Autoubiquitylation of the V(D)J recombinase protein RAG1.
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, UbcH3/CDC34, and requires an intact RAG1 RING finger motif. Disruption of the RING finger and certain RAG1 N-terminal truncations are associated with immunodeficiency in human patients, suggesting that RAG1's ubiquitin ligase is required for its biological role in lymphocyte development.
Mesh Terms:
Animals, Base Sequence, Binding Sites, Cloning, Molecular, DNA Primers, DNA-Binding Proteins, Homeodomain Proteins, Humans, Kinetics, Mice, Nuclear Proteins, Polymerase Chain Reaction, Recombinant Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Ubiquitin, VDJ Recombinases, Zinc
Animals, Base Sequence, Binding Sites, Cloning, Molecular, DNA Primers, DNA-Binding Proteins, Homeodomain Proteins, Humans, Kinetics, Mice, Nuclear Proteins, Polymerase Chain Reaction, Recombinant Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Ubiquitin, VDJ Recombinases, Zinc
Proc. Natl. Acad. Sci. U.S.A.
Date: Dec. 23, 2003
PubMed ID: 14671314
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