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Does TATA Matter? A Structural Exploration of the Selectivity Determinants in Its Complexes with TATA Box-binding Protein

Overview
Journal Biophys J
Publisher Cell Press
Specialty Biophysics
Date 1997 Aug 1
PMID 9251783
Citations 11
Authors
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Abstract

The binding of the TATA box-binding protein (TBP) to a TATA sequence in DNA is essential for eukaryotic basal transcription. TBP binds in the minor groove of DNA, causing a large distortion of the DNA helix. Given the apparent stereochemical equivalence of AT and TA basepairs in the minor groove, DNA deformability must play a significant role in binding site selection, because not all AT-rich sequences are bound effectively by TBP. To gain insight into the precise role that the properties of the TATA sequence have in determining the specificity of the DNA substrates of TBP, the solution structure and dynamics of seven DNA dodecamers have been studied by using molecular dynamics simulations. The analysis of the structural properties of basepair steps in these TATA sequences suggests a reason for the preference for alternating pyrimidine-purine (YR) sequences, but indicates that these properties cannot be the sole determinant of the sequence specificity of TBP. Rather, recognition depends on the interplay between the inherent deformability of the DNA and steric complementarity at the molecular interface.

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References
1.
Ravishanker G, Swaminathan S, Beveridge D, Lavery R, Sklenar H . Conformational and helicoidal analysis of 30 PS of molecular dynamics on the d(CGCGAATTCGCG) double helix: "curves", dials and windows. J Biomol Struct Dyn. 1989; 6(4):669-99. DOI: 10.1080/07391102.1989.10507729. View

2.
Wobbe C, Struhl K . Yeast and human TATA-binding proteins have nearly identical DNA sequence requirements for transcription in vitro. Mol Cell Biol. 1990; 10(8):3859-67. PMC: 360896. DOI: 10.1128/mcb.10.8.3859-3867.1990. View

3.
Hagerman P . Sequence-directed curvature of DNA. Annu Rev Biochem. 1990; 59:755-81. DOI: 10.1146/annurev.bi.59.070190.003543. View

4.
Lieberman P, Schmidt M, Kao C, Berk A . Two distinct domains in the yeast transcription factor IID and evidence for a TATA box-induced conformational change. Mol Cell Biol. 1991; 11(1):63-74. PMC: 359589. DOI: 10.1128/mcb.11.1.63-74.1991. View

5.
Zilliacus J, Wright A, Carlstedt-Duke J, Nilsson L, Gustafsson J . Modulation of DNA-binding specificity within the nuclear receptor family by substitutions at a single amino acid position. Proteins. 1995; 21(1):57-67. DOI: 10.1002/prot.340210107. View