期刊
GENES & DEVELOPMENT
卷 17, 期 5, 页码 581-585出版社
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/gad.1058103
关键词
RAG1; ubiquitin; E3 ligase; in vitro assay
资金
- NIAID NIH HHS [AI41711, R29 AI041711, R01 AI041711] Funding Source: Medline
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.
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