V(D)J recombination is mediated by the products of the recombination activation genes, RAG1 and RAG2. DNA binding and cleavage are targeted by recombination sequences that flank each gene segment and are composed of well-conserved heptamer and nonamer sequences separated either by 12 or 23 base pairs. Schatz and co-workers report the crystal structure of the RAG1 nonamer binding domain (NBD) bound to its cognate sequence. The NBD adopts an intertwined dimer that mediates the synapsis of two DNA molecules. Biochemical and FRET experiments support the structural findings and have implications for the regulation of DNA binding and cleavage by RAG1/2.
- Fang Fang Yin
- Scott Bailey
- David G Schatz