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Molecular recognition: monomer of the yeast transcriptional activator GCN4 recognizes its dimer DNA binding target sites specifically

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Abstract

It is widely believed that dimerization is a requirement for the yeast transcriptional activator GCN4 to recognize its specific DNA target sites. We used the basic region (226-252) of the yeast transcriptional activator GCN4, as both a monomeric peptide and a disulfide-linked dimer to investigate the interaction of the peptides with the DNA target sites AP-1 and CRE. CD and ITC experiments indicate that although the monomeric peptide GCN4-M has a weaker affinity with the DNA relative to the disulfide-linked dimer peptide GCN4-D, it recognizes AP-1 and CRE target sites specifically.

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Authors and Affiliations

  1. Institute of Physical Chemistry, College of Chemistry and Molecular Engineering, Peking University, 100871, Beijing, China

    Cao Wei, Liu Liang, Lai Luhua & Tang Youqi

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  1. Cao Wei
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  2. Liu Liang
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  3. Lai Luhua
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  4. Tang Youqi
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Correspondence to Lai Luhua.

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Cao, W., Liu, L., Lai, L. et al. Molecular recognition: monomer of the yeast transcriptional activator GCN4 recognizes its dimer DNA binding target sites specifically. Sc. China Ser. B-Chem. 43, 466–476 (2000). https://doi.org/10.1007/BF02969492

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  • DOI: https://doi.org/10.1007/BF02969492

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