Your browser doesn't support javascript.
loading
Structural and functional characterization of the RBBP4-ZNF827 interaction and its role in NuRD recruitment to telomeres.
Yang, Sile F; Sun, Ai-Ai; Shi, Yunyu; Li, Fudong; Pickett, Hilda A.
Afiliación
  • Yang SF; Telomere Length Regulation Unit, Children's Medical Research Institute, Sydney Medical School, Faculty of Medicine, University of Sydney, Westmead, NSW 2145, Australia.
  • Sun AA; Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, China.
  • Shi Y; Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, China.
  • Li F; Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, China lifudong@ustc.edu.cn hpickett@cmri.org.au.
  • Pickett HA; Telomere Length Regulation Unit, Children's Medical Research Institute, Sydney Medical School, Faculty of Medicine, University of Sydney, Westmead, NSW 2145, Australia lifudong@ustc.edu.cn hpickett@cmri.org.au.
Biochem J ; 475(16): 2667-2679, 2018 08 31.
Article en En | MEDLINE | ID: mdl-30045876
The nucleosome remodeling and histone deacetylase (NuRD) complex is an essential multi-subunit protein complex that regulates higher-order chromatin structure. Cancers that use the alternative lengthening of telomere (ALT) pathway of telomere maintenance recruit NuRD to their telomeres. This interaction is mediated by the N-terminal domain of the zinc-finger protein ZNF827. NuRD-ZNF827 plays a vital role in the ALT pathway by creating a molecular platform for recombination-mediated repair. Disruption of NuRD binding results in loss of ALT cell viability. Here, we present the crystal structure of the NuRD subunit RBBP4 bound to the N-terminal 14 amino acids of ZNF827. RBBP4 forms a negatively charged channel that binds to ZNF827 through a network of electrostatic interactions. We identify the precise amino acids in RBBP4 required for this interaction and demonstrate that disruption of these residues prevents RBBP4 binding to both ZNF827 and telomeres, but is insufficient to decrease ALT activity. These data provide insights into the structural and functional determinants of NuRD activity at ALT telomeres.
Asunto(s)
Palabras clave
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Unión al ADN / Complejo Desacetilasa y Remodelación del Nucleosoma Mi-2 / Proteína 4 de Unión a Retinoblastoma Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: Biochem J Año: 2018 Tipo del documento: Article País de afiliación: Australia Pais de publicación: Reino Unido
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Unión al ADN / Complejo Desacetilasa y Remodelación del Nucleosoma Mi-2 / Proteína 4 de Unión a Retinoblastoma Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: Biochem J Año: 2018 Tipo del documento: Article País de afiliación: Australia Pais de publicación: Reino Unido