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rdf:type |
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lifeskim:mentions |
umls-concept:C0030956,
umls-concept:C0035820,
umls-concept:C0080347,
umls-concept:C0205147,
umls-concept:C0750502,
umls-concept:C0812304,
umls-concept:C0871161,
umls-concept:C1009388,
umls-concept:C1148673,
umls-concept:C1335858,
umls-concept:C1449308,
umls-concept:C1706548
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pubmed:issue |
7
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pubmed:dateCreated |
2005-2-15
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pubmed:abstractText |
The recent design strategy of zinc finger peptides has mainly focused on the alpha-helix region, which plays a direct role in DNA recognition. On the other hand, the study of non-DNA-contacting regions is extremely scarce. By swapping the beta-hairpin regions between the Sp1 and GLI zinc fingers, in this study, we investigated how the beta-hairpin region of the C(2)H(2)-type zinc finger peptides contributes to the DNA binding properties. Surprisingly, the Sp1 mutant with the GLI-type beta-hairpin had a higher DNA binding affinity than that of the wild-type Sp1. The result of the DNase I footprinting analyses also showed the change in the DNA binding pattern. In contrast, the GLI zinc finger completely lost DNA binding ability as a result of exchanging the beta-hairpin region. These results strongly indicate that the beta-hairpin region appears to function as a scaffold and has an important effect on the DNA binding properties of the C(2)H(2)-type zinc finger peptides.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0006-2960
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
22
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pubmed:volume |
44
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2523-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15709764-Amino Acid Sequence,
pubmed-meshheading:15709764-Circular Dichroism,
pubmed-meshheading:15709764-DNA Footprinting,
pubmed-meshheading:15709764-DNA Methylation,
pubmed-meshheading:15709764-DNA-Binding Proteins,
pubmed-meshheading:15709764-Deoxyribonuclease I,
pubmed-meshheading:15709764-Humans,
pubmed-meshheading:15709764-Hydrogen Bonding,
pubmed-meshheading:15709764-Molecular Sequence Data,
pubmed-meshheading:15709764-Oncogene Proteins,
pubmed-meshheading:15709764-Peptide Fragments,
pubmed-meshheading:15709764-Polymerase Chain Reaction,
pubmed-meshheading:15709764-Protein Binding,
pubmed-meshheading:15709764-Protein Conformation,
pubmed-meshheading:15709764-Protein Structure, Secondary,
pubmed-meshheading:15709764-Sp1 Transcription Factor,
pubmed-meshheading:15709764-Trans-Activators,
pubmed-meshheading:15709764-Transcription Factors,
pubmed-meshheading:15709764-Zinc Fingers
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pubmed:year |
2005
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pubmed:articleTitle |
Swapping of the beta-hairpin region between Sp1 and GLI zinc fingers: significant role of the beta-hairpin region in DNA binding properties of C2H2-type zinc finger peptides.
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pubmed:affiliation |
Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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