The engineering, structure, and DNA binding properties of a novel His4-type zinc finger peptide.

Y. Hori; K. Suzuki; Y. Okuno; M. Nagaoka; S. Futaki; Y. Sugiura

doi:10.1093/nass/44.1.295

The engineering, structure, and DNA binding properties of a novel His4-type zinc finger peptide.

Y. Hori, K. Suzuki, Y. Okuno, M. Nagaoka, S. Futaki, Y. Sugiura

Research output: Contribution to journal › Article › peer-review

1 Citation (Scopus)

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.

Original language	English
Pages (from-to)	295-296
Number of pages	2
Journal	Nucleic acids symposium series
Issue number	44
DOIs	https://doi.org/10.1093/nass/44.1.295
Publication status	Published - 2000
Externally published	Yes

All Science Journal Classification (ASJC) codes

Medicine(all)

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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.",

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AU - Hori, Y.

AU - Suzuki, K.

AU - Okuno, Y.

AU - Nagaoka, M.

AU - Futaki, S.

AU - Sugiura, Y.

PY - 2000

Y1 - 2000

N2 - 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.

AB - 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.

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JO - Nucleic acids symposium series

JF - Nucleic acids symposium series

SN - 0261-3166

IS - 44

ER -

The engineering, structure, and DNA binding properties of a novel His4-type zinc finger peptide.

Abstract

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