Evidence map›Paper›PMID 23396834›Full record

ArticlePlant physiology2013

Phosphorylation of HopQ1, a type III effector from Pseudomonas syringae, creates a binding site for host 14-3-3 proteins.

Fabian Giska, Malgorzata Lichocka, Marcin Piechocki, Michał Dadlez, Elmon Schmelzer, Jacek Hennig, Magdalena Krzymowska

Abstract read
In one paragraph

Article in Plant physiology, 2013. 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
–field-weighted citation impact
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.

  1. Review
  2. Article
  3. Article
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  5. Article
  6. Review
  7. Multiple host targets ofbioRxiv : the preprint server for biology · 2023
    Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Salicylic acid-mediated plasmodesmal closure via Remorin-dependent lipid organization.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  15. Article
  16. Article
  17. NRG1 functions downstream of EDS1 to regulate TIR-NLR-mediated plant immunity inProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  18. Article
  19. Differential Suppression ofFrontiers in plant science · 2018
    Article
  20. Two Strategies ofFrontiers in plant science · 2018
    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

7 authors.

Fabian GiskaInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, 02-106 Warsaw, Poland.
Malgorzata Lichocka
Marcin Piechocki
Michał Dadlez
Elmon Schmelzer
Jacek Hennig
Magdalena Krzymowska

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

HopQ1 (for Hrp outer protein Q), a type III effector secreted by Pseudomonas syringae pv phaseolicola, is widely conserved among diverse genera of plant bacteria. It promotes the development of halo blight in common bean (Phaseolus vulgaris). However, when this same effector is injected into Nicotiana benthamiana cells, it is recognized by the immune system and prevents infection. Although the ability to synthesize HopQ1 determines host specificity, the role it plays inside plant cells remains unexplored. Following transient expression in planta, HopQ1 was shown to copurify with host 14-3-3 proteins. The physical interaction between HopQ1 and 14-3-3a was confirmed in planta using the fluorescence resonance energy transfer-fluorescence lifetime imaging microscopy technique. Moreover, mass spectrometric analyses detected specific phosphorylation of the canonical 14-3-3 binding site (RSXpSXP, where pS denotes phosphoserine) located in the amino-terminal region of HopQ1. Amino acid substitution within this motif abrogated the association and led to altered subcellular localization of HopQ1. In addition, the mutated HopQ1 protein showed reduced stability in planta. These data suggest that the association between host 14-3-3 proteins and HopQ1 is important for modulating the properties of this bacterial effector.

Indexed as

Bacterial Secretion SystemsHost-Pathogen Interactions14-3-3 ProteinsAmino Acid MotifsAmino Acid SequenceBacterial ProteinsBinding SitesChromatography, LiquidConserved SequenceFluorescence Resonance Energy TransferMass SpectrometryMolecular Sequence DataNicotianaPhaseolusPhosphorylationPhosphoserine14-3-3 ProteinsBacterial ProteinsBacterial Secretion SystemsPhosphoserinePlant Proteins

Identifiers

PMID23396834
PMCPMC3613475

What OpenQuestion holds

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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.