Resolution of transcription-induced hexasome-nucleosome complexes by Chd1 and FACT.
Mol Cell
; 84(18): 3423-3437.e8, 2024 Sep 19.
Article
em En
| MEDLINE
| ID: mdl-39270644
ABSTRACT
To maintain the nucleosome organization of transcribed genes, ATP-dependent chromatin remodelers collaborate with histone chaperones. Here, we show that at the 5' ends of yeast genes, RNA polymerase II (RNAPII) generates hexasomes that occur directly adjacent to nucleosomes. The resulting hexasome-nucleosome complexes are then resolved by Chd1. We present two cryoelectron microscopy (cryo-EM) structures of Chd1 bound to a hexasome-nucleosome complex before and after restoration of the missing inner H2A/H2B dimer by FACT. Chd1 uniquely interacts with the complex, positioning its ATPase domain to shift the hexasome away from the nucleosome. In the absence of the inner H2A/H2B dimer, its DNA-binding domain (DBD) packs against the ATPase domain, suggesting an inhibited state. Restoration of the dimer by FACT triggers a rearrangement that displaces the DBD and stimulates Chd1 remodeling. Our results demonstrate how chromatin remodelers interact with a complex nucleosome assembly and suggest how Chd1 and FACT jointly support transcription by RNAPII.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Saccharomyces cerevisiae
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Transcrição Gênica
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RNA Polimerase II
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Proteínas de Grupo de Alta Mobilidade
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Histonas
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Nucleossomos
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Microscopia Crioeletrônica
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Proteínas de Saccharomyces cerevisiae
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Fatores de Elongação da Transcrição
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Montagem e Desmontagem da Cromatina
Idioma:
En
Revista:
Mol Cell
Assunto da revista:
BIOLOGIA MOLECULAR
Ano de publicação:
2024
Tipo de documento:
Article
País de publicação:
Estados Unidos