Different contributions of three zinc fingers of transcription factor Sp1 to DNA recognition: novel binding mode of N-terminal finger 1.
To clarify binding properties of the first zinc finger of Sp1, finger 1, to GC-box DNA, two-finger mutant peptides Sp1 (zf12) and Sp1 (zf23) were created and their DNA binding characteristics have been compared with those of native three-zinc finger protein Sp1. Some gel electrophoretic experiments involving DNase I footprinting and gel mobility shift assays reveal that finger 1 is not essential to sequence-specific DNA recognition, but moderately contributes to total binding affinity and overall sequence specificity by three zinc fingers of Sp1.
Saegusa
N
N
Institute for Chemical Research, Kyoto University, Japan.
Yokono
M
M
Matsushita
K
K
Sugiura
Y
Y
D000595:Amino Acid Sequence; D001482:Base Composition; D001483:Base Sequence; D001665:Binding Sites; D016384:Consensus Sequence; D003596:Cytosine; D004247:DNA / Q000737:chemistry* / Q000378:metabolism*; D018983:DNA Footprinting; D003850:Deoxyribonuclease I; D006147:Guanine; D008958:Models, Molecular; D009838:Oligodeoxyribonucleotides / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D016329:Sp1 Transcription Factor / Q000737:chemistry* / Q000378:metabolism*; D016335:Zinc Fingers
D009838:Oligodeoxyribonucleotides; D016329:Sp1 Transcription Factor; D006147:Guanine; D003596:Cytosine; D004247:DNA; D003850:Deoxyribonuclease I