Characterization of C. elegans RING finger protein 1, a binding partner of ubiquitin-conjugating enzyme 1.

In a yeast two-hybrid screen, RING finger protein 1 (RFP-1) and UBR1 were identified as potential binding partners of C. elegans UBC-1, a ubiquitin-conjugating enzyme with a high degree of identity to S. cerevisiae UBC2/RAD6. The interaction of RFP-1 and UBC-1 was confirmed by co-immunoprecipitation experiments. Yeast interaction trap experiments ...
mapped the region of interaction to the basic N-terminal 313 residues of RFP-1. The acidic carboxy-terminal extension of UBC-1 was not required for the interaction with RFP-1. Western blot analysis and indirect immunohistochemical staining show that RFP-1 is present in embryos, larvae, and adults, where it is found in intestinal, nerve ring, pharyngeal, gonadal, and oocyte cell nuclei. Double-stranded RNA interference experiments against rfp-1 indicate that this gene is required for L1 development, vulval development, and for egg laying. By contrast, RNA interference against ubc-1 gave no obvious phenotype, suggesting that ubc-1 is nonessential or is functionally redundant.
Mesh Terms:
Amino Acid Sequence, Animals, Caenorhabditis elegans, Caenorhabditis elegans Proteins, Carrier Proteins, Molecular Sequence Data, Precipitin Tests, Protein Interaction Mapping, RNA Interference, Ubiquitin-Conjugating Enzymes
Dev. Biol.
Date: Jan. 15, 2004
Download Curated Data For This Publication
Switch View:
  • Interactions 3