Metal ion binding to a zinc finger peptide containing the Cys-X2-Cys-X4-His-X4-Cys domain of a nucleic acid binding protein encoded by the Drosophila Fw-element

The metal binding properties of a 18-residue zinc finger peptide containing a CCHC box which reproduces one of the cysteine-rich domains of a putative nucleic acid binding protein encoded by the Fw transposable element from Drosophila melanogaster were investigated through electronic and 1H NMR spec...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 1998-01, Vol.242 (2), p.385-389
Main Authors: Bavoso, A, Ostuni, A, Battistuzzi, G, Menabue, L, Saladini, M, Sola, M
Format: Article
Language:English
Subjects:
animal breeding
animal genetics
animal physiology
Animals
arthropods
Cobalt - metabolism
Cysteine - chemistry
Cysteine - metabolism
DNA-Binding Proteins - chemistry
Drosophila melanogaster - chemistry
entomology
Histidine - chemistry
Histidine - metabolism
Magnetic Resonance Spectroscopy
Metals - metabolism
Peptide Fragments - metabolism
Protein Binding
Spectrophotometry
Zinc - metabolism
Zinc Fingers
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Summary:The metal binding properties of a 18-residue zinc finger peptide containing a CCHC box which reproduces one of the cysteine-rich domains of a putative nucleic acid binding protein encoded by the Fw transposable element from Drosophila melanogaster were investigated through electronic and 1H NMR spectroscopy. Dissociation constants of 2(+/- 1) x 10(-12) M and 4(+/- 1) x 10(-7) M were determined for the Zn2+ and Co2+ adduct, respectively. These values are similar to those for other CCHC-peptides investigated previously, although the length of the spacer between the second cysteine and the histidine apparently exerts some influence on the spectral properties and on the stability of the Co(2+)-peptide adduct. The 1H NMR spectrum of the present Co(2+)-derivative contains a number of well resolved hyperfine-shifted resonances between 350 and -50 ppm which arise from the metal binding residues and nearby groups. These peaks can in principle be profitably exploited to monitor protein-nucleic acid interactions.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1997.7974