A regulated two-step mechanism of TBP binding to DNA: A solvent-exposed surface of TBP inhibits TATA box recognition

Zhao, X. M., Herr, W. (March 2002) A regulated two-step mechanism of TBP binding to DNA: A solvent-exposed surface of TBP inhibits TATA box recognition. Cell, 108 (5). pp. 615-627. ISSN 0092-8674

URL: http://www.ncbi.nlm.nih.gov/pubmed/11893333
DOI: 10.1016/S0092-8674(02)00648-7

Abstract

The TATA box binding protein TBP plays a universally important role in eukaryotic nuclear transcription. By mutagenesis, we have discovered a solvent-exposed surface of the structured TBP core domain that is important for inhibition of the DNA binding and DNA-bending activities of full-length wild-type TBP. Full-length wild-type TBP initially binds the TATA box to form an unstable complex containing unbent DNA, and then it slowly forms a stable complex containing bent DNA. TFIIB greatly accelerates formation of a bent TFIIB-TBP-TATA box complex, and the inhibitory DNA binding surface of TBP contributes to the cooperativity of binding to TFIIB. Using TBP and TFIIB, we show that TBP can bind the TATA box through a regulated two-step mechanism, involving a transition from unbent complex to bent complex.

Item Type: Paper
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing
bioinformatics > genomics and proteomics
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > DNA binding protein
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
CSHL Authors:
Communities: CSHL labs > Herr lab
Depositing User: Matt Covey
Date: March 2002
Date Deposited: 16 Oct 2013 16:26
Last Modified: 16 Oct 2013 16:26
Related URLs:
URI: http://repository.cshl.edu/id/eprint/28820

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