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Published September 16, 1988 | public
Journal Article

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.

Additional Information

© 1988 American Association for the Advancement of Science. 15 June 1988; accepted 12 August 1988. We thank B. R. Reid and G. Drobny and their groups for use of NMR facilities; H. Charbonneau, S. Kumar, M. Harrylock, R. Wade, and K. Walsh for assistance with amino acid compositional analysis and for sequencing the peptide; and our colleagues D. Allison, J. Herriott, and B. M. Shapiro for their helpful comments on the manuscript.

Additional details

August 19, 2023
October 19, 2023