Skip to Main content Skip to Navigation
Journal articles

A Role for the TFIIH XPB DNA Helicase in Promoter Escape by RNA Polymerase II

Abstract : TFIIH is an RNA polymerase II transcription factor that performs ATP-dependent functions in both transcription initiation, where it catalyzes formation of the open complex, and in promoter escape, where it suppresses arrest of the early elongation complex at promoter -proximal sites. TFIIH possesses three known ATP-dependent activities: a 3 3 5 DNA helicase catalyzed by its XPB subunit, a 5 3 3 DNA helicase catalyzed by its XPD subunit, and a carboxyl-terminal domain (CTD) ki-nase activity catalyzed by its CDK7 subunit. In this report , we exploit TFIIH mutants to investigate the contributions of TFIIH DNA helicase and CTD kinase activities to efficient promoter escape by RNA polymer-ase II in a minimal transcription system reconstituted with purified polymerase and general initiation factors. Our findings argue that the TFIIH XPB DNA helicase is primarily responsible for preventing premature arrest of early elongation intermediates during exit of polymerase from the promoter.
Complete list of metadata

Cited literature [41 references]  Display  Hide  Download
Contributor : Franck TIRODE Connect in order to contact the contributor
Submitted on : Tuesday, January 14, 2020 - 11:53:54 AM
Last modification on : Tuesday, October 19, 2021 - 12:51:51 PM
Long-term archiving on: : Wednesday, April 15, 2020 - 4:18:14 PM


 Restricted access
To satisfy the distribution rights of the publisher, the document is embargoed until : jamais

Please log in to resquest access to the document




Rodney J Moreland, Franck Tirode, Qin Yan, Joan Weliky Conaway, Jean-Marc Egly, et al.. A Role for the TFIIH XPB DNA Helicase in Promoter Escape by RNA Polymerase II. Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 1999, 274 (32), pp.22127-22130. ⟨10.1074/jbc.274.32.22127⟩. ⟨inserm-02438579⟩



Record views