Abstract:
: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.
journal_name
Celljournal_title
Cellauthors
Spanopoulou E,Zaitseva F,Wang FH,Santagata S,Baltimore D,Panayotou Gdoi
10.1016/s0092-8674(00)81344-6subject
Has Abstractpub_date
1996-10-18 00:00:00pages
263-76issue
2eissn
0092-8674issn
1097-4172pii
S0092-8674(00)81344-6journal_volume
87pub_type
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