An analysis of the solution structure and signaling mechanism of LovK, a sensor histidine kinase integrating light and redox signals.

ABSTRACT: Flavin-binding LOV domains are broadly conserved in plants, fungi, archaea, and bacteria. These approximately 100-residue photosensory modules are generally encoded within larger, multidomain proteins that control a range of blue light-dependent physiologies. The bacterium Caulobacter crescentus encodes a soluble LOV-histidine kinase, LovK, that regulates the adhesive properties of the cell. Full-length LovK is dimeric as are a series of systematically truncated LovK constructs containing only the N-terminal LOV sensory domain. Nonconserved sequence flanking the LOV domain functions to tune the signaling lifetime of the protein. Size exclusion chromatography and small-angle X-ray scattering (SAXS) demonstrate that the LOV sensor domain does not undergo a large conformational change in resp

SUBMITTER: Purcell EB 

PROVIDER: S-EPMC2915561 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature