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Originally published In Press as doi:10.1074/jbc.M206556200 on September 16, 2002

J. Biol. Chem., Vol. 277, Issue 47, 45510-45517, November 22, 2002
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Functional Analysis of the TFIID-specific Yeast TAF4 (yTAFII48) Reveals an Unexpected Organization of Its Histone-fold Domain*

Sylvie ThuaultDagger §, Yann-Gaël GangloffDagger ||, Jay Kirchner**, Steven Sanders**, Sebastiaan WertenDagger , Christophe RomierDagger , P. Anthony Weil**, and Irwin DavidsonDagger Dagger Dagger

From the Dagger  Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/Université Louis Pasteur, Boîte Postale 163-67404 Illkirch Cédex, Communauté Urbaine de Strasbourg, France, and the ** Department of Molecular Physiology and Biophysics, Vanderbilt University School of Medecine, Nashville, Tennessee 37232-0615

Yeast TFIID comprises the TATA binding protein and 14 TBP-associated factors (TAFIIs), nine of which contain histone-fold domains (HFDs). The C-terminal region of the TFIID-specific yTAF4 (yTAFII48) containing the HFD shares strong sequence similarity with Drosophila (d)TAF4 (dTAFII110) and human TAF4 (hTAFII135). A structure/function analysis of yTAF4 demonstrates that the HFD, a short conserved C-terminal domain (CCTD), and the region separating them are all required for yTAF4 function. Temperature-sensitive mutations in the yTAF4 HFD alpha 2 helix or the CCTD can be suppressed upon overexpression of yTAF12 (yTAFII68). Moreover, coexpression in Escherichia coli indicates direct yTAF4-yTAF12 heterodimerization optimally requires both the yTAF4 HFD and CCTD. The x-ray crystal structure of the orthologous hTAF4-hTAF12 histone-like heterodimer indicates that the alpha 3 region within the predicted TAF4 HFD is unstructured and does not correspond to the bona fide alpha 3 helix. Our functional and biochemical analysis of yTAF4, rather provides strong evidence that the HFD alpha 3 helix of the TAF4 family lies within the CCTD. These results reveal an unexpected and novel HFD organization in which the alpha 3 helix is separated from the alpha 2 helix by an extended loop containing a conserved functional domain.

* This work was partially supported by grants from CNRS, INSERM, the Hôpital Universitaire de Strasbourg, the Ministère de la Recherche et de la Technologie, the Association pour la Recherche contre le Cancer, the Ligue Nationale contre le Cancer, National Institutes of Health Grant GM52461 (to P. A. W.) and the Human Frontier Science Program Research Grant RG0196 (to I. D. and P. A. W.).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.

§ Supported by a fellowship from the Région Alsace.

Supported by a fellowship from the Ligue National Contre le Cancer.

|| Present address: The Friedrich Miescher Institute, Maulbeerstrasse 66, P.O. Box 2543, CH-4002 Basel, Switzerland.

Dagger Dagger To whom correspondence should be addressed. Tel.: 33-3-88-65-34-40-45; Fax: 33-3-88-65-32-01; E-mail: irwin@titus.u-strasbg.fr.

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