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Maintenance of Heterochromatin by the Large Subunit of the CAF-1 Replication-Coupled Histone Chaperone Requires Its Interaction with HP1a Through a Conserved Motif.
Roelens, Baptiste; Clémot, Marie; Leroux-Coyau, Mathieu; Klapholz, Benjamin; Dostatni, Nathalie.
Afiliación
  • Roelens B; Institut Curie, Paris Sciences et Lettres Research University.
  • Clémot M; Centre national de la recherche scientifique, Unité mixte de recherche 3664, 75248, Paris, France 75005 Paris, France.
  • Leroux-Coyau M; Sorbonne Universités, Université Pierre-et-Marie-Curie, 75005 Paris, France.
  • Klapholz B; Institut Curie, Paris Sciences et Lettres Research University.
  • Dostatni N; Centre national de la recherche scientifique, Unité mixte de recherche 3664, 75248, Paris, France 75005 Paris, France.
Genetics ; 205(1): 125-137, 2017 01.
Article en En | MEDLINE | ID: mdl-27838630
In eukaryotic cells, the organization of genomic DNA into chromatin regulates many biological processes, from the control of gene expression to the regulation of chromosome segregation. The proper maintenance of this structure upon cell division is therefore of prime importance during development for the maintenance of cell identity and genome stability. The chromatin assembly factor 1 (CAF-1) is involved in the assembly of H3-H4 histone dimers on newly synthesized DNA and in the maintenance of a higher order structure, the heterochromatin, through an interaction of its large subunit with the heterochromatin protein HP1a. We identify here a conserved domain in the large subunit of the CAF-1 complex required for its interaction with HP1a in the Drosophila fruit fly. Functional analysis reveals that this domain is dispensable for viability but participates in two processes involving heterochromatin: position-effect variegation and long range chromosomal interactions during meiotic prophase. Importantly, the identification in the large subunit of CAF-1 of a domain required for its interaction with HP1 allows the separation of its functions in heterochromatin-related processes from its function in the assembly of H3-H4 dimers onto newly synthesized DNA.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Cromosómicas no Histona / Proteínas de Drosophila / Proteína 4 de Unión a Retinoblastoma Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: Genetics Año: 2017 Tipo del documento: Article Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Cromosómicas no Histona / Proteínas de Drosophila / Proteína 4 de Unión a Retinoblastoma Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: Genetics Año: 2017 Tipo del documento: Article Pais de publicación: Estados Unidos