Histone Folds Mediate Selective Heterodimerization of Yeast TAFII25 with TFIID Components yTAFII47 and yTAFII65 and with SAGA Component ySPT7

doi:10.1128/MCB.21.5.1841-1853.2001

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Molecular and Cellular Biology, March 2001, p. 1841-1853, Vol. 21, No. 5
0270-7306/01/$04.00+0 DOI: 10.1128/MCB.21.5.1841-1853.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Histone Folds Mediate Selective Heterodimerization of Yeast TAF_II25 with TFIID Components yTAF_II47 and yTAF_II65 and with SAGA Component ySPT7

Yann-Gaël Gangloff,¹ Steven L. Sanders,² Christophe Romier,¹ Doris Kirschner,¹ P. Anthony Weil,² Laszlo Tora,¹ and Irwin Davidson¹^,^*

Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, Illkirch Cédex, C.U. de Strasbourg, France,¹ and Department of Molecular Physiology and Biophysics, Vanderbilt University School of Medicine, Nashville, Tennessee 37232²

Received 25 August 2000/Returned for modification 30 September 2000/Accepted 7 December 2000

We show that the yeast TFIID (yTFIID) component yTAF_II47 contains a histone fold domain (HFD) with homology to that previouslydescribed for hTAF_II135. Complementation in vivo indicates thatthe yTAF_II47 HFD is necessary and sufficient for vegetative growth.Mutation of highly conserved residues in the $alpha$ 1 helix of the yTAF_II47HFD results in a temperature-sensitive phenotype which can besuppressed by overexpression of yTAF_II25, as well as by yTAF_II40,yTAF_II19, and yTAF_II60. In yeast two-hybrid and bacterial coexpressionassays, the yTAF_II47 HFD selectively heterodimerizes with yTAF_II25,which we show contains an HFD with homology to the hTAF_II28 familyWe additionally demonstrate that yTAF_II65 contains a functionalHFD which also selectively heterodimerizes with yTAF_II25. Theseresults reveal the existence of two novel histone-like pairs inyTFIID. The physical and genetic interactions described here showthat the histone-like yTAF_IIs are organized in at least two substructureswithin TFIID rather than in a single octamer-like structure aspreviously suggested. Furthermore, our results indicate that ySPT7has an HFD homologous to that of yTAF_II47 which selectively heterodimerizeswith yTAF_II25, defining a novel histone-like pair in the SAGAcomplex.

^* Corresponding author. Mailing address: Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP,B.P. 163, 67404 Illkirch Cédex, C.U. de Strasbourg, France. Phone:33 3 88 65 34 40 (45). Fax: 33 3 88 65 32 01. E-mail: irwin{at}titus.u-strasbg.fr.

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