Allosteric activation of bacterial response regulators: the role of the cognate histidine kinase beyond phosphorylation.

ABSTRACT:

Unlabelled

Response regulators are proteins that undergo transient phosphorylation, connecting specific signals to adaptive responses. Remarkably, the molecular mechanism of response regulator activation remains elusive, largely because of the scarcity of structural data on multidomain response regulators and histidine kinase/response regulator complexes. We now address this question by using a combination of crystallographic data and functional analyses in vitro and in vivo, studying DesR and its cognate sensor kinase DesK, a two-component system that controls membrane fluidity in Bacillus subtilis. We establish that phosphorylation of the receiver domain of DesR is allosterically coupled to two distinct exposed surfaces of the protein, controlling noncanonical dimerization/tetram

SUBMITTER: Trajtenberg F 

PROVIDER: S-EPMC4251995 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature