Open AccessThe engineering, structure, and DNA binding properties of a novel His4-type zinc finger peptide
Author(s) -
Yuichiro Hori,
Kazuo Suzuki,
Yasushi Okuno,
Makoto Nagaoka,
Shiroh Futaki,
Y. SUGIURA
Publication year - 2000
Publication title -
nucleic acids symposium series
Language(s) - English
Resource type - Journals
eISSN - 1746-8272
pISSN - 0261-3166
DOI - 10.1093/nass/44.1.295
Subject(s) - zinc finger , dna , zinc finger nuclease , lim domain , ring finger domain , peptide , protein–dna interaction , computational biology , chemistry , transcription factor , protein engineering , biophysics , dna binding protein , biology , biochemistry , gene , enzyme
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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom