Evidence for Ku70/Ku80 association with full-length RAG1

• Published in: Nucleic acids research Vol. 36; no. 6; pp. 2060 - 2072
• Main Authors: Raval, Prafulla, Kriatchko, Aleksei N, Kumar, Sushil, Swanson, Patrick C
• Format: Journal Article
• Language: English
• Published: England Oxford University Press 01-04-2008; Oxford Publishing Limited (England)
• Subjects: Antigens, Nuclear - metabolism; Binding Sites; Cell Line; DNA-Binding Proteins - metabolism; Gene Rearrangement; Homeodomain Proteins - chemistry; Homeodomain Proteins - isolation & purification; Homeodomain Proteins - metabolism; Humans; Ku Autoantigen; Molecular Biology; Protein Structure, Tertiary; Regulatory Sequences, Nucleic Acid
• ISSN: 0305-1048; 1362-4962
• DOI: 10.1093/nar/gkn049

Antigen receptor genes are assembled by a site-specific DNA rearrangement process called V(D)J recombination. This process proceeds through two distinct phases: a cleavage phase in which the RAG1 and RAG2 proteins introduce DNA double-strand breaks at antigen receptor gene segments, and a joining phase in which the resulting DNA breaks are processed and repaired via the non-homologous end-joining (NHEJ) repair pathway. Genetic and biochemical evidence suggest that the RAG proteins play an active role in guiding the repair of DNA breaks introduced during V(D)J recombination to the NHEJ pathway. However, evidence for specific association between the RAG proteins and any of the factors involved in NHEJ remains elusive. Here we present evidence that two components of the NHEJ pathway, Ku70 and Ku80, interact with full-length RAG1, providing a biochemical link between the two phases of V(D)J recombination.