The RAG1 N-terminal domain is an E3 ubiquitin ligase.
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.
Yurchenko
Vyacheslav
V
Department of Pathology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Xue
Zhu
Z
Sadofsky
Moshe
M
D000818:Animals; D015321:Gene Rearrangement / Q000502:physiology; D018398:Homeodomain Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D007135:Immunoglobulin Variable Region / Q000235:genetics; D008025:Ligases / Q000378:metabolism*; D051379:Mice; D017434:Protein Structure, Tertiary / Q000235:genetics / Q000502:physiology; D044763:Ubiquitin-Conjugating Enzymes; D044767:Ubiquitin-Protein Ligases
D018398:Homeodomain Proteins; D007135:Immunoglobulin Variable Region; C064658:RAG-1 protein; C105156:UBE2C protein, human; D044763:Ubiquitin-Conjugating Enzymes; D044767:Ubiquitin-Protein Ligases; D008025:Ligases