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Nucleic Acids Research, 1993, Vol. 21, No. 18 4348-4355
© 1993

MOLECULAR BIOLOGY

Dimerization of leucine zippers analyzed by random selection

William T. Pu and Kevin Struhl*

Department Biological Chemistry and molecular Pharmacology, Harvard Medical School Boston, MA 02115 USA

*To whom correspondence should be addressed

Received April 8, 1993. Revised July 16, 1993. Accepted July 16, 1993.

The leucine zipper Is a coiled coll that mediates specific dimerization of bZIP DNA-binding domains. A hydrophobic spine involving the conserved leuclnes runs down the colled-coll and is thought to stabilize the dimer. We used the method of random selection to further define the primary sequence requirements for homodlmer formation and heterodimer formation with Fos. When positions on either side of the hydrophobic spine of GCN4 are diversified to Include the corresponding residues of Jun, a large percentage of the resulting sequences form homodimers, and a large percentage form heterodlmers with Fos. Basic residues were preferred, but not essential, at position e of zippers which heterodlmertze with Fos. When random sequences containing 5 heptad repeat of leuclnes are subject to a selection for homodimer formation, a diverse set of sequences is Isolated. Certain residues are preferred at each position In the heptad repeat, although no essential primary sequence determinants could be identified. No pair of residues not involving the conserved leucines could be Identified which strongly promotes homodimerizatlon. These results suggest that factors determining leucine zipper dimerization are complex, with numerous interactions contributing to the association.


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