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Originally published In Press as doi:10.1074/jbc.M203792200 on June 21, 2002

J. Biol. Chem., Vol. 277, Issue 35, 31761-31767, August 30, 2002
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p52 Mediates XPB Function within the Transcription/Repair Factor TFIIH*,

Anass JawhariDagger §, Jean-Philippe Lainé§, Sandy Dubaele, Valérie Lamour, Arnaud Poterszman, Frédéric Coin, Dino Moras, and Jean-Marc Egly

From the Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/Universite Louis Pasteur, B. P.10142, 67404 Illkirch Cedex, France

To further our understanding of the transcription/DNA repair factor TFIIH, we investigated the role of its p52 subunit in TFIIH function. Using a completely reconstituted in vitro transcription or nucleotide excision repair (NER) system, we show that deletion of the C-terminal region of p52 results in a dramatic reduction of TFIIH NER and transcription activities. This mutation prevents promoter opening and has no effect on the other enzymatic activities of TFIIH. Moreover, we demonstrate that intact p52 is needed to anchor the XPB helicase within TFIIH, providing an explanation for the transcription and NER defects observed with the mutant p52. We show that these two subunits physically interact and map domains involved in the interface. Taken together, our results show that the p52/Tfb2 subunit of TFIIH regulates the function of XPB through pair-wise interactions as described previously for p44 and XPD.

* This work was supported by grants from the Institut National de la Recherche et de la Santé, the Centre National de la Recherche Scientifique, and the Association pour la Recherche sur le Cancer and Grant QLG1-CT-1999-0081 from the European Economic Community.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains sequence alignment of human p52 with its orthologs. Alignments are shown of Homo sapiens p52 sequence with its eukaryotic counterparts: Mus musculus, Drosophila melanogaster, Saccharomyces cerevisiae, Saccharomyces pombe, and Caenorhabditis elegans. Conserved and strictly conserved residues are drawn in yellow and blue, respectively. Boxes I, II, III, IV, and V correspond to stretches of highly conserved residues. The sequences are numbered according to the human protein.

Dagger Recipient of the Egide/CNRS fellowship.

§ Both authors contributed equally to this work.

To whom correspondence should be addressed. E-mail: egly@igbmc.u-strasbg.fr.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.


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