Deciphering novel enzymatic and non-enzymatic lysine lactylation in <i>Salmonella</i>.

ABSTRACT: Lysine lactylation, a novel post-translational modification, is involved in multiple cellular processes. The role of lactylation remains largely unknown, especially in bacteria. Here, we identified 1090 lactylation sites on 469 proteins by mass spectrometry in Salmonella Typhimurium. Many proteins involved in metabolic processes, protein translation, and other biological functions are lactylated, with lactylation levels varying according to the growth phase or lactate supplementation. Lactylation is regulated by glycolysis, and inhibition of L-lactate utilization can enhance lactylation levels. In addition to the known lactylase in E. coli, the acetyltransferase YfiQ can also catalyse lactylation. More importantly, L-lactyl coenzyme A (L-La-CoA) and S,D-lactoylglutathi

SUBMITTER: Zhang C 

PROVIDER: S-EPMC11924271 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature