ArticleThe Journal of biological chemistry2009
Molecular mechanism underlying RAG1/RAG2 synaptic complex formation.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 34 citations in OpenAlex.
- Assembly of Synaptic Protein-DNA Complexes: Critical Role of Non-Specific Interactions.International journal of molecular sciences · 2023Article
- Site-Search Process for Synaptic Protein-DNA Complexes.International journal of molecular sciences · 2021Article
- Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging.Journal of visualized experiments : JoVE · 2019Article
- Insight into dynamics of APOBEC3G protein in complexes with DNA assessed by high speed AFM.Nanoscale advances · 2019Article
- Computational Model and Dynamics of Monomeric Full-Length APOBEC3G.ACS central science · 2017Article
- Nanoscale Characterization of Interaction of APOBEC3G with RNA.Biochemistry · 2017Article
- Assembly Pathway and Characterization of the RAG1/2-DNA Paired and Signal-end Complexes.The Journal of biological chemistry · 2015Article
- 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
- Direct Detection of α-Synuclein Dimerization Dynamics: Single-Molecule Fluorescence Analysis.Biophysical journal · 2015Article
- Single-molecule analysis of RAG-mediated V(D)J DNA cleavage.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The architecture of the 12RSS in V(D)J recombination signal and synaptic complexes.Nucleic acids research · 2015Article
- Recombination-activating gene 1 and 2 (RAG1 and RAG2) in flounder (Paralichthys olivaceus).Journal of biosciences · 2014Article
- Histone methylation and V(D)J recombination.International journal of hematology · 2014Review
- Modeling of the RAG reaction mechanism.Cell reports · 2014Article
- DNA bending in the synaptic complex in V(D)J recombination: turning an ancestral transpososome upside down.Discoveries (Craiova, Romania) · 2014Review
- Visualization of DNA and protein-DNA complexes with atomic force microscopy.Methods in molecular biology (Clifton, N.J.) · 2014Article
- RAG and HMGB1 create a large bend in the 23RSS in the V(D)J recombination synaptic complexes.Nucleic acids research · 2013Article
- Mica functionalization for imaging of DNA and protein-DNA complexes with atomic force microscopy.Methods in molecular biology (Clifton, N.J.) · 2013Article
- Article
- Specificity of binding of single-stranded DNA-binding protein to its target.Biochemistry · 2012Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
Abstract
Two lymphoid cell-specific proteins, RAG1 and RAG2 (RAG), initiate V(D)J recombination by assembling a synaptic complex with recombination signal sequences (RSSs) abutting two different antigen receptor gene coding segments, and then introducing a DNA double strand break at the end of each RSS. Despite the biological importance of this system, the structure of the synaptic complex, and the RAG protein stoichiometry and arrangement of DNA within the synaptosome, remains poorly understood. Here we applied atomic force microscopy to directly visualize and characterize RAG synaptic complexes. We report that the pre-cleavage RAG synaptic complex contains about twice the protein content as a RAG complex bound to a single RSS, with a calculated mass consistent with a pair of RAG heterotetramers. In the synaptic complex, the RSSs are predominantly oriented in a side-by-side configuration with no DNA strand crossover. The mass of the synaptic complex, and the conditions under which it is formed in vitro, favors an association model of assembly in which isolated RAG-RSS complexes undergo synapsis mediated by RAG protein-protein interactions. The replacement of Mg2+ cations with Ca2+ leads to a dramatic change in protein stoichiometry for all RAG-RSS complexes, suggesting that the cation composition profoundly influences the type of complex assembled.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.