RAG1 and RAG2 form a stable postcleavage synaptic complex with DNA containing signal ends in V(D)J recombination

Article Abstract:

Nuclease sensitivity, mobility shift and immunoprecipitation techniques were used to determine the protein-DNA complexes that exist after cleavage of recombination activating genes 1 and 2 (RAG1 and RAG2) during V(D)J recombination. The results identified a stable postcleavage synaptic complex composed of the proteins RAG1, RAG2, HMG-1 or the closely related HMG-2 and the components of the DNA-dependent protein kinase. The complex was observed to be formed between synapsed recombination signals.

Usage, Protein binding, DNA binding proteins, Immunoassay

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RAG1 mediates signal sequence recognition and recruitment of RAG2 in V(D)J recombination

Article Abstract:

The recombination activating genes, RAG-1 and RAG-2, mediate the variable(diversity)joining (V(D)J) recombination and lymphocyte development during embryogenesis. In vivo one hybrid analysis of V(D)J recombination indicates a direct interaction between RAG1 and RAG2 with the recombination signals during the formation of a 12 signal-23 signal synaptic complex. Furthermore, inhibition of RAG2 activity did not alter the heptamer-nonamer recognition activities of RAG1.

Cellular signal transduction

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The homedomain region of Rag-1 reveals the parallel mechanisms of bacterial and V(D)J recombination

Article Abstract:

The deoxyribonucleic acid (DNA)-recognition mechanism that occur between Rag-1 and Rag-2 during variable(diversity)joining recombination are initiated by the recombination signal sequences that are produced by Rag-1. Furthermore, the specific DNA cleavage activities of the Rag1-Rag2 complex require an intact heptamer and nonamer motif. However, a domain within the 384-477 amino acid sequence of Rag-1 is required for the specific binding of the nonamer.

DNA, Nucleic acids

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