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The Isy1p component of the NineTeen complex interacts with the ATPase Prp16p to regulate the fidelity of pre-mRNA splicing.
Villa, Tommaso; Guthrie, Christine.
Afiliación
  • Villa T; Department of Biochemistry and Biophysics, University of California, San Francisco, 94143-2200, USA.
Genes Dev ; 19(16): 1894-904, 2005 Aug 15.
Article en En | MEDLINE | ID: mdl-16103217
ABSTRACT
Prp16p is a DEAH-box ATPase that transiently associates with the spliceosome to promote the structural transition required for the second chemical step. Yeast strains carrying the cold-sensitive allele prp16-302 stall the release of Prp16p at low temperatures, yet splice precursors with aberrant branchpoints at increased frequency. To identify new factors involved in the regulation of splicing fidelity, we sought suppressors of the prp16-302 growth phenotype. Deletion of the nonessential ISY1 gene (1) improves growth of prp16-302 strains, (2) alleviates stalling, and (3) restores fidelity of branchpoint usage to wild-type levels. Isy1p is a subunit of the NineTeen Complex containing Prp19p, an essential E3 ubiquitin ligase homolog required for splicing. Notably, Deltaisy1 PRP16 strains display reduced fidelity of 3'-splice site selection. Consistent with a recent two-state model of the spliceosome, our genetic and biochemical results suggest that Isy1p acts together with U6 snRNA to promote a spliceosomal conformation favorable for first-step chemistry. We propose that deletion of ISY1 favors the premature release of Prp16p, thus promoting second-step chemistry of precursors with inappropriate 3'-splice sites.
Asunto(s)

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Precursores del ARN / Procesamiento Postranscripcional del ARN / Empalme del ARN / Proteínas de Unión al ARN / Adenosina Trifosfatasas / Proteínas de Saccharomyces cerevisiae Tipo de estudio: Prognostic_studies Idioma: En Revista: Genes Dev Asunto de la revista: BIOLOGIA MOLECULAR Año: 2005 Tipo del documento: Article País de afiliación: Estados Unidos

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Precursores del ARN / Procesamiento Postranscripcional del ARN / Empalme del ARN / Proteínas de Unión al ARN / Adenosina Trifosfatasas / Proteínas de Saccharomyces cerevisiae Tipo de estudio: Prognostic_studies Idioma: En Revista: Genes Dev Asunto de la revista: BIOLOGIA MOLECULAR Año: 2005 Tipo del documento: Article País de afiliación: Estados Unidos