Structural basis for gene regulation by a B12-dependent photoreceptor

Marco Jost, Jésus Fernández-Zapata, María Carmen Polanco, Juan Manuel Ortiz-Guerrero, Percival Yang-Ting Chen, Gyunghoon Kang, S. Padmanabhan (), Montserrat Elías-Arnanz () and Catherine L. Drennan ()
Additional contact information
Marco Jost: Massachusetts Institute of Technology
Jésus Fernández-Zapata: Instituto de Química Física “Rocasolano”, Consejo Superior de Investigaciones Científicas
María Carmen Polanco: Area of Genetics (Unidad Asociada al Instituto de Química Física “Rocasolano”, Consejo Superior de Investigaciones Científicas), Faculty of Biology, Universidad de Murcia
Juan Manuel Ortiz-Guerrero: Area of Genetics (Unidad Asociada al Instituto de Química Física “Rocasolano”, Consejo Superior de Investigaciones Científicas), Faculty of Biology, Universidad de Murcia
Percival Yang-Ting Chen: Massachusetts Institute of Technology
Gyunghoon Kang: Massachusetts Institute of Technology
S. Padmanabhan: Instituto de Química Física “Rocasolano”, Consejo Superior de Investigaciones Científicas
Montserrat Elías-Arnanz: Area of Genetics (Unidad Asociada al Instituto de Química Física “Rocasolano”, Consejo Superior de Investigaciones Científicas), Faculty of Biology, Universidad de Murcia
Catherine L. Drennan: Massachusetts Institute of Technology

Nature, 2015, vol. 526, issue 7574, 536-541

Abstract: Abstract 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 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 B12 and provide fundamental insight into a new mode of light-dependent gene regulation.

Date: 2015
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DOI: 10.1038/nature14950

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