Interplay between chromophore binding and domain assembly by the B₁₂-dependent photoreceptor protein, CarH.

ABSTRACT: Organisms across the natural world respond to their environment through the action of photoreceptor proteins. The vitamin B₁₂-dependent photoreceptor, CarH, is a bacterial transcriptional regulator that controls the biosynthesis of carotenoids to protect against photo-oxidative stress. The binding of B₁₂ to CarH monomers in the dark results in the formation of a homo-tetramer that complexes with DNA; B₁₂ photochemistry results in tetramer dissociation, releasing DNA for transcription. Although the details of the response of CarH to light are beginning to emerge, the biophysical mechanism of B₁₂-binding in the dark and how this drives domain assembly is poorly understood. Here - using a combination of molecular dynamics simulations, native ion mob

SUBMITTER: Camacho IS 

PROVIDER: S-EPMC8221060 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature