Requirement for TFIIH kinase activity in transcription by RNA polymerase II

1 October 1995

journal article
letter
Published by Springer Nature in Nature

Vol. 377 (6549) , 557-560
https://doi.org/10.1038/377557a0

Abstract

AN array of tandem heptapeptide repeats at the carboxv -terminal domain (CTD) of the largest subunit of RNA polymerase II constitute a highly conserved structure essential for viability^1á¤-3. Studies have established that the CTD is phosphorylated at different stages of the transcription cycle^4á¤-7, and that it may be involved in transcriptional regulation^8á¤-12. The exact role of the CTD remains elusive, as in vitro reconstituted transcription using the adenovirus major late promoter does not require the CTD^13,14. Previous studies^7,15,16 showed that transcription from the murine dihydro-folate reductase (DHFR) promoter can be only accomplished by the form of RNA polymerase II that contains the hypophosphoryl-ated CTD (RNAPIIA), but not by the form that lacks it (RNAPIIB)⁷. Here we show that the CTD, but not its phosphoryla-tion, is required for initiation of transcription. We also show that transcription requires CTD kinase activity provided by the CDK⁷ subunit of TFIIH^17á¤-19.

Keywords

RNA POLYMERASE II

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