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J Biol Chem, Vol. 273, Issue 48, 32254-32264, November 27, 1998

Identification of Highly Conserved Amino-terminal Segments of dTAF_II230 and yTAF_II145 That Are Functionally Interchangeable for Inhibiting TBP-DNA Interactions in Vitro and in Promoting Yeast Cell Growth in Vivo

Tomohiro Kotani, Tsuyoshi Miyake, Yoshihiro Tsukihashi, Alan G. Hinnebusch^§, Yoshihiro Nakatani^¶, Masashi Kawaichi, and Tetsuro Kokubo

From the  Division of Gene Function in Animals, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0101, Japan and the Laboratories of ^§ Eukaryotic Gene Regulation and ^¶ Molecular Growth Regulation, NICHD, National Institutes of Health, Bethesda, Maryland 20892

TFIID is a multiprotein complex composed of TBP and several TAF_IIs. Small amino-terminal segments (TAF N-terminal domain (TAND)) of Drosophila TAF_II230 (dTAF_II230) and yeast TAF_II145 (yTAF_II145) bind strongly to TBP and inhibit TBP-DNA interactions. yTAF_II145 TAND (yTAND) was divided into two subdomains, yTANDI_10-37 and yTANDII_46-71, that function cooperatively. Here, we identify dTANDII within the amino terminus of dTAF_II230 at 118-143 amino acids in addition to dTANDI_18-77, reported previously. dTANDII exhibits pronounced sequence similarity to yTANDII, and the two were shown to be functionally equivalent in binding to TBP and inhibiting TBP-DNA interactions in vitro. Alanine scanning mutation analysis demonstrated that Phe-57 (yTANDII) and Tyr-129 (dTANDII) are critically required for the interaction with TBP.

Yeast strains containing mutant yTAF_II145 lacking yTANDI or yTANDII showed a temperature-sensitive growth phenotype. The conserved core of dTANDII could substitute for the yTANDII core, and Phe-57 or Tyr-129 described above was critically required for the function of this segment in promoting normal cell growth at 37 °C. In these respects, the impact of yTANDII mutations on cell growth paralleled their effects on TBP binding in vitro, strongly suggesting that the yTAF_II145-TBP interaction and its negative effects on TFIID binding to core promoters are physiologically important.

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