ArticleMolecular and cellular biology2007
Fluorescence resonance energy transfer analysis of recombination signal sequence configuration in the RAG1/2 synaptic complex.
Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Real-time analysis of RAG complex activity in V(D)J recombination.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Distinct Roles of Histone H3 and H2A Tails in Nucleosome Stability.Scientific reports · 2016Article
- The architecture of the 12RSS in V(D)J recombination signal and synaptic complexes.Nucleic acids research · 2015Article
- DNA bending in the synaptic complex in V(D)J recombination: turning an ancestral transpososome upside down.Discoveries (Craiova, Romania) · 2014Review
- Article
- RAG and HMGB1 create a large bend in the 23RSS in the V(D)J recombination synaptic complexes.Nucleic acids research · 2013Article
- Initial stages of V(D)J recombination: the organization of RAG1/2 and RSS DNA in the postcleavage complex.Molecular cell · 2009Article
- Molecular mechanism underlying RAG1/RAG2 synaptic complex formation.The Journal of biological chemistry · 2009Article
- Structure of the RAG1 nonamer binding domain with DNA reveals a dimer that mediates DNA synapsis.Nature structural & molecular biology · 2009Article
- Quantitative analyses of RAG-RSS interactions and conformations revealed by atomic force microscopy.Biochemistry · 2008Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
A critical step in V(D)J recombination is the synapsis of complementary (12/23) recombination signal sequences (RSSs) by the RAG1 and RAG2 proteins to generate the paired complex (PC). Using a facilitated ligation assay and substrates that vary the helical phasing of the RSSs, we provide evidence that one particular geometric configuration of the RSSs is favored in the PC. To investigate this configuration further, we used fluorescent resonance energy transfer (FRET) to detect the synapsis of fluorescently labeled RSS oligonucleotides. FRET requires an appropriate 12/23 RSS pair, a divalent metal ion, and high-mobility-group protein HMGB1 or HMGB2. Energy transfer between the RSSs was detected with all 12/23 RSS end positions of the fluorescent probes but was not detected when probes were placed on the two ends of the same RSS. Energy transfer was confirmed to originate from the PC by using an in-gel FRET assay. The results argue against a unique planar configuration of the RSSs in the PC and are most easily accommodated by models in which synapsed 12- and 23-RSSs are bent and cross one another, with implications for the organization of the RAG proteins and the DNA substrates at the time of cleavage.
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