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An integrated SAGA and TFIID PIC assembly pathway selective for poised and induced promoters.
Mittal, Chitvan; Lang, Olivia; Lai, William K M; Pugh, B Franklin.
Afiliación
  • Mittal C; Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, Pennsylvania 16801, USA.
  • Lang O; Department of Molecular Biology and Genetics, Cornell University, Ithaca, New York 14850, USA.
  • Lai WKM; Department of Molecular Biology and Genetics, Cornell University, Ithaca, New York 14850, USA.
  • Pugh BF; Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, Pennsylvania 16801, USA.
Genes Dev ; 36(17-18): 985-1001, 2022 09 01.
Article en En | MEDLINE | ID: mdl-36302553
Genome-wide, little is understood about how proteins organize at inducible promoters before and after induction and to what extent inducible and constitutive architectures depend on cofactors. We report that sequence-specific transcription factors and their tethered cofactors (e.g., SAGA [Spt-Ada-Gcn5-acetyltransferase], Mediator, TUP, NuA4, SWI/SNF, and RPD3-L) are generally bound to promoters prior to induction ("poised"), rather than recruited upon induction, whereas induction recruits the preinitiation complex (PIC) to DNA. Through depletion and/or deletion experiments, we show that SAGA does not function at constitutive promoters, although a SAGA-independent Gcn5 acetylates +1 nucleosomes there. When inducible promoters are poised, SAGA catalyzes +1 nucleosome acetylation but not PIC assembly. When induced, SAGA catalyzes acetylation, deubiquitylation, and PIC assembly. Surprisingly, SAGA mediates induction by creating a PIC that allows TFIID (transcription factor II-D) to stably associate, rather than creating a completely TFIID-independent PIC, as generally thought. These findings suggest that inducible systems, where present, are integrated with constitutive systems.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteínas de Saccharomyces cerevisiae / Factor de Transcripción TFIID Idioma: En Revista: Genes Dev Asunto de la revista: BIOLOGIA MOLECULAR Año: 2022 Tipo del documento: Article País de afiliación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteínas de Saccharomyces cerevisiae / Factor de Transcripción TFIID Idioma: En Revista: Genes Dev Asunto de la revista: BIOLOGIA MOLECULAR Año: 2022 Tipo del documento: Article País de afiliación: Estados Unidos