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Sequence-specific DNA binding by glucocorticoid receptor "zinc finger peptides".
Author(s) -
Trevor Archer,
Gordon L. Hager,
James G. Omichinski
Publication year - 1990
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.87.19.7560
Subject(s) - zinc finger , hormone response element , dna , glucocorticoid receptor , dna binding domain , ring finger domain , biochemistry , biology , dna binding protein , zinc finger nuclease , lim domain , dna binding site , peptide , binding site , chemistry , microbiology and biotechnology , transcription factor , receptor , genetics , gene , estrogen receptor , promoter , gene expression , cancer , breast cancer
Steroid hormone receptors can activate or repress transcription from responsive loci by binding to DNA. We have examined the mechanism of DNA binding by individually synthesizing the putative "zinc finger peptides" from the rat glucocorticoid receptor. Atomic absorption studies show that the peptides will bind zinc on an equimolar basis, and circular dichroism experiments demonstrate a significant alteration in secondary structure in the presence of zinc. The results from a series of experiments establish that metal ion is required for binding to DNA and that the amino-terminal zinc finger shows a significantly greater affinity for glucocorticoid response element-containing DNA over control DNA. These observations indicate that a single synthetic "zinc finger peptide" is able to bind to DNA in a sequence-specific manner.

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