Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/141984
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Title

Structural basis for gene regulation by a B12-dependent photoreceptor

AuthorsJost, M.; Fernández-Zapata, J.; Polanco, M.C.; Ortiz-Guerrero, J.M.; Chen, P.Y.T.; Kang, G.; Padmanabhan, Subramanian CSIC ORCID; Elías-Arnanz, Montserrat; Drennan, C.L.
Issue Date2015
CitationNature 526: 536- 541 (2015)
AbstractPhotoreceptor proteins enable organisms to sense and respond to light. The newly discovered CarH-type photoreceptors use a Vitamin B derivative, adenosylcobalamin, as the light-sensing chromophore to mediate light-dependent gene regulation. Here we present crystal structures of Thermus thermophilus CarH in all three relevant states: in the dark, both free and bound to operator DNA, and after light exposure. These structures provide visualizations of how adenosylcobalamin mediates CarH tetramer formation in the dark, how this tetramer binds to the promoter -35 element to repress transcription, and how light exposure leads to a large-scale conformational change that activates transcription. In addition to the remarkable functional repurposing of adenosylcobalamin from an enzyme cofactor to a light sensor, we find that nature also repurposed two independent protein modules in assembling CarH. These results expand the biological role of Vitamin B and provide fundamental insight into a new mode of light-dependent gene regulation.
URIhttp://hdl.handle.net/10261/141984
DOI10.1038/nature14950
Identifiersdoi: 10.1038/nature14950
issn: 1476-4687
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