Opposing effects of Ctk1 kinase and Fcp1 phosphatase at Ser 2 of the RNA polymerase II C-terminal domain

Eun Jung Cho, Michael S. Kobor, Minkyu Kim, Jack Greenblatt, Stephen Buratowski

Producción científica: Articlerevisión exhaustiva

342 Citas (Scopus)

Resumen

The C-terminal domain (CTD) of the RNA polymerase II (Pol II) largest subunit is hyperphosphorylated during transcription. Using an in vivo cross-linking/chromatin immunoprecipitation assay, we found previously that different phosphorylated forms of RNA Pol II predominate at different stages of transcription. At promoters, the Pol II CTD is phosphorylated at Ser 5 by the basal transcription factor TFIIH. However, in coding regions, the CTD is predominantly phosphorylated at Ser 2. Here we show that the elongation-associated phosphorylation of Ser 2 is dependent upon the Ctk1 kinase, a putative yeast homolog of Cdk9/P-TEFb. Furthermore, mutations in the Fcp1 CTD phosphatase lead to increased levels of Ser 2 phosphorylation. Both Ctk1 and Fcp1 cross-link to promoter and coding regions, suggesting that they associate with the elongating polymerase. Both Ctk1 and Fcp1 have been implicated in regulation of transcription elongation. Our results suggest that this regulation may occur by modulating levels of Ser 2 phosphorylation, which in turn, may regulate the association of elongation factors with the polymerase.

Idioma originalEnglish (US)
Páginas (desde-hasta)3319-3329
Número de páginas11
PublicaciónGenes and Development
Volumen15
N.º24
DOI
EstadoPublished - dic 15 2001
Publicado de forma externa

ASJC Scopus subject areas

  • Genetics
  • Developmental Biology

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