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Characterization of a novel DNA binding domain within the amino‐terminal region of the RAG‐1 protein
Author(s) -
Alva Jackelyn A.,
Lin Albert,
Lyon Christopher J.,
Aguilera Renato J.,
Galic Zoran
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800202922
Subject(s) - recombination signal sequences , recombinase , dna , hmg box , recombinant dna , recombination , biology , nucleic acid , genetics , microbiology and biotechnology , gene , dna binding domain , dna binding protein , recombination activating gene , transcription factor
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.