In vitro V(D)J recombination: Signal joint formation Journal Article


Authors: Cortes, P.; Weis-Garcia, F.; Misulovin, Z.; Nussenzweig, A.; Lai, J. S.; Li, G.; Nussenzweig, M. C.; Baltimore, D.
Article Title: In vitro V(D)J recombination: Signal joint formation
Abstract: The first step V(D)J recombination, specific cleavage at the recombination signal sequence (RSS), can be carried out by the recombination activating proteins RAG1 and RAG2. In vivo, the cleaved coding and signal ends must be rejoined to generate functional antigen receptors and maintain chromosomal integrity. We have investigated signal joint formation using deletion and inversion substrates in a cell free system. RAG1 and RAG2 alone or in combination were unable to generate signal joints. However, RAG1 and RAG2 complemented with nuclear extracts were able to recombine an extrachromosomal substrate and form precise signal joints. The in vitro reaction resembled authentic V(D)J recombination in being Ku-antigen- dependent.
Keywords: controlled study; unclassified drug; human cell; dna-binding proteins; nonhuman; conference paper; polymerase chain reaction; proteins; animal cell; animals; cell line; protein; homeodomain proteins; transfection; animalia; nuclear proteins; gene rearrangement; genetic recombination; immunoglobulin variable region; recombination, genetic; recombinant proteins; protein biosynthesis; base sequence; dna primers; vdj recombinases; dna helicases; cho cell; cho cells; cricetinae; dna nucleotidyltransferases; antigens, nuclear; genes, immunoglobulin; humans; human; priority journal; immunoglobulin joining region; recombination activating protein rag1; recombination activating protein rag2; protein rag 1; protein rag 2
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 93
Issue: 24
ISSN: 0027-8424
Publisher: National Academy of Sciences  
Date Published: 1996-11-26
Start Page: 14008
End Page: 14013
Language: English
DOI: 10.1073/pnas.93.24.14008
PUBMED: 8943051
PROVIDER: scopus
PMCID: PMC19485
DOI/URL:
Notes: Conference Paper -- Export Date: 22 November 2017 -- Source: Scopus
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  1. Gloria C Li
    132 Li