Nucleic Acids Research, 1994, Vol. 22, No. 7 1179-1185
© 1994
MOLECULAR BIOLOGY |
Multimerization of the mouse TATA-binding protein (TBP) driven by its C-terminal conserved domain
Department of Biology, Faculty of Science, Chiba University 1–33 Yayoicho, Inage-ku, Chiba-263 1Department of Agricultual Chemistry, Faculty of Agriculture, Tokyo University of Agriculture Sakuraga-oka, Setagaya-ku, Tokyo-156 2Department of Biochemistry, Saitama Medical School, Moroyama Iruma-gun, Saitama-350, Japan
*To whom correspondence should be addressed
Received January 4, 1994. Revised March 9, 1994. Accepted March 9, 1994.
The conformatioal states of the mouse TATA-binding protein (TBP) in solution were studied. A histldlne tag and a factor Xa recognition site-carrying mouse TBP was expressed in E.coli, highly purified, and its fundamental functions as a TBP were demonstrated. We analyzed the molecular states of mouse TBP by gel filtration and glycerol gradient sedimentation, and found that TBP forms heterogeneous multimers in solution. Direct binding of TBP molecules to each other was proven by the far-Western procedure. Analyses using TBPs truncated at the N- and C-termlni demonstrated that the functionally important C-termlnal domain was responsible for homomultlmer formation, and the N-termlnal domain enhances multimerization. Furthermore, it was found that the TATA sequence dissociates homomultlmers, and only monomeric TBP binds to the TATA-box. We suggest that TBP shares structural motifs in the C-terminal conserved domain for intermolecular interaction and TATA-binding.
+Present address: Department of Biotechnology, Faculty of Engineering, Osaka University, 2-1 Yamada-oka. Suita-565, Japan
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