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A Jun-binding protein related to a putative tumor suppressor.


ABSTRACT: A lambda gt11 cDNA library of chicken embryo fibroblasts was screened with biotinylated Jun protein to identify Jun-binding clones. Eight such clones were isolated; one contains a gene referred to as jif-1 that is homologous to the putative tumor suppressor gene QM. jif-1 codes for a protein of 25 kDa that binds to the leucine zipper of viral and cellular Jun. The Jif-1 protein also binds to itself. Jif-1 does not contain a leucine zipper, and it does not bind to the 12-O-tetradecanoylphorbol 13-acetate response element DNA sequence. Complex formation of Jif-1 with Jun inhibits DNA binding and reduces transactivation by Jun. Addition of Fos protein to Jun-Jif-1 complexes restores DNA-binding activity. These observations suggest that Jif-1 is a negative regulator of Jun.

SUBMITTER: Monteclaro FS 

PROVIDER: S-EPMC47005 | biostudies-other | 1993 Jul

REPOSITORIES: biostudies-other

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A Jun-binding protein related to a putative tumor suppressor.

Monteclaro F S FS   Vogt P K PK  

Proceedings of the National Academy of Sciences of the United States of America 19930701 14


A lambda gt11 cDNA library of chicken embryo fibroblasts was screened with biotinylated Jun protein to identify Jun-binding clones. Eight such clones were isolated; one contains a gene referred to as jif-1 that is homologous to the putative tumor suppressor gene QM. jif-1 codes for a protein of 25 kDa that binds to the leucine zipper of viral and cellular Jun. The Jif-1 protein also binds to itself. Jif-1 does not contain a leucine zipper, and it does not bind to the 12-O-tetradecanoylphorbol 13  ...[more]

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