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Molecular and Cellular Biology, April 2004, p. 3089-3099, Vol. 24, No. 8
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.8.3089-3099.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Autonomous Function of the Amino-Terminal Inhibitory Domain of TAF1 in Transcriptional Regulation

Shinya Takahata,1 Koji Kasahara,1 Masashi Kawaichi,2 and Tetsuro Kokubo1*

Division of Molecular and Cellular Biology, Graduate School of Integrated Science, Yokohama City University, Yokohama 230-0045,1 Division of Gene Function in Animals, Nara Institute of Science and Technology, Ikoma 630-0192, Japan2

Received 26 August 2003/ Returned for modification 8 October 2003/ Accepted 13 January 2004

The general transcription factor TFIID is composed of TATA-binding protein (TBP) and 14 TBP-associated factors (TAFs). TFIID mediates the transcriptional activation of a subset of eukaryotic promoters. The N-terminal domain (TAND) of TAF1 protein (Taf1p) inhibits TBP by binding to its concave and convex surfaces. This study examines the role of the TAND in transcriptional regulation and tests whether the TAND is an autonomous regulator of TBP. The TAND binds to and regulates TBP function when it is fused to the amino or carboxy terminus of Taf1p, the amino or carboxy terminus of Taf5p, or the amino terminus of Taf11p. However, a carboxy-terminal fusion of the TAND and Taf11p is not compatible with several other TAF proteins, including Taf1p, in the TFIID complex. These results indicate that there is no or minimal geometric constraint on the ability of the TAND to function normally in transcriptional regulation as long as TFIID assembly is secured.

* Corresponding author. Mailing address: Division of Molecular and Cellular Biology, Graduate School of Integrated Science, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan. Phone: 045-508-7237. Fax: 045-508-7369. E-mail: kokubo{at}tsurumi.yokohama-cu.ac.jp.

Molecular and Cellular Biology, April 2004, p. 3089-3099, Vol. 24, No. 8
0022-538X/04/$08.00+0     DOI: 10.1128/MCB.24.8.3089-3099.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Takahashi, H., Kasahara, K., Kokubo, T. (2009). Saccharomyces cerevisiae Med9 comprises two functionally distinct domains that play different roles in transcriptional regulation. GENES CELLS 14: 53-67 [Abstract] [Full Text]  
  • Kasahara, K., Ki, S., Aoyama, K., Takahashi, H., Kokubo, T. (2008). Saccharomyces cerevisiae HMO1 interacts with TFIID and participates in start site selection by RNA polymerase II. Nucleic Acids Res 36: 1343-1357 [Abstract] [Full Text]  
  • Mal, T. K., Takahata, S., Ki, S., Zheng, L., Kokubo, T., Ikura, M. (2007). Functional Silencing of TATA-binding Protein (TBP) by a Covalent Linkage of the N-terminal Domain of TBP-associated Factor 1. J. Biol. Chem. 282: 22228-22238 [Abstract] [Full Text]  


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