
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DOI
http://dx.doi.org/10.1016/j.nbt.2014.03.002
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info:eu-repo/semantics/article
Description
©2014. The authors. This document is made available under the CC-BY 4.0 license http://creativecommons.org/licenses/by /4.0/
This document is the accepted version of a published work that appeared in final form in New Biotechnology. To access the final edited and published work see http://dx.doi.org/10.1016/j.nbt.2014.03.002
Abstract
Post-translational modification of proteins is a reversible mechanism of cellular adaptation to changing environmental conditions. In eukaryotes, the physiological relevance of N-e-lysine protein acetylation is well demonstrated. In recent times, important roles in the regulation of metabolic processes in bacteria are being uncovered, adding complexity to cellular regulatory networks. The aim of this mini-review is to sum up the current state-of-the-art in the regulation of bacterial physiology by protein acetylation. Current knowledge on the molecular biology aspects of known bacterial protein acetyltransferases and deacetylases will be summarized. Protein acetylation in Escherichia coli, Salmonella enterica, Bacillus subtilis, Rhodopseudomonas palustris and Mycobacterium tuberculosis, will be explained in the light of their physiological relevance. Progress in the elucidation of bacterial acetylomes and the emerging understanding of chemical acylation mechanisms will be discussed together with their regulatory and evolutionary implications. Fundamental molecular
studies detailing this recently discovered regulatory mechanism pave the way for their prospective application for the construction of synthetic regulation networks.
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Citation
New Biotechnology Dec 25
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