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Science 20 May 1994:
Vol. 264. no. 5162, pp. 1130 - 1133
DOI: 10.1126/science.8178171
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Articles

Science, Vol 264, Issue 5162, 1130-1133
Copyright © 1994 by American Association for the Advancement of Science

articles

DNA targets for certain bZIP proteins distinguished by an intrinsic bend

DN Paolella, CR Palmer, and A Schepartz

Department of Chemistry, Yale University, New Haven, CT 06511.

In spite of the large amount of sequence conservation among the DNA binding segments of basic region leucine zipper (bZIP) proteins, these proteins can discriminate differently between target sequences that differ in half-site spacing. Here it is shown that the half-site spacing preferences of bZIP proteins are the result of (i) the differential intrinsic curvature in target binding sites that differ by insertion or deletion of a single base pair and (ii) the ability of some bZIP proteins to overcome this intrinsic curvature through a mechanism dependent on basic segment residues.


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