Characterization of a novel DNA binding domain within the amino-terminal region of the RAG-1 protein.
Rag-1 and Rag-2 are the critical components of the V-(D)-J recombinase required for site-specific recombination of the antigen receptor genes. In this study, we have examined the ability of recombinant (r) Rag-1 and Rag-2 to bind the recombination signal sequences (RSS) and have determined that rRag-1, but not rRag-2, is able to directly bind DNA. rRAG-1 DNA binding activity was found to reside within a novel amino-terminal arginine-rich (RR) domain with partial homology to a variety of nucleic acid binding domains. Although the RR-domain did not demonstrate RSS-specificity, this DNA binding domain may stabilize the interaction of RAG-1 with, or increase the affinity for, the V-(D)-J recombination signals.
Department of Molecular Cellular and Developmental Biology, University of California, Los Angeles 90095-1606, USA.
Z
Z
Galic
J A
JA
Alva
A
A
Lin
C J
CJ
Lyon
R J
RJ
Aguilera
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D004247:DNA / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D018398:Homeodomain Proteins / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D009687:Nuclear Proteins; D011487:Protein Conformation; D016601:RNA-Binding Proteins / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry; D017384:Sequence Deletion; D017386:Sequence Homology, Amino Acid
D004268:DNA-Binding Proteins; D018398:Homeodomain Proteins; D009687:Nuclear Proteins; C499311:RAG2 protein, human; D016601:RNA-Binding Proteins; D011994:Recombinant Proteins; C064655:V(D)J recombination activating protein 2; C064658:RAG-1 protein; D004247:DNA