English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/141984
COMPARTIR / IMPACTO:
Estadísticas
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:
Título

Structural basis for gene regulation by a B12-dependent photoreceptor

AutorJost, M.; Fernández-Zapata, J.; Polanco, M.C.; Ortiz-Guerrero, J.M. ; Chen, P.Y.T.; Kang, G.; Padmanabhan, Subramanian ; Elías-Arnanz, Montserrat; Drennan, C.L.
Fecha de publicación2015
CitaciónNature 526: 536- 541 (2015)
ResumenPhotoreceptor 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
Identificadoresdoi: 10.1038/nature14950
issn: 1476-4687
Aparece en las colecciones: (IQFR) Artículos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
accesoRestringido.pdf15,38 kBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo
 

Artículos relacionados:


NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.