Evidence map›Paper›PMID 21199565›Full record

ArticleMolecular plant pathology2011

Functional mapping of harpin HrpZ of Pseudomonas syringae reveals the sites responsible for protein oligomerization, lipid interactions and plant defence induction.

Minna Haapalainen, Stefan Engelhardt, Isabell Küfner, Chun-Mei Li, Thorsten Nürnberger, Justin Lee, Martin Romantschuk, Suvi Taira

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In one paragraph

Article in Molecular plant pathology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
7.5field-weighted citation impact, top 3% 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

33 citing papers in PubMed, 71 citations in OpenAlex.

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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

8 authors at 4 institutions in 3 countries.

Minna HaapalainenGeneral Microbiology, Department of Biological and Environmental Sciences, FI-00014 University of Helsinki, Helsinki, Finland. Minna.Haapalainen@helsinki.fi
Stefan Engelhardt
Isabell Küfner
Chun-Mei Li
Thorsten Nürnberger
Justin Lee
Martin Romantschuk
Suvi Taira
University of Helsinki · FIUniversity of Tübingen · DEJames Hutton Institute · GBLeibniz Institute of Plant Biochemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Harpin HrpZ is one of the most abundant proteins secreted through the pathogenesis-associated type III secretion system of the plant pathogen Pseudomonas syringae. HrpZ shows membrane-binding and pore-forming activities in vitro, suggesting that it could be targeted to the host cell plasma membrane. We studied the native molecular forms of HrpZ and found that it forms dimers and higher order oligomers. Lipid binding by HrpZ was tested with 15 different membrane lipids, with HrpZ interacting only with phosphatidic acid. Pore formation by HrpZ in artificial lipid vesicles was found to be dependent on the presence of phosphatidic acid. In addition, HrpZ was able to form pores in vesicles prepared from Arabidopsis thaliana plasma membrane, providing evidence for the suggested target of HrpZ in the host. To map the functions associated with HrpZ, we constructed a comprehensive series of deletions in the hrpZ gene derived from P. syringae pv. phaseolicola, and studied the mutant proteins. We found that oligomerization is mainly mediated by a region near the C-terminus of the protein, and that the same region is also essential for membrane pore formation. Phosphatidic acid binding seems to be mediated by two regions separate in the primary structure. Tobacco, a nonhost plant, recognizes, as a defence elicitor, a 24-amino-acid HrpZ fragment which resides in the region indispensable for the oligomerization and pore formation functions of HrpZ.

Indexed as

Lipid MetabolismAmino Acid SequenceArabidopsisBacterial Outer Membrane ProteinsMolecular Sequence DataMutant ProteinsNicotianaPeptidesPhosphatidic AcidsProtein BindingProtein Structure, QuaternaryProtein Structure, TertiaryProtein SubunitsPseudomonas syringaeSequence DeletionStructure-Activity RelationshipBacterial Outer Membrane ProteinsHrpZ protein, Pseudomonas syringaeMutant ProteinsPeptidesPhosphatidic AcidsProtein Subunits

Identifiers

PMID21199565
PMCPMC6640321
OpenAlexW2145163823

What OpenQuestion holds

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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.