ArticleMolecular and cellular biology2001
A C-terminal region of RAG1 contacts the coding DNA during V(D)J recombination.
Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 37 citations in OpenAlex.
- The recombinase activating genes: architects of immune diversity during lymphocyte development.Frontiers in immunology · 2023Review
- RAG Deficiency: Two Genes, Many Diseases.Journal of clinical immunology · 2018Review
- HypomorphicBlood · 2018Article
- Characterization of T and B cell repertoire diversity in patients with RAG deficiency.Science immunology · 2016Article
- Human RAG mutations: biochemistry and clinical implications.Nature reviews. Immunology · 2016Review
- An interdomain boundary in RAG1 facilitates cooperative binding to RAG2 in formation of the V(D)J recombinase complex.Protein science : a publication of the Protein Society · 2015Article
- Cooperative recruitment of HMGB1 during V(D)J recombination through interactions with RAG1 and DNA.Nucleic acids research · 2013Article
- A non-sequence-specific DNA binding mode of RAG1 is inhibited by RAG2.Journal of molecular biology · 2009Article
- Full-length RAG1 promotes contact with coding and intersignal sequences in RAG protein complexes bound to recombination signals paired in cis.Nucleic acids research · 2009Article
- A RAG1 mutation found in Omenn syndrome causes coding flank hypersensitivity: a novel mechanism for antigen receptor repertoire restriction.Journal of immunology (Baltimore, Md. : 1950) · 2008Article
- The structure-specific nicking of small heteroduplexes by the RAG complex: implications for lymphoid chromosomal translocations.DNA repair · 2007Article
- Requirements for DNA hairpin formation by RAG1/2.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- RAG1 core and V(D)J recombination signal sequences were derived from Transib transposons.PLoS biology · 2005Article
- DNA cleavage activity of the V(D)J recombination protein RAG1 is autoregulated.Molecular and cellular biology · 2004Article
- Ordered DNA release and target capture in RAG transposition.The EMBO journal · 2004Article
- Increased frequency of aberrant V(D)J recombination products in core RAG-expressing mice.Nucleic acids research · 2004Article
- The RAG1 N-terminal domain is an E3 ubiquitin ligase.Genes & development · 2003Article
- Evidence of a critical architectural function for the RAG proteins in end processing, protection, and joining in V(D)J recombination.Genes & development · 2002Article
- Mutational analysis of all conserved basic amino acids in RAG-1 reveals catalytic, step arrest, and joining-deficient mutants in the V(D)J recombinase.Molecular and cellular biology · 2002Article
- The RAG proteins in V(D)J recombination: more than just a nuclease.Nucleic acids research · 2001Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The site-specific DNA rearrangement process, called V(D)J recombination, creates much of the diversity of immune receptor molecules in the adaptive immune system. Central to this reaction is the organization of the protein-DNA complex containing the proteins RAG1 and RAG2 and their DNA targets. A long-term goal is to appreciate the three-dimensional relationships between the proteins and DNA that allow the assembly of the appropriate reaction intermediates, resulting in concerted cleavage and directed rejoining of the DNA ends. Previous cross-linking approaches have mapped RAG1 contacts on the DNA. RAG1 protein contacts the DNA at the conserved heptamer and nonamer sequences as well as at the coding DNA adjacent to the heptamer. Here we subject RAG1, covalently cross-linked to DNA substrates, to partial cyanogen bromide degradation or trypsin proteolysis in order to map contacts on the protein. We find that coding-sequence contacts occur near the C terminus of RAG1, while contacts made within the recombination signal sequence occur nearer the N terminus of the core region of RAG1. A deletion protein lacking the C-terminal DNA-contacting region is still capable of making the N-terminal contacts. This suggests that the two binding interactions may exist on two separate domains of the protein. A trypsin cleavage pattern of the native protein supports this conclusion. A two-domain model for RAG1 is evaluated with respect to the larger recombination complex.
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