title: Regulation of bacterial physiology by lysine acetylation of proteins.
abstract: Post-translational modification of proteins is a reversible mechanism of cellular adaptation to changing environmental conditions. In eukaryotes, the physiological relevance of N-ɛ-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.
authors.affiliation: Department of Biochemistry and Molecular Biology B and Immunology, Faculty of Chemistry, University of Murcia, Campus de Espinardo, Regional Campus of International Excellence "Campus Mare Nostrum", P.O. Box 4021, Murcia E-30100, Spain. Electronic address: vbernal@um.es.
authors.forename: Vicente
authors.initials: V
authors.lastname: Bernal
authors.affiliation: Department of Biochemistry and Molecular Biology B and Immunology, Faculty of Chemistry, University of Murcia, Campus de Espinardo, Regional Campus of International Excellence "Campus Mare Nostrum", P.O. Box 4021, Murcia E-30100, Spain.
authors.forename: Sara
authors.initials: S
authors.lastname: Castaño-Cerezo
authors.affiliation: Department of Biochemistry and Molecular Biology B and Immunology, Faculty of Chemistry, University of Murcia, Campus de Espinardo, Regional Campus of International Excellence "Campus Mare Nostrum", P.O. Box 4021, Murcia E-30100, Spain.
authors.forename: Julia
authors.initials: J
authors.lastname: Gallego-Jara
authors.affiliation: Department of Biochemistry and Molecular Biology B and Immunology, Faculty of Chemistry, University of Murcia, Campus de Espinardo, Regional Campus of International Excellence "Campus Mare Nostrum", P.O. Box 4021, Murcia E-30100, Spain.
authors.forename: Ana
authors.initials: A
authors.lastname: Écija-Conesa
authors.affiliation: Department of Biochemistry and Molecular Biology B and Immunology, Faculty of Chemistry, University of Murcia, Campus de Espinardo, Regional Campus of International Excellence "Campus Mare Nostrum", P.O. Box 4021, Murcia E-30100, Spain.
authors.forename: Teresa
authors.initials: T
authors.lastname: de Diego
authors.affiliation: Department of Biochemistry and Molecular Biology B and Immunology, Faculty of Chemistry, University of Murcia, Campus de Espinardo, Regional Campus of International Excellence "Campus Mare Nostrum", P.O. Box 4021, Murcia E-30100, Spain.
authors.forename: José Luis
authors.initials: JL
authors.lastname: Iborra
authors.affiliation: Department of Biochemistry and Molecular Biology B and Immunology, Faculty of Chemistry, University of Murcia, Campus de Espinardo, Regional Campus of International Excellence "Campus Mare Nostrum", P.O. Box 4021, Murcia E-30100, Spain. Electronic address: mcanovas@um.es.
authors.forename: Manuel
authors.initials: M
authors.lastname: Cánovas
mesh_terms: D000107:Acetylation; D000215:Acylation; D018407:Bacterial Physiological Phenomena; D001426:Bacterial Proteins / Q000378:metabolism*; D008239:Lysine / Q000378:metabolism*; D058615:Synthetic Biology
chemical_list: D001426:Bacterial Proteins; D008239:Lysine