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Science 23 November 1990:
Vol. 250. no. 4984, pp. 1104 - 1110
DOI: 10.1126/science.2174572

Articles

Science, Vol 250, Issue 4984, 1104-1110
Copyright © 1990 by American Association for the Advancement of Science


articles

Differences and similarities in DNA-binding preferences of MyoD and E2A protein complexes revealed by binding site selection

TK Blackwell and H Weintraub

Department of Genetics, Fred Hutchinson Cancer Research Center, Seattle, WA.

A technique was developed for studying protein-DNA recognition that can be applied to any purified protein, partially purified protein, or cloned gene. From oligonucleotides in which particular positions are of random sequence, that subset to which a given protein binds is amplified by the polymerase chain reaction and sequenced as a pool. These selected and amplified binding site (SAAB) "imprints" provide a characteristic set of preferred sequences for protein binding. With this technique, it was shown that homo- and heterooligomers of the helix-loop-helix proteins MyoD and E2A recognize a common consensus sequence, CA--TG, but otherwise bind to flanking and internal positions with different sequence preferences that suggest half-site recognition. These findings suggest that different combinations of dimeric proteins can have different binding sequence preferences.


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