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Regulation of bacterial physiology by lysine acetylation of proteins

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dc.contributor.authorBernal Sánchez, Vicente
dc.contributor.authorCastaño Cerezo, Sara
dc.contributor.authorÉcija Conesa, Ana
dc.contributor.authorIborra Pastor, José Luis
dc.contributor.authorCánovas Díaz, Manuel
dc.contributor.authorDiego Puente, Teresa de
dc.contributor.authorGallego Jara, Julia
dc.contributor.departmentBioquímica y Biología Molecular B e Inmunología
dc.date.accessioned2023-12-12T23:11:57Z
dc.date.available2023-12-12T23:11:57Z
dc.date.issued2014
dc.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
dc.description.abstractPost-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.
dc.formatapplication/pdfes_ES
dc.format.extent10
dc.identifier.citationNew Biotechnology Dec 25
dc.identifier.doihttp://dx.doi.org/10.1016/j.nbt.2014.03.002
dc.identifier.issn1871-6784
dc.identifier.urihttp://hdl.handle.net/10201/136585
dc.languageenges_ES
dc.publisherElsevier
dc.relationThis work has been partly funded by MINECO BIO2011-29233-C02-01 and Fundacio´n Se´neca-CARM 08660/PI/08 projects.
dc.relation.isreferencedbyED_IDENTRADA=1276
dc.relation.publisherversionhttps://pubmed.ncbi.nlm.nih.gov/37532220/
dc.rightsinfo:eu-repo/semantics/openAccess*
dc.rightsAtribución 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.titleRegulation of bacterial physiology by lysine acetylation of proteinses_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dspace.entity.typePublicationes
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relation.isAuthorOfPublication0212fc0f-e15c-4b27-9a2d-116768a47044
relation.isAuthorOfPublication.latestForDiscovery57bf3537-1124-49ab-8774-bd0c3bdf1c28
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