Zinc-Dependent Structure of a Single-Finger Domain of Yeast ADR1
SciencePublished 16 September 1988
Grace Párraga, Suzanna J. Horvath, Amur Eisen, Wayne E. Taylor, Leroy Hood, Elton T. Young
Citations315
SJR quartileQ1
SJR score10.42
SNIP6.62
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TL;DR
An experimentally determined model of thesingle 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.
Abstract
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.
Keywords
Biochemistry, Genetics and Molecular Biology
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