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1: Cell. 1996 Oct 18;87(2):263-76.
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The homeodomain region of Rag-1 reveals the parallel mechanisms of bacterial and V(D)J recombination.

Spanopoulou E, Zaitseva F, Wang FH, Santagata S, Baltimore D, Panayotou G.

Ruttenberg Cancer Center, Mount Sinai School of Medicine, New York, New York 10029, USA.

The V(D)J recombinase subunits Rag-1 and Rag-2 mediate assembly of antigen receptor gene segments. We studied the mechanisms of DNA recognition by Rag-1/Rag-2 using surface plasmon resonance. The critical step for signal recognition is binding of Rag-1 to the nonamer. This is achieved by a region of Rag-1 homologous to the DNA-binding domain of the Hin family of bacterial invertases and to homeodomain proteins. Strikingly, the Hin homeodomain can functionally substitute for the Rag-1 homologous region. Rag-1 also interacts with the heptamer but with low affinity. Rag-2 shows no direct binding to DNA. Once the Rag-1/Rag-2 complex is engaged on the DNA, subsequent cleavage is directed by the heptamer sequence. This order of events remarkably parallels mechanisms that mediate transposition in bacteria and nematodes.

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PMID: 8861910 [PubMed - indexed for MEDLINE]