Evidence map›Paper›PMID 19740377›Full record

ArticleImmunology2009

Correlation between recombinase activating gene 1 ubiquitin ligase activity and V(D)J recombination.

Carrie Simkus, Anamika Bhattacharyya, Ming Zhou, Timothy D Veenstra, Jessica M Jones

Open access · greenAbstract read
In one paragraph

Article in Immunology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

13 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Role of RAG1 autoubiquitination in V(D)J recombination.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Autoinhibition of DNA cleavage mediated by RAG1 and RAG2 is overcome by an epigenetic signal in V(D)J recombination.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  11. Article
  12. Article
  13. Cellular strategies for making monoubiquitin signals.Critical reviews in biochemistry and molecular biology
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Carrie SimkusDepartment of Biochemistry, Molecular and Cellular Biology, Georgetown University, Washington, DC 20057, USA.
Anamika Bhattacharyya
Ming Zhou
Timothy D Veenstra
Jessica M Jones
Georgetown University · USScience Applications International Corporation (United States) · US

Funding

Tissue Culture Shared ResourceP30CA051008 · NCI · GEORGETOWN UNIVERSITY · PI STEPHEN W BYERS · 1990 to 2026
$71.5M
Role of RAG1 Ubiquitin Ligase Activity in RecombinationR01AI062854 · NIAID · GEORGETOWN UNIVERSITY · PI JONES, JESSICA MORGAN · 2005 to 2009
$1.3M
Role of RAG1 Ubiquitin Ligase Activity in RecombinationR56AI062854 · NIAID · GEORGETOWN UNIVERSITY · PI JONES, JESSICA MORGAN · 2005 to 2005
$73k
NCI NIH HHS N01 CO012400NCI NIH HHS N01-CO-12400NCI NIH HHS P30 CA051008NCI NIH HHS P30CA051008NIAID NIH HHS AI062854-01NIAID NIH HHS R01 AI062854NIAID NIH HHS R56 AI062854
6 · The paper itself

Abstract

The really interesting new gene (RING) finger ubiquitin ligase domain of the recombinase activating gene 1 (RAG1) V(D)J recombinase protein adopts a standard cross-brace architecture but co-ordinates three zinc ions as opposed to the canonical two. We demonstrated previously that disruption of the conserved zinc co-ordination sites resulted in loss of structural integrity and ubiquitin ligase (E3) activity and interfered with the ability of full-length RAG1 to support recombination. Here we present evidence that amino acids surrounding the third, non-canonical site also contribute to functional interaction with the ubiquitin conjugating (E2) enzyme CDC34, while certain residues on the RING domain's surface important for interaction between other E2-E3 pairs are less critical to the functional RAG1-CDC34 interaction in this assay. Partial reduction of ubiquitin ligase activity was significantly correlated with reduction in the ability of RAG1 to support recombination of extra-chromosomal substrates (r = 0.805, P = 0.009). While poly-ubiquitin chains could be generated, RAG1 did not promote rapid chain extension following mono-ubiquitylation of substrate, regardless of the E2 enzyme used. No single ubiquitin lysine mutant disrupted the ability of CDC34 to form ubiquitin chains on RAG1, and mass spectrometric analysis of the poly-ubiquitylated products indicated ubiquitin chain linkages through lysines 48 and 11. These data suggest that RAG1 promotes a mono-ubiquitylation reaction that is required for optimal levels of V(D)J recombination.

Indexed as

Anaphase-Promoting Complex-CyclosomeAnimalsGenes, RAG-1Homeodomain ProteinsMiceMutagenesisRecombination, GeneticStructure-Activity RelationshipUbiquitinationUbiquitin-Protein Ligase ComplexesUbiquitin-Protein LigasesVDJ RecombinasesAnaphase-Promoting Complex-CyclosomeHomeodomain ProteinsRAG-1 proteinUbiquitin-Protein Ligase ComplexesUbiquitin-Protein LigasesVDJ Recombinases

Identifiers

PMID19740377
PMCPMC2767310
OpenAlexW1998372961

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.