Allosteric coupling activation mechanism in histidine kinases.

ABSTRACT: Histidine kinases (HKs) are crucial regulators of cellular functions, mediating the phosphorylation of specific proteins to modulate their activity and localization. Upon signal detection, HKs transfer a phosphate group from ATP to a conserved histidine residue within their Dimerization and Histidine phosphotransfer domain, subsequently passing the phosphate to a response regulator (RR) that typically interacts with DNA promoters to regulate gene expression. This study investigates the signal transduction mechanism of Bacillus subtilis HK DesK. We generated substitutions on the conserved phospho-acceptor histidine and evaluated their effects on DesK's activity in both in vivo and in vitro contexts. Notably, we found that a variant of DesK lacking the conserved histidine could still activat

SUBMITTER: Almada JC 

PROVIDER: S-EPMC12033271 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature