Abstract
A 30-amino acid peptide, which corresponds to the second "zinc finger" domain of transcription factor IIIA, has been synthesized and purified. This peptide folds in the presence of zinc: adding Zn2+ significantly changes the circular dichroism spectrum, and Zn2+ protects the peptide from tryptic digestion. The peptide also binds Co2+, and the absorption spectrum of the Co2+ complex suggests that a tetrahedral binding site is formed by two cysteines and two histidines. Experiments at higher temperatures (60-75 degrees C) suggest that these folded metal-peptide complexes are quite thermostable. The peptide shows some sequence-specific effects in DNase and methylation protection experiments. However, it does not give a clear "footprint," and some effects are observed in the absence of added zinc.
Dates
Type | When |
---|---|
Created | 19 years, 2 months ago (May 31, 2006, 6:22 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 12:31 p.m.) |
Indexed | 1 month, 2 weeks ago (July 8, 2025, 10:07 a.m.) |
Issued | 38 years, 1 month ago (July 1, 1987) |
Published | 38 years, 1 month ago (July 1, 1987) |
Published Online | 38 years, 1 month ago (July 1, 1987) |
Published Print | 38 years, 1 month ago (July 1, 1987) |
@article{Frankel_1987, title={Metal-dependent folding of a single zinc finger from transcription factor IIIA.}, volume={84}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.84.14.4841}, DOI={10.1073/pnas.84.14.4841}, number={14}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Frankel, A D and Berg, J M and Pabo, C O}, year={1987}, month=jul, pages={4841–4845} }