Abstract
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.
Original language | English (US) |
---|---|
Pages (from-to) | 581-585 |
Number of pages | 5 |
Journal | Genes and Development |
Volume | 17 |
Issue number | 5 |
DOIs | |
State | Published - Mar 1 2003 |
Keywords
- E3 ligase
- In vitro assay
- RAG1
- Ubiquitin
ASJC Scopus subject areas
- Genetics
- Developmental Biology