A novel mode of histone-like protein HupB regulating Sinorhizobium meliloti cell division through lysine acetylation.

ABSTRACT: HU, a small, basic histone-like protein, binds to bacterial genomic DNA, influencing DNA conformation, replication, and transcription. Its acetylation is a key post-translational modification affecting its DNA-binding activity. The role of HU acetylation in regulating cell division through the cell cycle regulatory system remained largely unknown. In this study, we find that stimulation of lysine acetylation or non-acetylation in HupB, a homolog of HU, differentially regulates the expression of cell cycle regulators, as well as cell growth and division in Sinorhizobium meliloti. Lys3, Lys13, and Lys83 in HupB were identified as acetylated residues by mass spectrometry. Mutating these residues to arginine (stimulating non-acetylation) in HupB impedes normal cell division, while subst

SUBMITTER: Li N 

PROVIDER: S-EPMC11803250 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature