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Curr Genet. 2016 May;62(2):335-41. doi: 10.1007/s00294-015-0552-4. Epub 2015 Dec 12.

Bacterial protein acetylation: new discoveries unanswered questions.

Author information

1
Department of Microbiology and Immunology, Stritch School of Medicine, Loyola University Chicago, 2160 S. First Ave., Bldg. 105, Maywood, IL, 60153, USA. awolfe@luc.edu.

Abstract

Nε-acetylation is emerging as an abundant post-translational modification of bacterial proteins. Two mechanisms have been identified: one is enzymatic, dependent on an acetyltransferase and acetyl-coenzyme A; the other is non-enzymatic and depends on the reactivity of acetyl phosphate. Some, but not most, of those acetylations are reversed by deacetylases. This review will briefly describe the current status of the field and raise questions that need answering.

KEYWORDS:

Acetyl phosphate; Acetyltransferase; CRP; Deacetylase; Metabolism; Post-translational modification

PMID:
26660885
PMCID:
PMC4826803
DOI:
10.1007/s00294-015-0552-4
[Indexed for MEDLINE]
Free PMC Article

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