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J Biol Chem, Vol. 274, Issue 32, 22127-22130, August 6, 1999

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

Rodney J. Moreland, Franck Tirode^§, Qin Yan^¶, Joan Weliky Conaway^¶, Jean-Marc Egly^§, and Ronald C. Conaway

From the  Program in Molecular and Cell Biology, Oklahoma Medical Research Foundation, Oklahoma City, Oklahoma 73104, the ^§ Institut de Genetique et de Biologie Moleculaire et Cellulaire, CNRS/INSERM/ULP, B. P. 163, Illkirch, C.U. de Strasbourg, France, the ^¶ Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73190, and the  Howard Hughes Medical Institute, Oklahoma Medical Research Foundation, Oklahoma City, Oklahoma 73104

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'  5' DNA helicase catalyzed by its XPB subunit, a 5'  3' DNA helicase catalyzed by its XPD subunit, and a carboxyl-terminal domain (CTD) kinase 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 polymerase 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.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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