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Science 15 May 1992: Vol. 256. no. 5059, pp. 1014 - 1018 DOI: 10.1126/science.1589769
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Articles
Science, Vol 256, Issue 5059, 1014-1018
Copyright © 1992 by American Association for the Advancement of Science
Interaction cloning: identification of a helix-loop-helix zipper protein that interacts with c-Fos
MA Blanar
and
WJ Rutter
Hormone Research Institute, University of California, San Francisco 94143.
A facile method for isolating genes that encode interacting proteins has been developed with a polypeptide probe that contains an amino-terminal extension with recognition sites for a monoclonal antibody, a specific endopeptidase, and a site-specific protein kinase. This probe, containing the basic region-leucine zipper dimerization motif of c-Fos, was used to screen a complementary DNA library. A complementary DNA that encoded a member of the basic-helix-loop-helix-zipper (bHLH-Zip) family of proteins was isolated. The complementary DNA-encoded polypeptide FIP (Fos interacting protein) bound to oligonucleotide probes that contained DNA binding motifs for other HLH proteins. When cotransfected with c-Fos, FIP stimulated transcription of an AP-1-responsive promoter.
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