Transposition mediated by RAG1 and RAG2 and its implications for the evolution of the immune system

Alka Agrawal, Quinn M. Eastman and David G. Schatz ()
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Alka Agrawal: Department of Pharmacology
Quinn M. Eastman: Department of Molecular Biophysics and Biochemistry
David G. Schatz: Howard Hughes Medical Institute, Section of Immunobiology, Yale University School of Medicine

Nature, 1998, vol. 394, issue 6695, 744-751

Abstract: Abstract Immunoglobulin and T-cell-receptor genes are assembled from component gene segments in developing lymphocytes by a site-specific recombination reaction, V (D)J recombination. The proteins encoded by the recombination-activating genes, RAG1 and RAG2, are essential in this reaction, mediating sequence-specific DNA recognition of well-defined recombination signals and DNA cleavage next to these signals. Here we show that RAG1 and RAG2 together form a transposase capable of excising a piece of DNA containing recombination signals from a donor site and inserting it into a target DNA molecule. The products formed contain a short duplication of target DNA immediately flanking the transposed fragment, a structure like that created by retroviral integration and all known transposition reactions. The results support the theory that RAG1 and RAG2 were once components of a transposable element, and that the split nature of immunoglobulin and T-cell-receptor genes derives from germline insertion of this element into an ancestral receptor gene soon after the evolutionary divergence of jawed and jawless vertebrates.

Date: 1998
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DOI: 10.1038/29457

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