Evidence map›Paper›PMID 23248273›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Disassembly of synthetic Agrobacterium T-DNA-protein complexes via the host SCF(VBF) ubiquitin-ligase complex pathway.

Adi Zaltsman, Benoît Lacroix, Yedidya Gafni, Vitaly Citovsky

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

19 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. International journal of molecular sciences · 2020
    Article
  6. Pathways of DNA Transfer to Plants fromAnnual review of phytopathology · 2019
    Article
  7. Article
  8. Article
  9. Virulence protein VirD5 ofProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Assaying proteasomal degradation in a cell-free system in plants.Journal of visualized experiments : JoVE · 2014
    Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
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

4 authors at 3 institutions in 2 countries.

Adi ZaltsmanDepartment of Biochemistry and Cell Biology, State University of New York, Stony Brook, NY 11794, USA.
Benoît Lacroix
Yedidya Gafni
Vitaly Citovsky
Stony Brook University · USAgricultural Research Organization · ILState University of New York · US

Funding

TRANSPORT THROUGH PLASMODESMATAR01GM050224 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI CITOVSKY, VITALY H · 1994 to 2020
$5.7M
NIGMS NIH HHS R01 GM050224
6 · The paper itself

Abstract

One the most intriguing, yet least studied, aspects of the bacterium-host plant interaction is the role of the host ubiquitin/proteasome system (UPS) in the infection process. Increasing evidence indicates that pathogenic bacteria subvert the host UPS to facilitate infection. Although both mammalian and plant bacterial pathogens are known to use the host UPS, the first prokaryotic F-box protein, an essential component of UPS, was identified in Agrobacterium. During its infection, which culminates in genetic modification of the host cell, Agrobacterium transfers its T-DNA--as a complex (T-complex) with the bacterial VirE2 and host VIP1 proteins--into the host cell nucleus. There the T-DNA is uncoated from its protein components before undergoing integration into the host genome. It has been suggested that the host UPS mediates this uncoating process, but there is no evidence indicating that this activity can unmask the T-DNA molecule. Here we provide support for the idea that the plant UPS uncoats synthetic T-complexes via the Skp1/Cullin/F-box protein VBF pathway and exposes the T-DNA molecule to external enzymatic activity.

Indexed as

Active Transport, Cell NucleusAgrobacteriumArabidopsis ProteinsBacterial ProteinsBlotting, WesternDNA, BacterialDNA-Binding ProteinsDNA PrimersHost-Pathogen InteractionsIon ChannelsMacromolecular SubstancesNicotianaProteasome Endopeptidase ComplexReverse Transcriptase Polymerase Chain ReactionTransformation, GeneticArabidopsis ProteinsBacterial ProteinsDNA, BacterialDNA-Binding ProteinsDNA PrimersIon ChannelsMacromolecular SubstancesProteasome Endopeptidase ComplexT-DNAVIP1 protein, ArabidopsisvirE2 protein, Agrobacterium

Identifiers

PMID23248273
PMCPMC3538200
OpenAlexW2033478551

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.