The RAG1 N-terminal domain is an E3 ubiquitin ligase

Vyacheslav Yurchenko; Zhu Xue; Moshe Sadofsky

doi:10.1101/gad.1058103

The RAG1 N-terminal domain is an E3 ubiquitin ligase

Vyacheslav Yurchenko, Zhu Xue, Moshe Sadofsky

Pathology

Research output: Contribution to journal › Article › peer-review

74 Scopus citations

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	https://doi.org/10.1101/gad.1058103
State	Published - Mar 1 2003

Keywords

E3 ligase
In vitro assay
RAG1
Ubiquitin

ASJC Scopus subject areas

Genetics
Developmental Biology

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10.1101/gad.1058103

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AU - Xue, Zhu

AU - Sadofsky, Moshe

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N2 - 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.

AB - 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.

KW - E3 ligase

KW - In vitro assay

KW - RAG1

KW - Ubiquitin

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The RAG1 N-terminal domain is an E3 ubiquitin ligase

Abstract

Keywords

ASJC Scopus subject areas

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