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Article

Hairpin coding end opening is mediated by RAG1 and RAG2 proteins.

Molecular cell - 1 Dec 1998

Besmer E, Mansilla-Soto J, Cassard S, Sawchuk D J, Brown G, Sadofsky M, Lewis S M, Nussenzweig M C, Cortes P

Abstract excerpt

Despite the importance of hairpin opening in antigen receptor gene assembly, the molecular machinery that mediates this reaction has not been defined. Here, we show that RAG1 plus RAG2 can open DNA hairpins. Hairpin opening by RAGs is not sequence specific, but in Mg2+, hairpin opening occurs only in the context of a regulated cleavage complex. The chemical mechanism of hairpin opening by RAGs resembles RSS...

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Source

Identifiers

PMID: 9885569
DOI: 10.1016/s1097-2765(00)80296-8

Genes

RAG1
RAG2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Hairpin coding end opening is mediated by RAG1 and RAG2 proteins.PMID 9885569Read ↗

Requirements for DNA hairpin formation by RAG1/2.Semantic proximity Read ↗

Autoinhibition of DNA cleavage mediated by RAG1 and RAG2 is overcome by an epigenetic signal in V(D)J recombination.Semantic proximity Read ↗

Understanding how the V(D)J recombinase catalyzes transesterification: distinctions between DNA cleavage and transposition.Semantic proximity Read ↗

Full-length RAG1 promotes contact with coding and intersignal sequences in RAG protein complexes bound to recombination signals paired in cis.Semantic proximity Read ↗

Role of recombination activating genes in the generation of antigen receptor diversity and beyond.Semantic proximity Read ↗

The structure of the mammalian RNase H2 complex provides insight into RNA.NA hybrid processing to prevent immune dysfunction.Semantic proximity Read ↗

Real-time monitoring of RAG-catalyzed DNA cleavage unveils dynamic changes in coding end association with the coding end complex.Semantic proximity Read ↗

The RAG1/RAG2 complex constitutes a 3' flap endonuclease: implications for junctional diversity in V(D)J and transpositional recombination.Semantic proximity Read ↗

RAG proteins shepherd double-strand breaks to a specific pathway, suppressing error-prone repair, but RAG nicking initiates homologous recombination.Semantic proximity Read ↗

Evidence of a critical architectural function for the RAG proteins in end processing, protection, and joining in V(D)J recombination.Semantic proximity Read ↗

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.Semantic proximity Read ↗

Crystal structure of the V(D)J recombinase RAG1-RAG2.Semantic proximity Read ↗

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