The RAG1 N-terminal domain is an E3 ubiquitin ligase.
RAG1 and RAG2 initiate V(D)J recombination, which is the assembly of immunoglobulin and T cell receptor genes. The N-terminal region of RAG1 can be deleted, leaving an enzymatic "core" able to catalyze the complete reaction. Here we report that the N-terminal portion of RAG1 has a distinct enzymatic role separate ... from the rest of the protein. It acts as an E3 ligase in the ubiquitylation of a test substrate and formation of polyubiquitin chains in vitro. This finding suggests a new way in which V(D)J recombination can be regulated and coupled to other aspects of cell physiology.
Mesh Terms:
Animals, Gene Rearrangement, Homeodomain Proteins, Immunoglobulin Variable Region, Ligases, Mice, Protein Structure, Tertiary, Ubiquitin-Conjugating Enzymes, Ubiquitin-Protein Ligases
Animals, Gene Rearrangement, Homeodomain Proteins, Immunoglobulin Variable Region, Ligases, Mice, Protein Structure, Tertiary, Ubiquitin-Conjugating Enzymes, Ubiquitin-Protein Ligases
Genes Dev.
Date: Mar. 01, 2003
PubMed ID: 12629039
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