ArticleThe Journal of biological chemistry2015
Assembly Pathway and Characterization of the RAG1/2-DNA Paired and Signal-end Complexes.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- A Synthetic Platform for Antibody Junctional Diversification Beyond Natural Constraints.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Activity of zebrafish THAP9 transposase and zebrafish P element-like transposons.bioRxiv : the preprint server for biology · 2024Article
- Insights into RAG Evolution from the Identification of "Missing Link" Family A RAGL Transposons.Molecular biology and evolution · 2023Article
- Structural insights into the evolution of the RAG recombinase.Nature reviews. Immunology · 2022Review
- Inner workings of RAG recombinase and its specialization for adaptive immunity.Current opinion in structural biology · 2021Review
- The recent advances in non-homologous end-joining through the lens of lymphocyte development.DNA repair · 2020Review
- How mouse RAG recombinase avoids DNA transposition.Nature structural & molecular biology · 2020Article
- Cutting antiparallel DNA strands in a single active site.Nature structural & molecular biology · 2020Article
- Structure of a P element transposase-DNA complex reveals unusual DNA structures and GTP-DNA contacts.Nature structural & molecular biology · 2019Article
- Cracking the DNA Code for V(D)J Recombination.Molecular cell · 2018Article
- Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Mammalian immune receptor diversity is established via a unique restricted set of site-specific DNA rearrangements in lymphoid cells, known as V(D)J recombination. The lymphoid-specific RAG1-RAG2 protein complex (RAG1/2) initiates this process by binding to two types of recombination signal sequences (RSS), 12RSS and 23RSS, and cleaving at the boundaries of RSS and V, D, or J gene segments, which are to be assembled into immunoglobulins and T-cell receptors. Here we dissect the ordered assembly of the RAG1/2 heterotetramer with 12RSS and 23RSS DNAs. We find that RAG1/2 binds only a single 12RSS or 23RSS and reserves the second DNA-binding site specifically for the complementary RSS, to form a paired complex that reflects the known 12/23 rule of V(D)J recombination. The assembled RAG1/2 paired complex is active in the presence of Mg(2+), the physiologically relevant metal ion, in nicking and double-strand cleavage of both RSS DNAs to produce a signal-end complex. We report here the purification and initial crystallization of the RAG1/2 signal-end complex for atomic-resolution structure elucidation. Strict pairing of the 12RSS and 23RSS at the binding step, together with information from the crystal structure of RAG1/2, leads to a molecular explanation of the 12/23 rule.
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