GNAT family Pat2 is required for long-term survival on glycerol and catalyzes lysine acetylation of glycerol kinase in hypersaline-adapted archaea.

ABSTRACT: Lysine acetylation is a widespread post-translational modification that regulates key biological processes including metabolism and chromatin dynamics, yet its roles in archaea remain poorly understood. Here, we investigated two Gcn5-related N-acetyltransferase (GNAT) family homologs, pat1 and pat2, in the halophilic archaeon Haloferax volcanii (Hv). A ∆pat2 mutant exhibited premature cell death on glycerol, a phenotype not observed in the parent strain, ∆pat1 mutant, or on glucose. Complementation of the ∆pat2 mutant with plasmid-expressed pat2 restored survival on glycerol, confirming the essential role of pat2 in this process. In vitro assays revealed HvPat2 catalyzes lysine acetylation of glycerol kinase, HvGlpK, an enzyme

SUBMITTER: Judd HN 

PROVIDER: S-EPMC12607858 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature