Structural analysis of Rtt106p reveals a DNA binding role required for heterochromatin silencing.
J Biol Chem
; 285(6): 4251-4262, 2010 Feb 05.
Article
en En
| MEDLINE
| ID: mdl-20007951
ABSTRACT
Rtt106p is a Saccharomyces cerevisiae histone chaperone with roles in heterochromatin silencing and nucleosome assembly. The molecular mechanism by which Rtt106p engages in chromatin dynamics remains unclear. Here, we report the 2.5 A crystal structure of the core domain of Rtt106p, which adopts an unusual "double pleckstrin homology" domain architecture that represents a novel structural mode for histone chaperones. A histone H3-H4-binding region and a novel double-stranded DNA-binding region have been identified. Mutagenesis studies reveal that the histone and DNA binding activities of Rtt106p are involved in Sir protein-mediated heterochromatin formation. Our results uncover the structural basis of the diverse functions of Rtt106p and provide new insights into its cellular roles.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Heterocromatina
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Regulación Fúngica de la Expresión Génica
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Chaperonas Moleculares
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Proteínas de Saccharomyces cerevisiae
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Proteínas de Unión al ADN
Idioma:
En
Revista:
J Biol Chem
Año:
2010
Tipo del documento:
Article