Structural basis for gene regulation by a B12-dependent photoreceptor

Jost, Marco; Fernández-Zapata, Jésus; Polanco, María Carmen; Ortiz-Guerrero, Juan Manuel; Chen, Percival Yang-Ting; Kang, Gyunghoon; Padmanabhan, S.; Elías-Arnanz, Montserrat; Drennan, Catherine L.

doi:10.1038/nature14950

Title: Structural basis for gene regulation by a B₁₂-dependent photoreceptor

Journal Article · Mon Sep 28 00:00:00 EDT 2015 · Nature (London)

DOI:https://doi.org/10.1038/nature14950· OSTI ID:1225071

Jost, Marco ^[1]; Fernández-Zapata, Jésus ^[2]; Polanco, María Carmen ^[3]; Ortiz-Guerrero, Juan Manuel ^[3]; Chen, Percival Yang-Ting ^[1]; Kang, Gyunghoon ^[1]; Padmanabhan, S. ^[2]; Elías-Arnanz, Montserrat ^[3]; Drennan, Catherine L. ^[4]

Massachusetts Inst. of Technology (MIT), Cambridge, MA (United States). Dept. of Chemistry
Spanish National Research Council (CSIC), Madrid (Spain). Inst. of Physical Chemistry "Rocasolano"
Univ. of Murcia (Spain). Faculty of Biology. Dept. of Genetics and Microbiology. Area of Genetics
Massachusetts Inst. of Technology (MIT), Cambridge, MA (United States). Dept. of Chemistry. Dept. of Biology. Howard Hughes Medical Inst.

Photoreceptor proteins enable organisms to sense and respond to light. The newly discovered CarH-type photoreceptors use a vitamin B₁₂ derivative, adenosylcobalamin, as the light-sensing chromophore to mediate light-dependent gene regulation. Here in this paper, 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. Finally, these results expand the biological role of vitamin B₁₂ and provide fundamental insight into a new mode of light-dependent gene regulation.

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Research Organization:: Massachusetts Inst. of Technology (MIT), Cambridge, MA (United States); Spanish National Research Council (CSIC), Madrid (Spain); Univ. of Murcia (Spain)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER); National Inst. of Health (NIH) (United States); Ministry of Economy and Competitiveness (Spain); Spanish National Research Council (CSIC) (Spain)

Grant/Contract Number:: AC02-76SF00515; AC02-06CH11357; GM069857; P41GM103393; P41GM103403; BFU2012-40184-C02-01; BFU2012-40184-C02-02

OSTI ID:: 1225071

Journal Information:: Nature (London), Vol. 526, Issue 7574; ISSN 0028-0836

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 124 works

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Title: Structural basis for gene regulation by a B12-dependent photoreceptor

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Title: Structural basis for gene regulation by a B₁₂-dependent photoreceptor