Biochemical characterization of the TATA-binding protein-Gal4 activation domain complex

20Citations
Citations of this article
17Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

It has been suggested that complexes between gene-specific activators and the TATA-binding protein (TBP) play an important role in the expression of many genes. However, few detailed studies of well defined activator-TBP complexes have been reported. An analysis of the biochemical properties of the complex formed by the acidic activation domain (AAD) of the yeast activator Gal4 and TBP is presented here. This is shown to be composed of two AAD and one TBP molecule. DNA binding experiments reveal that TATA-containing DNAs and the Gal4 AAD bind TBP competitively, suggesting that the AAD and TATA boxes recognize overlapping surfaces of TBP. The kinetics of the formation and dissociation of the AAD2-TBP complex is also probed. The impact of these findings on models for Gal4-mediated transcriptional activation is considered.

Cite

CITATION STYLE

APA

Xie, Y., Denison, C., Yang, S. H., Fancy, D. A., & Kodadek, T. (2000). Biochemical characterization of the TATA-binding protein-Gal4 activation domain complex. Journal of Biological Chemistry, 275(41), 31914–31920. https://doi.org/10.1074/jbc.M003760200

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free