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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Gene Rearrangement / physiology
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Homeodomain Proteins / chemistry
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Homeodomain Proteins / genetics*
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Homeodomain Proteins / metabolism*
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Immunoglobulin Variable Region / genetics
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Ligases / metabolism*
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Mice
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Protein Structure, Tertiary / genetics
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Protein Structure, Tertiary / physiology
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Ubiquitin-Conjugating Enzymes*
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Ubiquitin-Protein Ligases
Substances
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Homeodomain Proteins
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Immunoglobulin Variable Region
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RAG-1 protein
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UBE2C protein, human
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Ubiquitin-Conjugating Enzymes
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Ubiquitin-Protein Ligases
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Ligases