Evidence map›Paper›PMID 12391148›Full record

ArticleMolecular and cellular biology2002

A RAG-1/RAG-2 tetramer supports 12/23-regulated synapsis, cleavage, and transposition of V(D)J recombination signals.

Patrick C Swanson

Erratum issuedOpen access · greenAbstract read
In one paragraph

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. An erratum has been issued. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.6field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

41 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. H3K4me3 induces allosteric conformational changes in the DNA-binding and catalytic regions of the V(D)J recombinase.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  5. 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 · 2016
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Single-molecule analysis of RAG-mediated V(D)J DNA cleavage.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  11. Article
  12. Article
  13. HMGB1 in health and disease.Molecular aspects of medicine · 2014
    Review
  14. Article
  15. Review
  16. Article
  17. Article
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4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

Patrick C SwansonDepartment of Medical Microbiology and Immunology, School of Medicine, Creighton University, Omaha, Nebraska 68178, USA. pswanson@creighton.edu
Creighton University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Initiation of V(D)J recombination involves the synapsis and cleavage of a 12/23 pair of recombination signal sequences by RAG-1 and RAG-2. Ubiquitous nonspecific DNA-bending factors of the HMG box family, such as HMG-1, are known to assist in these processes. After cleavage, the RAG proteins remain bound to the cut signal ends and, at least in vitro, support the integration of these ends into unrelated target DNA via a transposition-like mechanism. To investigate whether the protein complex supporting synapsis, cleavage, and transposition of V(D)J recombination signals utilized the same complement of RAG and HMG proteins, I compared the RAG protein stoichiometries and activities of discrete protein-DNA complexes assembled on intact, prenicked, or precleaved recombination signal sequence (RSS) substrates in the absence and presence of HMG-1. In the absence of HMG-1, I found that two discrete RAG-1/RAG-2 complexes are detected by mobility shift assay on all RSS substrates tested. Both contain dimeric RAG-1 and either one or two RAG-2 subunits. The addition of HMG-1 supershifts both complexes without altering the RAG protein stoichiometry. I find that 12/23-regulated recombination signal synapsis and cleavage are only supported in a protein-DNA complex containing HMG-1 and a RAG-1/RAG-2 tetramer. Interestingly, the RAG-1/RAG-2 tetramer also supports transposition, but HMG-1 is dispensable for its activity.

Indexed as

Chromosome PairingRecombination, GeneticCell LineDNADNA-Binding ProteinsGenes, RAG-1HMGB1 ProteinHomeodomain ProteinsHumansMacromolecular SubstancesNuclear ProteinsNucleic Acid ConformationProtein Sorting SignalsReceptors, Antigen, T-CellRecombinant Fusion ProteinsTransposasesDNADNA-Binding ProteinsHMGB1 ProteinHomeodomain ProteinsMacromolecular SubstancesNuclear ProteinsProtein Sorting SignalsRAG-1 proteinRAG2 protein, humanReceptors, Antigen, T-CellRecombinant Fusion ProteinsTransposasesV(D)J recombination activating protein 2

Identifiers

PMID12391148
PMCPMC134746
OpenAlexW2160186676

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.