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J. Biol. Chem., Vol. 275, Issue 41, 31963-31971, October 13, 2000
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From the In an effort to understand the structure function
relationship of TFIIH, a transcription/repair factor, we focused our
attention on the p44 subunit, which plays a central role in both
mechanisms. The amino-terminal portion of p44 has been shown to be
involved in the regulation of the XPD helicase activity; here we
show that its carboxyl-terminal domain is essential for TFIIH
transcription activity and that it binds three zinc atoms through two
independent modules. The first contains a C4 zinc finger motif, whereas
the second is characterized by a
CX2CX2-4FCADCD
motif, corresponding to interleaved zinc binding sites. The solution
structure of this second module reveals an unexpected homology with the
regulatory domain of protein kinase C and provides a framework to study
its role at the molecular level.
The atomic coordinates and the structure factors (code 1e53) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/). This work is dedicated to the memory of Jean-François
Lefèvre.
Structural Characterization of the Cysteine-rich Domain of
TFIIH p44 Subunit*
§¶,
,,,,, and
Institut de Génétique et de
Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, 1, rue
Laurent Fries, Boite Postale 163, 67404 Illkirch Cedex,
Communaunté Urbaine de Strasbourg, Laboratoire de
Résonance Magnétique Nucleaire, CNRS-UPR 9004, Ecole
Supérieure de Biotechnologie de Strasbourg, 67400 Illkirch-Graffenstaden, and ** Laboratoire de Spectrométrie de
Masse Bio-Organique, CNRS-UMR 7509/ULP, 1, rue Blaise Pascal,
67008 Strasbourg, France
*
This work was supported by INSERM, CNRS, l'Hopital
Universitaire de Strasbourg, l'Association de la Recherche contre le
Cancer, and the Conseil Général d'Alsace for the financing
of a Quattro II spectrometer and the TMR network (peptide and protein
structure elucidation by mass spectrometry (European Community Contract ERBCHRXCT940425)).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.
To whom correspondence should be addressed. Tel.: 33 3 88 65 32 20; Fax: 33 3 88 65 32 76; E-mail: moras@igbmc.u-strasbg.fr.
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