Zinc is required for folding and binding of a single zinc finger to DNA.
A synthetic peptide corresponding to zinc finger 31 of the Xenopus protein Xfin adopts a folded conformation in the presence of zinc. The same peptide in the absence of zinc is not folded in a stable tertiary conformation, as determined by NMR. Binding experiments have shown that the peptide binds non-specifically to DNA only in the presence of zinc. Moreover, competitive DNA binding experiments indicate interaction with 3.9 +/- 0.4 base pairs.
Lee
M S
MS
Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, CA 92037.
Gottesfeld
J M
JM
Wright
P E
PE
D000595:Amino Acid Sequence; D001483:Base Sequence; D004247:DNA / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D066298:In Vitro Techniques; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D011089:Polydeoxyribonucleotides / Q000378:metabolism; D015032:Zinc / Q000502:physiology*; D016335:Zinc Fingers
D004268:DNA-Binding Proteins; D010455:Peptides; D011089:Polydeoxyribonucleotides; C031156:poly d(I-C); D004247:DNA; D015032:Zinc