Dynamic acetylation of a conserved lysine impacts glycerol kinase activity and abundance in the haloarchaeon Haloferax volcanii.

ABSTRACT: Lysine acetylation is a key regulator of metabolism, but its role in archaeal carbon metabolism remains unclear. In halophilic archaea such as Haloferax volcanii, glycerol kinase (GK, glpK) catalyzes the phosphorylation of glycerol to glycerol-3-phosphate, the first committed step in glycerol catabolism. Unlike bacterial GKs, which are typically repressed during glucose metabolism, H. volcanii prefers glycerol as a carbon and energy source rather than glucose, suggesting that GK across species is regulated by distinct mechanisms. Here, we show that lysine acetylation enhances H. volcanii GK (HvGK) activity, allosteric behavior, stability, and cellular abundance during growth on glycerol. Lysine residue 153 (K153), located within a conserved flexible loop, was identified as the primary acet

SUBMITTER: Sanchez KM 

PROVIDER: S-EPMC12853182 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature