Abstract
Reversible lysine acetylation is a mechanism used by bacteria and archaea to control protein function. Jeter and Escalante-Semerena (e00333-21) identified the enzymes of Campylobacter jejuni that acetylate and deacetylate the central metabolic enzyme acetyl coenzyme A synthetase of this bacterium. Strains of Salmonella enterica were used to demonstrate the functionality of the C. jejuni Acs acetylating/deacetylating enzymes, which specifically target residue K617 of CjAcs. Of note, the deacetylating enzyme is a NAD+-consuming sirtuin enzyme. The stage is set for the analysis of C. jejuni strains lacking the alluded functions, so we can better understand acetate metabolism in this human pathogen.
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