Biochemical and structural characterization of a GNAT superfamily protein acetyltransferase from Helicobacter pylori.

ABSTRACT: Helicobacter pylori (H. pylori), a gastric pathogen with high genetic variability and a unique niche, causes peptic ulcers and gastric cancer. Natural transformation contributes to the genetic variability of H. pylori. To date, protein acetylation and the associated acetyltransferase(s) have not been reported in this bacterium. Here, we report protein acetylation in H. pylori and identify a putative protein acetyltransferase, HP0935, capable of acetylating amino acids and proteins, including DNA processing protein A (DprA), which is involved in natural transformation. HP0935 acetylates residue K133 in DprA, which is important for DNA binding, thus is likely to regulate natural transformation. We determined the crystal structures of HP0935 in its apo form and in complex with acetyl-coenzyme

SUBMITTER: Dadireddy V 

PROVIDER: S-EPMC12273574 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature