Evidence map›Paper›PMID 17350264›Full record

ArticleCurrent biology : CB2007

A J domain virulence effector of Pseudomonas syringae remodels host chloroplasts and suppresses defenses.

Joanna Jelenska, Nan Yao, Boris A Vinatzer, Christine M Wright, Jeffrey L Brodsky, Jean T Greenberg

Open access · greenAbstract read
In one paragraph

Article in Current biology : CB, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 124 papers.

0numbers the graph read from it
0cells of the map it votes in
124citing papers in PubMed
21.1field-weighted citation impact, top 1% 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

124 citing papers in PubMed, 298 citations in OpenAlex.

  1. Article
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  3. The Candidate Effector Cgmas2 Orchestrates Biphasic Infection ofInternational journal of molecular sciences · 2026
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  15. TheMolecules and cells · 2023
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  17. International journal of molecular sciences · 2023
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  19. Article
  20. Article

64 more citing papers are in PubMed but not listed here.

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

6 authors at 3 institutions in 2 countries.

Joanna JelenskaDepartment of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, Illinois 60637, USA.
Nan Yao
Boris A Vinatzer
Christine M Wright
Jeffrey L Brodsky
Jean T Greenberg
University of Chicago · USUniversity of Pittsburgh · USSun Yat-sen University · CN

Funding

ER Associated Degradation of Membrane Proteins in YeastR01GM075061 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BRODSKY, JEFFREY L. · 2006 to 2019
$3.2M
NIGMS NIH HHS GM75061NIGMS NIH HHS R01 GM075061
6 · The paper itself

Abstract

backgroundThe plant pathogen Pseudomonas syringae injects 20-40 different proteins called effectors into host plant cells, yet the functions and sites of action of these effectors in promoting pathogenesis are largely unknown. Plants in turn defend themselves against P. syringae by activating the salicylic acid (SA)-mediated signaling pathway. The P. syringae-specific HopI1 effector has a putative chloroplast-targeting sequence and a J domain. J domains function by activating 70 kDa heat-shock proteins (Hsp70).

resultsHopI1 is a ubiquitous P. syringae virulence effector that acts inside plant cells. When expressed in plants, HopI1 localizes to chloroplasts, the site of SA synthesis. HopI1 causes chloroplast thylakoid structure remodeling and suppresses SA accumulation. HopI1's C terminus has bona fide J domain activity that is necessary for HopI1-mediated virulence and thylakoid remodeling. Furthermore, HopI1-expressing plants have increased heat tolerance, establishing that HopI1 can engage the plant stress-response machinery.

conclusionsThese results strongly suggest that chloroplast Hsp70 is targeted by the P. syringae HopI1 effector to promote bacterial virulence by suppressing plant defenses. The targeting of Hsp70 function through J domain proteins is known to occur in a mammalian virus, SV40. However, this is the first example of a bacterial pathogen exploiting a J domain protein to promote pathogenesis through alterations of chloroplast structure and function.

Indexed as

ArabidopsisBacterial ProteinsChloroplastsHeat-Shock ResponseHSP70 Heat-Shock ProteinsMolecular Sequence DataNicotianaPhosphorylationPisum sativumProtein Structure, TertiaryPseudomonas syringaeSalicylic AcidSignal TransductionThylakoidsVirulence FactorsBacterial ProteinsHSP70 Heat-Shock ProteinsSalicylic AcidVirulence Factors

Identifiers

PMID17350264
PMCPMC1857343
OpenAlexW2140422929

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.