| First Author | Yurchenko V | Year | 2003 |
| Journal | Genes Dev | Volume | 17 |
| Issue | 5 | Pages | 581-5 |
| PubMed ID | 12629039 | Mgi Jnum | J:159076 |
| Mgi Id | MGI:4441135 | Doi | 10.1101/gad.1058103 |
| Citation | Yurchenko V, et al. (2003) The RAG1 N-terminal domain is an E3 ubiquitin ligase. Genes Dev 17(5):581-5 |
| abstractText | 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. |
