Evidence map›Paper›PMID 20696004›Full record

ArticleMolecular plant pathology2010

The Xanthomonas citri effector protein PthA interacts with citrus proteins involved in nuclear transport, protein folding and ubiquitination associated with DNA repair.

Mariane Noronha Domingues, Tiago Antonio De Souza, Raúl Andrés Cernadas, Maria Luiza Peixoto de Oliveira, Cássia Docena, Chuck Shaker Farah, Celso Eduardo Benedetti

Open access · bronzeAbstract read
In one paragraph

Article in Molecular plant pathology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
5.4field-weighted citation impact, top 5% 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

28 citing papers in PubMed, 52 citations in OpenAlex.

  1. eLife · 2024
    Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. PthA4Molecular plant pathology · 2019
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
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  19. Review
  20. 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

7 authors at 3 institutions in 2 countries.

Mariane Noronha DominguesCentro Nacional de Pesquisa em Energia e Materiais, Campinas, SP, Brazil.
Tiago Antonio De Souza
Raúl Andrés Cernadas
Maria Luiza Peixoto de Oliveira
Cássia Docena
Chuck Shaker Farah
Celso Eduardo Benedetti
Laboratório Nacional de Ciência e Tecnologia do Bioetanol · BRUniversidade de São Paulo · BRIowa State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Xanthomonas axonopodis pv. citri utilizes the type III effector protein PthA to modulate host transcription to promote citrus canker. PthA proteins belong to the AvrBs3/PthA family and carry a domain comprising tandem repeats of 34 amino acids that mediates protein-protein and protein-DNA interactions. We show here that variants of PthAs from a single bacterial strain localize to the nucleus of plant cells and form homo- and heterodimers through the association of their repeat regions. We hypothesize that the PthA variants might also interact with distinct host targets. Here, in addition to the interaction with alpha-importin, known to mediate the nuclear import of AvrBs3, we describe new interactions of PthAs with citrus proteins involved in protein folding and K63-linked ubiquitination. PthAs 2 and 3 preferentially interact with a citrus cyclophilin (Cyp) and with TDX, a tetratricopeptide domain-containing thioredoxin. In addition, PthAs 2 and 3, but not 1 and 4, interact with the ubiquitin-conjugating enzyme complex formed by Ubc13 and ubiquitin-conjugating enzyme variant (Uev), required for K63-linked ubiquitination and DNA repair. We show that Cyp, TDX and Uev interact with each other, and that Cyp and Uev localize to the nucleus of plant cells. Furthermore, the citrus Ubc13 and Uev proteins complement the DNA repair phenotype of the yeast Deltaubc13 and Deltamms2/uev1a mutants, strongly indicating that they are also involved in K63-linked ubiquitination and DNA repair. Notably, PthA 2 affects the growth of yeast cells in the presence of a DNA damage agent, suggesting that it inhibits K63-linked ubiquitination required for DNA repair.

Indexed as

DNA RepairProtein FoldingUbiquitinationActive Transport, Cell NucleusBacterial ProteinsCell NucleusCitrusLeucine-Rich Repeat ProteinsLysineNicotianaPlant ProteinsProtein BindingProtein MultimerizationProteinsProtein Structure, TertiaryTranscription Activator-Like EffectorsBacterial ProteinsLeucine-Rich Repeat ProteinsLysinePlant ProteinsProteinsPthA protein, Xanthomonas campestrisTranscription Activator-Like Effectors

Identifiers

PMID20696004
PMCPMC6640223
OpenAlexW2155659941

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.