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- W2017101977 endingPage "595" @default.
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- W2017101977 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." @default.
- W2017101977 created "2016-06-24" @default.
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- W2017101977 creator A5069287246 @default.
- W2017101977 creator A5080540849 @default.
- W2017101977 creator A5091633756 @default.
- W2017101977 date "2014-12-01" @default.
- W2017101977 modified "2023-10-03" @default.
- W2017101977 title "Regulation of bacterial physiology by lysine acetylation of proteins" @default.
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- W2017101977 doi "https://doi.org/10.1016/j.nbt.2014.03.002" @default.
- W2017101977 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24636882" @default.
- W2017101977 hasPublicationYear "2014" @default.