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Science 21 February 1992:
Vol. 255. no. 5047, pp. 979 - 983
DOI: 10.1126/science.1312255
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Articles

Science, Vol 255, Issue 5047, 979-983
Copyright © 1992 by American Association for the Advancement of Science

articles

Molecular characterization of helix-loop-helix peptides

SJ Anthony-Cahill, PA Benfield, R Fairman, ZR Wasserman, SL Brenner, WF Stafford 3rd, C Altenbach, WL Hubbell, and WF DeGrado

Biotechnology Department, DuPont Merck Pharmaceutical Co., Wilmington, DE 19880-0328.

A class of regulators of eukaryotic gene expression contains a conserved amino acid sequence responsible for protein oligomerization and binding to DNA. This structure consists of an arginine- and lysine-rich basic region followed by a helix-loop-helix motif, which together mediate specific binding to DNA. Peptides were prepared that span this motif in the MyoD protein; in solution, they formed alpha-helical dimers and tetramers. They bound to DNA as dimers and their alpha-helical content increased on binding. Parallel and antiparallel four-helix models of the DNA-bound dimer were constructed. Peptides containing disulfide bonds were engineered to test the correctness of the two models. A disulfide that is compatible with the parallel model promotes specific interaction with DNA, whereas a disulfide compatible with the antiparallel model abolishes specific binding. Electron paramagnetic resonance (EPR) measurements of nitroxide-labeled peptides provided intersubunit distance measurements that also supported the parallel model.


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