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Science 16 September 1988:
Vol. 241. no. 4872, pp. 1489 - 1492
DOI: 10.1126/science.3047872
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Articles

Science, Vol 241, Issue 4872, 1489-1492
Copyright © 1988 by American Association for the Advancement of Science

articles

Zinc-dependent structure of a single-finger domain of yeast ADR1

G Parraga, SJ Horvath, A Eisen, WE Taylor, L Hood, ET Young, and RE Klevit

Department of Biochemistry, University of Washington, Seattle 98195.

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.


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