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The leucine zipper of c-Jun binds to ribosomal protein L18a: a role in Jun protein regulation?
Journal article

The leucine zipper of c-Jun binds to ribosomal protein L18a: a role in Jun protein regulation?

  • 1995-05-01
Published in:
  • Biological chemistry Hoppe-Seyler. - 1995
Amino Acid Sequence
Bacteriophages
Base Sequence
Gene Expression Regulation
Genes, jun
Humans
Leucine Zippers
Molecular Sequence Data
Oncogene Proteins, Fusion
Proto-Oncogene Proteins c-jun
Ribosomal Proteins
Tropomyosin
English Recently we developed a method called direct interaction rescue (DIRE) for selective cloning in filamentous phage. The rescue is effected by the interaction of two heterologous proteins, one fused to the N-terminus of gene 3 adhesion protein, the other fused to the C-terminus. When heterologous fusion proteins interact with each other, gene 3 protein activity in restored thereby rescuing phage infectivity. We have used the leucine zipper of c-Jun protein as a 'bait' to select for interacting proteins from a human cDNA library. Two interacting clones were isolated, one coding for ribosomal protein L18a, a component of the large ribosomal subunit, and the other for tropomyosin, a component of the cytoskeleton. L18a contains two zipper-like domains which probably interact with c-Jun. We consider it possible that L18a (and tropomyosin) are involved in the cellular regulation of Jun protein levels.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://fredi.hepvs.ch/global/documents/175406
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