ArticleMolecular and cellular biology2002
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.
Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 70 citations in OpenAlex.
- Evolutionary insights and structural characterization guide the development of RAG1/RAG2-deficient swine models for immunological research.Frontiers in immunology · 2026Article
- Generating combinatorial diversity via engineered V(D)J-like recombination in Saccharomyces cerevisiae.Nature communications · 2025Article
- Generation of inactivated IL2RG and RAG1 monkeys with severe combined immunodeficiency using base editing.Signal transduction and targeted therapy · 2023Article
- HIV‑1 integrase inhibitors targeting various DDE transposases: Retroviral integration versus RAG‑mediated recombination (Review).Molecular medicine reports · 2019Review
- Structural insights into the mechanism of double strand break formation by Hermes, a hAT family eukaryotic DNA transposase.Nucleic acids research · 2018Article
- T cell receptor β-chains display abnormal shortening and repertoire sharing in type 1 diabetes.Nature communications · 2017Article
- RAG2 and XLF/Cernunnos interplay reveals a novel role for the RAG complex in DNA repair.Nature communications · 2016Article
- Mapping and Quantitation of the Interaction between the Recombination Activating Gene Proteins RAG1 and RAG2.The Journal of biological chemistry · 2015Article
- Article
- A hypomorphic recombination-activating gene 1 (RAG1) mutation resulting in a phenotype resembling common variable immunodeficiency.The Journal of allergy and clinical immunology · 2014Article
- Real-time monitoring of RAG-catalyzed DNA cleavage unveils dynamic changes in coding end association with the coding end complex.Nucleic acids research · 2012Article
- Non-consensus heptamer sequences destabilize the RAG post-cleavage complex, making ends available to alternative DNA repair pathways.Nucleic acids research · 2010Article
- The role of mechanistic factors in promoting chromosomal translocations found in lymphoid and other cancers.Advances in immunology · 2010Review
- Molecular analysis of T-B-NK+ severe combined immunodeficiency and Omenn syndrome cases in Saudi Arabia.BMC medical genetics · 2009Article
- RAG: a recombinase diversified.Nature immunology · 2009Review
- Molecular mechanism underlying RAG1/RAG2 synaptic complex formation.The Journal of biological chemistry · 2009Article
- A zinc site in the C-terminal domain of RAG1 is essential for DNA cleavage activity.Journal of molecular biology · 2009Article
- Initial stages of V(D)J recombination: the organization of RAG1/2 and RSS DNA in the postcleavage complex.Molecular cell · 2009Article
- Structure of the RAG1 nonamer binding domain with DNA reveals a dimer that mediates DNA synapsis.Nature structural & 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
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Although both RAG-1 and RAG-2 are required for all steps of V(D)J recombination, little is known about the specific contribution of either protein to these steps. RAG-1 contains three acidic active-site amino acids that are thought to coordinate catalytic metal ions. To search for additional catalytic amino acids and to better define the functional anatomy of RAG-1, we mutated all 86 conserved basic amino acids to alanine and evaluated the mutant proteins for DNA binding, nicking, hairpin formation, and joining. We found several amino acids outside of the canonical nonamer-binding domain that are critical for DNA binding, several step arrest mutants with defects in nicking or hairpin formation, and four RAG-1 mutants defective specifically for joining. Analysis of coding joints formed by some of these mutants revealed excessive deletions, frequent use of short sequence homologies, and unusually long palindromic junctional inserts, known as P nucleotides, that result from aberrant hairpin opening. These features characterize junctions found in scid mice, which are deficient for the catalytic subunit of DNA-dependent protein kinase (DNA-PKcs), suggesting that the RAG proteins and DNA-PKcs perform overlapping functions in coding joint formation. Interestingly, the amino acids that are altered in 12 of our mutants are also mutated in human inherited immunodeficiency syndromes. Our analysis of these mutants provides insights into the molecular mechanisms underlying these disorders.
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