The RAG1 N-terminal domain is an E3 ubiquitin ligase

Vyacheslav Yurchenko, Zhu Xue, Moshe J. Sadofsky

Research output: Contribution to journalArticle

65 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)581-585
Number of pages5
JournalGenes and Development
Volume17
Issue number5
DOIs
StatePublished - Mar 1 2003

Fingerprint

V(D)J Recombination
Ubiquitin-Protein Ligases
Polyubiquitin
T-Cell Receptor Genes
Cell Physiological Phenomena
Ubiquitination
Immunoglobulins
Proteins
In Vitro Techniques

Keywords

  • E3 ligase
  • In vitro assay
  • RAG1
  • Ubiquitin

ASJC Scopus subject areas

  • Genetics
  • Developmental Biology

Cite this

The RAG1 N-terminal domain is an E3 ubiquitin ligase. / Yurchenko, Vyacheslav; Xue, Zhu; Sadofsky, Moshe J.

In: Genes and Development, Vol. 17, No. 5, 01.03.2003, p. 581-585.

Research output: Contribution to journalArticle

Yurchenko, Vyacheslav ; Xue, Zhu ; Sadofsky, Moshe J. / The RAG1 N-terminal domain is an E3 ubiquitin ligase. In: Genes and Development. 2003 ; Vol. 17, No. 5. pp. 581-585.
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