The engineering, structure, and DNA binding properties of a novel His4-type zinc finger peptide.
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.
Hori
Y
Y
Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.
Suzuki
K
K
Okuno
Y
Y
Nagaoka
M
M
Futaki
S
S
Sugiura
Y
Y
D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites / Q000235:genetics; D002942:Circular Dichroism; D004247:DNA / Q000235:genetics / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D006639:Histidine / Q000737:chemistry; D066298:In Vitro Techniques; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D019906:Nuclear Magnetic Resonance, Biomolecular; D015202:Protein Engineering; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D016329:Sp1 Transcription Factor / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D016335:Zinc Fingers / Q000235:genetics*
D004268:DNA-Binding Proteins; D016329:Sp1 Transcription Factor; D006639:Histidine; D004247:DNA