Zinc-dependent structure of a single-finger domain of yeast ADR1.
In the proposed "zinc finger" DNA-binding motif, each repeat unit binds a zinc metal ion through invariant Cys and His residues and this drives the folding of each 30-residue unit into an independent nucleic acid-binding domain. To obtain structural information, we synthesized single and double zinc finger peptides from the yeast transcription activator ADR1, and assessed the metal-binding and DNA-binding properties of these peptides, as well as the solution structure of the metal-stabilized domains, with the use of a variety of spectroscopic techniques. A single zinc finger can exist as an independent structure sufficient for zinc-dependent DNA binding. An experimentally determined model of the single finger is proposed that is consistent with circular dichroism, one- and two-dimensional nuclear magnetic resonance, and visual spectroscopy of the single-finger peptide reconstituted in the presence of zinc.
D002942:Circular Dichroism; D004252:DNA Mutational Analysis; D004268:DNA-Binding Proteins; D009682:Magnetic Resonance Spectroscopy; D008667:Metalloproteins; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae; D013329:Structure-Activity Relationship; D014157:Transcription Factors; D015032:Zinc / Q000502:physiology*
D004268:DNA-Binding Proteins; D008667:Metalloproteins; D014157:Transcription Factors; D015032:Zinc