Publikationsdatum:
1988-09-16
Beschreibung:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Parraga, G -- Horvath, S J -- Eisen, A -- Taylor, W E -- Hood, L -- Young, E T -- Klevit, R E -- New York, N.Y. -- Science. 1988 Sep 16;241(4872):1489-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3047872" target="_blank"〉PubMed〈/a〉
Schlagwort(e):
Circular Dichroism
;
DNA Mutational Analysis
;
*DNA-Binding Proteins
;
Magnetic Resonance Spectroscopy
;
Metalloproteins
;
Protein Conformation
;
Saccharomyces cerevisiae
;
Structure-Activity Relationship
;
*Transcription Factors
;
Zinc/*physiology
Print ISSN:
0036-8075
Digitale ISSN:
1095-9203
Thema:
Biologie
,
Chemie und Pharmazie
,
Informatik
,
Medizin
,
Allgemeine Naturwissenschaft
,
Physik
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