English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/148377
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

Sub1 contacts the RNA polymerase II stalk to modulate mRNA synthesis

AutorGaravís, Miguel; González-Polo, Noelia; Allepuz-Fuster, Paula; Alegrio Louro, Jaime; Fernández-Tornero, Carlos ; Calvo, Olga
Fecha de publicación17-mar-2017
EditorOxford University Press
CitaciónNucleic Acids Research 45(5): 2458-2471(2017)
ResumenBiogenesis ofmessenger RNA is critically influenced by the phosphorylation state of the carboxy-terminal domain (CTD) in the largest RNA polymerase II(RNAPII) subunit. Several kinases and phosphatases are required to maintain proper CTD phosphorylation levels and, additionally, several other proteins modulate them, including Rpb4/7 and Sub1. The Rpb4/7 heterodimer, constituting the RNAPII stalk, promote phosphatase functions and Sub1 globally influences CTD phosphorylation, though its mechanism remains mostly unknown. Here, we show that Sub1 physically interacts with the RNAPII stalk domain,Rpb4/7, likely through its C-terminal region,and associates with Fcp1. While Rpb4 is not required for Sub1 interaction with RNAPII complex, a fully functional heterodimer is required for Sub1 association to promoters. We also demonstrate that a complete CTD is necessary for proper association of Sub1 to chromatin and to the RNAPII. Finally, genetic data show a functional relationship between Sub1 and the RNAPII clamp domain. Altogether, our results indicate that Sub1, Rpb4/7 and Fcp1 interaction modulates CTD phosphorylation. In addition, Sub1 interaction with Rpb4/7 can also modulate transcription start site selection and transcription elongation rate likely by influencing the clamp function.
Descripción14 p.-8 fig.
Versión del editorhttp://dx.doi.org/10.1093/nar/gkw1206
URIhttp://hdl.handle.net/10261/148377
DOI10.1093/nar/gkw1206
ISSN0305-1048
E-ISSN1362-4962
Aparece en las colecciones: (IBFG) Artículos
(CIB) Artículos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
Nuc.Ac.Res. 2017.pdfArtículo principal1,87 MBAdobe 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.