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Logo of jbcThe Journal of Biological Chemistry
J Biol Chem. 2015 May 8; 290(19): 11818.
PMCID: PMC4424322

Elucidating the Role of an Important Endonuclease's Components During V(D)J Recombination in Immune Cells♦

Mapping and Quantitation of the Interaction between the Recombination Activating Gene Proteins RAG1 and RAG2

♦ See referenced article, J. Biol. Chem. 2015, 290, 11802–11817

The RAG endonuclease functions in developing B and T lymphocytes to promote V(D)J recombination, which assembles the variable regions of immunoglobulin and T cell receptor genes. The endonuclease has two components. RAG1 contains the active site for DNA cleavage. RAG2 is an accessory factor that is important for RAG1 function. However, researchers wish to discover how interacting with RAG2 activates RAG1. In this Paper of the Week, a team led by David Schatz at the Yale School of Medicine demonstrated with a series of structural and biochemical experiments that only a small portion of RAG1 was needed to interact robustly with RAG2. The small portion of RAG1 consisted of the active site and its immediate surroundings. The interaction between RAG1 and RAG2 had a binding constant of ~0.4 μm. The investigators concluded that the two components of the RAG endonuclease interacted with modest affinity relative to their estimated concentrations in the lymphocyte nucleus. The authors say, “Inefficient association of RAG1 with RAG2 could help limit damage to the genome.”

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Model of RAG1 catalytic and RAG2 binding regions.

Articles from The Journal of Biological Chemistry are provided here courtesy of American Society for Biochemistry and Molecular Biology