Protein Acetyltransferases Mediate Bacterial Adaptation to a Diverse Environment.
Escherichia coli acetyltransferase
Salmonella acetyltransferase
histone acetylation
histone deacetylase
lysine acetyltransferase
protein acetylation
Journal
Journal of bacteriology
ISSN: 1098-5530
Titre abrégé: J Bacteriol
Pays: United States
ID NLM: 2985120R
Informations de publication
Date de publication:
08 09 2021
08 09 2021
Historique:
pubmed:
13
7
2021
medline:
22
12
2021
entrez:
12
7
2021
Statut:
ppublish
Résumé
Protein lysine acetylation is a conserved posttranslational modification that modulates several cellular processes. Protein acetylation and its physiological implications in eukaryotes are well understood; however, its role in bacteria is emerging. Lysine acetylation in bacteria is fine-tuned by the concerted action of lysine acetyltransferases (KATs), protein deacetylases (KDACs), and metabolic intermediates, e.g., acetyl coenzyme A (Ac-CoA) and acetyl phosphate (AcP). AcP-mediated nonenzymatic acetylation is predominant in bacteria due to its high acetyl transfer potential, whereas enzymatic acetylation by bacterial KATs (bKATs) is considered less abundant.
Identifiants
pubmed: 34251868
doi: 10.1128/JB.00231-21
pmc: PMC8425404
doi:
Substances chimiques
Bacterial Proteins
0
Acetyltransferases
EC 2.3.1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
e0023121Références
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