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Updated: Jul 29, 2026

Analyzing and Building Nucleic Acid Structures with 3DNA
Published on: April 26, 2013
Selection of a high-affinity DNA pool for a bZip protein with an out-of-phase alignment of the basic region relative
Y Lee1, D G Gurnon, J J Hollenbeck
1Department of Chemistry, Indiana University, 800 East Kirkwood Avenue, Bloomington, IN 47405-7102, USA.
Abstract:
bZip transcription factors contain two regions that are required for DNA binding: a leucine zipper dimerization domain and a highly charged basic region that directly contacts DNA. The spacing between these subdomains is strictly conserved, and changes in this spacing result in a loss of function. Using an in vitro selection strategy, we have investigated the ability of a bZip protein with incorrect spacing between these two regions to bind specifically to DNA. Surprisingly, we find that although such a protein does not bind to its predicted site, it is possible to isolate a pool of DNAs that bind with very similar affinity to that of GCN4 for its optimum DNA site.

