Nucleic Acids Research, 1993, Vol. 21, No. 8 1789-1796
© 1993
MOLECULAR BIOLOGY |
Effect of the non-conserved N-terminus on the DNA binding activity of the yeast TATA binding protein
Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine Pittsburgh, PA 15261, USA
* To whom correspondence should be addressed
Received January 25, 1993. Revised March 12, 1993. Accepted March 12, 1993.
We have studied the DNA binding activity of recombinant yeast TATA Binding Protein (TBP) with particular interest in the role played by the non-conserved N-termlnal domain. By comparing the DNA binding activity of wild type yeast TBP with a mutant form of TBP that lacks the non-conserved N-termlnal domain (TBP
57), we have determined that the N-terminus of TBP alters both the shape and the stability of the TBP—DNA complex. Measurements of the DNA bending angle Indicate that the N-termlnus enhances the bending of the DNA that Is induced by TBP binding and greatly destabilizes the TBP—DNA complex during native gel electrophoresls. In solution, the N-termlnus has only a slight effect on the equilibrium dissociation constant and the dissociation rate constant. However, the N-termlnal domain reduces the association rate constant In a temperature dependent manner and Increases the apparent activation energy of the TBP—DNA complex formation by 3 kcal/mole. These data suggest that a conformational change involving the N-termlnus of TBP may be one of the Isomerizatlon steps In the formation of a stable TBP—DNA complex.
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