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 |