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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
TAFII25 with TFIID Components yTAFII47 and
yTAFII65 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
yTAFII47 contains a histone fold domain (HFD) with homology
to that previously described for hTAFII135. Complementation
in vivo indicates that the yTAFII47 HFD is necessary and
sufficient for vegetative growth. Mutation of highly conserved residues
in the
1 helix of the yTAFII47 HFD results in a
temperature-sensitive phenotype which can be suppressed by
overexpression of yTAFII25, as well as by
yTAFII40, yTAFII19, and yTAFII60.
In yeast two-hybrid and bacterial coexpression assays, the
yTAFII47 HFD selectively heterodimerizes with
yTAFII25, which we show contains an HFD with homology to
the hTAFII28 family We additionally demonstrate that
yTAFII65 contains a functional HFD which also selectively
heterodimerizes with yTAFII25. These results reveal the
existence of two novel histone-like pairs in yTFIID. The physical and
genetic interactions described here show that the histone-like
yTAFIIs are organized in at least two substructures within TFIID rather than in a single octamer-like structure as previously suggested. Furthermore, our results indicate that ySPT7 has
an HFD homologous to that of yTAFII47 which selectively
heterodimerizes with yTAFII25, defining a novel
histone-like pair in the SAGA complex.
*
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.
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.
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