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The RAG1 N-terminal domain is an E3 ubiquitin ligase
Vyacheslav Yurchenko1, Zhu Xue, Moshe Sadofsky
1Department of Pathology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Genes & Development
|March 12, 2003
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.