Abstract
We have created a novel His4-type zinc finger protein (H4Sp1) engineered by Cys-->His mutations of the Cys2His2-type zinc finger in transcription factor Sp1. The CD and NMR studies reveal that the His4 domain has Zn(II)-dependent folding properties and similar secondary structures to wild-type Cys2His2 domain. The DNA binding experiments demonstrate that H4Sp1 can bind DNA in a specific way. The present artificial peptide H4Sp1 will provide valuable information about the interaction between a metallopeptide and DNA.
MeSH terms
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Amino Acid Sequence
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Base Sequence
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Binding Sites / genetics
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Circular Dichroism
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DNA / genetics
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DNA / metabolism
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DNA-Binding Proteins / chemistry*
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DNA-Binding Proteins / genetics*
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DNA-Binding Proteins / metabolism
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Histidine / chemistry
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In Vitro Techniques
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Models, Molecular
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Nuclear Magnetic Resonance, Biomolecular
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Protein Engineering
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Protein Folding
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Protein Structure, Tertiary
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Sp1 Transcription Factor / chemistry*
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Sp1 Transcription Factor / genetics*
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Sp1 Transcription Factor / metabolism
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Zinc Fingers / genetics*
Substances
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DNA-Binding Proteins
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Sp1 Transcription Factor
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Histidine
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DNA