INTERACTION CLONING - IDENTIFICATION OF A HELIX-LOOP-HELIX ZIPPER PROTEIN THAT INTERACTS WITH C-FOS

被引：334

作者：

BLANAR, MA ^{[1
]}

RUTTER, WJ ^{[1
]}

机构：

[1] UNIV CALIF SAN FRANCISCO, DEPT BIOCHEM & BIOPHYS, SAN FRANCISCO, CA 94143 USA

来源：

SCIENCE | 1992年 / 256卷 / 5059期

关键词：

D O I：

10.1126/science.1589769

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：1014 / 1018

页数：5

共 59 条

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