YfmK is an N^ε-lysine acetyltransferase that directly acetylates the histone-like protein HBsu in Bacillus subtilis.

ABSTRACT: N^ε-lysine acetylation is an abundant and dynamic regulatory posttranslational modification that remains poorly characterized in bacteria. In bacteria, hundreds of proteins are known to be acetylated, but the biological significance of the majority of these events remains unclear. Previously, we characterized the Bacillus subtilis acetylome and found that the essential histone-like protein HBsu contains seven previously unknown acetylation sites in vivo. Here, we investigate whether acetylation is a regulatory component of the function of HBsu in nucleoid compaction. Using mutations that mimic the acetylated and unacetylated forms of the protein, we show that the inability to acetylate key HBsu lysine residues results in a more compacted nucleoid. We further investigated t

SUBMITTER: Carabetta VJ 

PROVIDER: S-EPMC6397556 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature