title: Metal binding and DNA recognition in transcription factor Sp1.
abstract: DNA binding domain of Sp1 encompassing three Cys2His2-type Zn-finger motifs is cloned and expressed in E.coli. The Sp1 fragment shows metal-dependent folding and DNA binding. The Zn(II)-induced folding of the three fingers is probably cooperative. Release of one equivalent of Zn decreases but does not abolish DNA binding activity of Sp1.
authors.affiliation: Institute for Chemical Research, Kyoto University, Japan.
authors.forename: J
authors.initials: J
authors.lastname: Kuwahara
authors.forename: M
authors.initials: M
authors.lastname: Futamura
authors.forename: N
authors.initials: N
authors.lastname: Sogo
authors.forename: A
authors.initials: A
authors.lastname: Yonezawa
authors.forename: Y
authors.initials: Y
authors.lastname: Sugiura
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D004247:DNA / Q000378:metabolism*; D008969:Molecular Sequence Data; D016329:Sp1 Transcription Factor / Q000378:metabolism*; D015032:Zinc / Q000378:metabolism*; D016335:Zinc Fingers
chemical_list: D016329:Sp1 Transcription Factor; D004247:DNA; D015032:Zinc