Autoubiquitylation of the V(D)J recombinase protein RAG1.

@article{Jones2003AutoubiquitylationOT,
  title={Autoubiquitylation of the V(D)J recombinase protein RAG1.},
  author={Jessica M. Jones and Martin Gellert},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2003},
  volume={100 26},
  pages={15446-51}
}
V(D)J recombination, the rearrangement of gene segments to assemble Ig and T cell receptor coding regions, is vital to B and T lymphocyte development. Here, we demonstrate that the V(D)J recombinase protein RAG1 undergoes ubiquitylation in cells. In vitro, the RING finger domain of RAG1 acts as a ubiquitin ligase that mediates its own ubiquitylation at a highly conserved K residue in the RAG1 amino-terminal region. Ubiquitylation is best supported by a specific ubiquitin-conjugating enzyme… CONTINUE READING

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