N^ε-lysine acetylation of the histone-like protein HBsu influences antibiotic survival and persistence in <i>Bacillus subtilis</i>.

ABSTRACT: N^ε-lysine acetylation is recognized as a prevalent post-translational modification (PTM) that regulates proteins across all three domains of life. In Bacillus subtilis, the histone-like protein HBsu is acetylated at seven sites, which regulates DNA compaction and the process of sporulation. In Mycobacteria, DNA compaction is a survival strategy in response antibiotic exposure. Acetylation of the HBsu ortholog HupB decondenses the chromosome to escape this drug-induced, non-growing state, and in addition, regulates the formation of drug-tolerant subpopulations by altering gene expression. We hypothesized that the acetylation of HBsu plays similar regulatory roles. First, we measured nucleoid area by fluorescence microscopy and in agreement, we found that wild-type cells co

SUBMITTER: Carr RA 

PROVIDER: S-EPMC11148388 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature