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Originally published In Press as doi:10.1074/jbc.M008208200 on October 16, 2000

J. Biol. Chem., Vol. 276, Issue 1, 395-405, January 5, 2001
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Mutations in the TATA-binding Protein, Affecting Transcriptional Activation, Show Synthetic Lethality with the TAF145 Gene Lacking the TAF N-terminal Domain in Saccharomyces cerevisiae*

Akiko Kobayashi, Tsuyoshi MiyakeDagger , Yoshifumi Ohyama, 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

The general transcription factor TFIID, which is composed of the TATA box-binding protein (TBP) and a set of TBP-associated factors (TAFs), is crucial for both basal and regulated transcription by RNA polymerase II. The N-terminal small segment of yeast TAF145 (yTAF145) binds to TBP and thereby inhibits TBP function. To understand the physiological role of this inhibitory domain, which is designated as TAND (TAF N-terminal domain), we screened mutations, synthetically lethal with the TAF145 gene lacking TAND (taf145Delta TAND), in Saccharomyces cerevisiae by exploiting a red/white colony-sectoring assay. Our screen yielded several recessive nsl (Delta TAND synthetic lethal) mutations, two of which, nsl1-1 and nsl1-2, define the same complementation group. The NSL1 gene was found to be identical to the SPT15 gene encoding TBP. Interestingly, both temperature-sensitive nsl1/spt15 alleles, which harbor the single amino acid substitutions, S118L and P65S, respectively, were defective in transcriptional activation in vivo. Several other previously characterized activation-deficient spt15 alleles also displayed synthetic lethal interactions with taf145Delta TAND, indicating that TAND and TBP carry an overlapping but as yet unidentified function that is specifically required for transcriptional regulation.

* This study was supported by grants from the Ministry of Education, Science, and Culture of Japan, by the CREST Japan Science and Technology Corp., the Uehara Memorial Foundation, the Asahi Glass Foundation, the NAITO Foundation, the Sumitomo Foundation, and NOVARTIS Foundation for the Promotion of Science.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.

Dagger Present address: Dept. of Biochemistry and Molecular Genetics, Health Sciences Center, University of Virginia, Charlottesville, VA 22908.

§ To whom correspondence should be addressed: Division of Gene Function in Animals, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0101, Japan. Tel.: 81-743-72-5531; Fax: 81-743-72-5539; E-mail: kokubo@bs.aist-nara.ac.jp.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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