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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本期重要文章

可逆的赖氨酸乙酰化是细菌和古细菌用来控制蛋白质功能的一种机制。Jeter 和 Escalante-Semerena (e00333-21) 鉴定了空肠弯曲杆菌的酶，这些酶可以使该细菌的中心代谢酶乙酰辅酶 A 合成酶乙酰化和去乙酰化。肠沙门氏菌菌株用于证明空肠弯曲杆菌 Acs 乙酰化/去乙酰化酶的功能，该酶专门针对 CjAcs 的残基 K617。值得注意的是，去乙酰化酶是一种消耗 NAD+ 的去乙酰化酶。为分析缺乏上述功能的空肠弯曲菌菌株做好了准备，因此我们可以更好地了解这种人类病原体中的乙酸盐代谢。