Nucleic Acids Research, Vol 25, Issue 15 3042-3050, Copyright © 1997 by Oxford University Press
AL Vuidepot, F Bontems, M Gervais, B Guiard, E Shechter and JY Lallemand
The DNA binding domain of the yeast transcriptional activator CYP1(HAP1)
contains a zinc-cluster structure. The structures of the DNA binding
domain-DNA complexes of two other zinc-cluster proteins (GAL4 and PPR1)
have been studied by X-ray crystallography. Their binding domains present,
besides the zinc cluster, a short linker peptide and a dimerization
element. They recognize, as homodimers, two rotationally symmetric CGG
trinucleotides, the linker peptide and the dimerization element playing a
crucial role in binding specificity. Surprisingly, CYP1 recognizes
degenerate forms of a direct repeat, CGGnnnTAnCGGnnnTA, and the role of its
linker is under discussion. To better understand the binding specificity of
CYP1, we have studied, by NMR, the interaction between the CYP1(55-126)
peptide and two DNA fragments derived from the CYC1 upstream activation
sequence 1B. Our data indicate that CYP1(55-126) interacts with a CGG and
with a thymine 5 bp downstream. The CGG trinucleotide is recognized by the
zinc cluster in the major groove, as for GAL4 and PPR1, and the thymine is
bound in the minor groove by the N-terminal region, which possesses a basic
stretch of arginyl and lysyl residues. This suggests that the CYP1(55-126)
N- terminal region could play a role in the affinity and/or specificity of
the interaction with its DNA targets, in contrast to GAL4 and PPR1.
ARTICLES
NMR analysis of CYP1(HAP1) DNA binding domain-CYC1 upstream activation sequence interactions: recognition of a CGG trinucleotide and of an additional thymine 5 bp downstream by the zinc cluster and the N- terminal extremity of the protein
Groupe de RMN, DCSO, Ecole Polytechnique, F91128 Palaiseau, France.
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  L.-C. Lai, A. L. Kosorukoff, P. V. Burke, and K. E. Kwast Metabolic-State-Dependent Remodeling of the Transcriptome in Response to Anoxia and Subsequent Reoxygenation in Saccharomyces cerevisiae. Eukaryot. Cell, September 1, 2006; 5(9): 1468 - 1489. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 L.-C. Lai, A. L. Kosorukoff, P. V. Burke, and K. E. Kwast Dynamical Remodeling of the Transcriptome during Short-Term Anaerobiosis in Saccharomyces cerevisiae: Differential Response and Role of Msn2 and/or Msn4 and Other Factors in Galactose and Glucose Media Mol. Cell. Biol., May 15, 2005; 25(10): 4075 - 4091. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. v. Helden, Alma. F. Rios, and J. Collado-Vides Discovering regulatory elements in non-coding sequences by analysis of spaced dyads Nucleic Acids Res., April 15, 2000; 28(8): 1808 - 1818. [Abstract] [Full Text] [PDF]
|
|