Abstract
It has been demonstrated that coupling a host-guest complex formation onto the DNA binding ability of short peptides gave raise a cooperative DNA binding by short peptide dimers. This strategy was extend to study the DNA binding by oligomers of short peptide. An amino acid bearing the adamantyl group was incorporated at the N-terminal of a peptide derived from the basic region of a yeast transcription activator GCN4, and beta-cyclodextrin was attached at the C-terminal cysteine residue in the same peptide chain. DNA binding of the peptide with both host and guest molecules to tandemly repeated DNA sequences was studied by gel shift assay.
MeSH terms
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Amino Acid Sequence
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Base Sequence
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Binding Sites
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Cyclodextrins
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DNA / chemistry
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DNA / genetics
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DNA / metabolism*
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DNA-Binding Proteins*
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Fungal Proteins / chemistry
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Fungal Proteins / genetics
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Fungal Proteins / metabolism
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Molecular Sequence Data
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Oligopeptides / chemistry
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Oligopeptides / genetics
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Oligopeptides / metabolism*
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Peptide Fragments / chemistry
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Peptide Fragments / genetics
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Peptide Fragments / metabolism
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Protein Binding
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Protein Kinases / chemistry
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Protein Kinases / genetics
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Protein Kinases / metabolism
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Repetitive Sequences, Nucleic Acid
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Saccharomyces cerevisiae Proteins*
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Trans-Activators / chemistry
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Trans-Activators / genetics
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Trans-Activators / metabolism
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beta-Cyclodextrins*
Substances
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Cyclodextrins
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DNA-Binding Proteins
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Fungal Proteins
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Oligopeptides
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Peptide Fragments
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Saccharomyces cerevisiae Proteins
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Trans-Activators
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beta-Cyclodextrins
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DNA
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Protein Kinases
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betadex