Functional analysis of the TFIID-specific yeast TAF4 (yTAFII48) reveals an unexpected organisation of its histone fold domain

doi:10.1074/jbc.M206556200

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Papers In Press, published online ahead of print September 16, 2002
J. Biol. Chem, 10.1074/jbc.M206556200
Submitted on July 2, 2002
Revised on September 4, 2002
Accepted on September 16, 2002

Functional analysis of the TFIID-specific yeast TAF4 (yTAFII48) reveals an unexpected organisation of its histone fold domain

Sylvie Thuault, Yann-Gael Gangloff, Jay Kirchner, Steven Sanders, Sebastiaan Werten, Christophe Romier, Peter Anthony Weil, and Irwin Davidson

I.G.B.M.C., Illkirch 67404

Corresponding Author: irwin{at}titus.u-strasbg.fr

Yeast TFIID comprises the TATA binding protein (TBP) and 14 TBP-associated factors (TAFIIs), nine of which contain histone fold domains (HFD). 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 alpha2 helix or the CCTD can be suppressed upon overexpression of yTAF12 (yTAFII68). Moreover, coexpression in E.coli indicates direct yTAF4-yTAF12 heterodimerisation 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 bone fide a3 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 organisation in which the alpha 3 helix is separated from the alpha 2 helix by an extended loop containing a conserved functional domain.

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