Evidence map›Paper›PMID 27909045›Full record

ArticlePlant physiology2017

A Subset of Ubiquitin-Conjugating Enzymes Is Essential for Plant Immunity.

Bangjun Zhou, Ravi V Mural, Xuanyang Chen, Matt E Oates, Richard A Connor, Gregory B Martin, Julian Gough, Lirong Zeng

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
14.4field-weighted citation impact, top 2% 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

32 citing papers in PubMed, 71 citations in OpenAlex.

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  15. SUMO conjugating enzyme: a vital player of SUMO pathway in plants.Physiology and molecular biology of plants : an international journal of functional plant biology · 2021
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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 1 institution in 3 countries.

Bangjun ZhouPlant Science Innovation Center and Plant Pathology Department, University of Nebraska, Lincoln, Nebraska 68583 (B.Z., L.Z.).ORCID 0000-0003-2986-6310
Ravi V MuralPlant Science Innovation Center and Plant Pathology Department, University of Nebraska, Lincoln, Nebraska 68583 (B.Z., L.Z.).ORCID 0000-0002-1173-0493
Xuanyang ChenPlant Science Innovation Center and Plant Pathology Department, University of Nebraska, Lincoln, Nebraska 68583 (B.Z., L.Z.).ORCID 0000-0002-3977-5554
Matt E OatesPlant Science Innovation Center and Plant Pathology Department, University of Nebraska, Lincoln, Nebraska 68583 (B.Z., L.Z.).ORCID 0000-0002-0001-3675
Richard A ConnorPlant Science Innovation Center and Plant Pathology Department, University of Nebraska, Lincoln, Nebraska 68583 (B.Z., L.Z.).
Gregory B MartinPlant Science Innovation Center and Plant Pathology Department, University of Nebraska, Lincoln, Nebraska 68583 (B.Z., L.Z.).ORCID 0000-0003-0044-6830
Julian GoughPlant Science Innovation Center and Plant Pathology Department, University of Nebraska, Lincoln, Nebraska 68583 (B.Z., L.Z.).ORCID 0000-0002-1965-4982
Lirong ZengPlant Science Innovation Center and Plant Pathology Department, University of Nebraska, Lincoln, Nebraska 68583 (B.Z., L.Z.); lzeng3@unl.edu.ORCID 0000-0001-8802-4872
University of Arkansas at Little Rock · US

Funding

Biotechnology and Biological Sciences Research Council BB/G022771/1
6 · The paper itself

Abstract

Of the three classes of enzymes involved in ubiquitination, ubiquitin-conjugating enzymes (E2) have been often incorrectly considered to play merely an auxiliary role in the process, and few E2 enzymes have been investigated in plants. To reveal the role of E2 in plant innate immunity, we identified and cloned 40 tomato genes encoding ubiquitin E2 proteins. Thioester assays indicated that the majority of the genes encode enzymatically active E2. Phylogenetic analysis classified the 40 tomato E2 enzymes into 13 groups, of which members of group III were found to interact and act specifically with AvrPtoB, a Pseudomonas syringae pv tomato effector that uses its ubiquitin ligase (E3) activity to suppress host immunity. Knocking down the expression of group III E2 genes in Nicotiana benthamiana diminished the AvrPtoB-promoted degradation of the Fen kinase and the AvrPtoB suppression of host immunity-associated programmed cell death. Importantly, silencing group III E2 genes also resulted in reduced pattern-triggered immunity (PTI). By contrast, programmed cell death induced by several effector-triggered immunity elicitors was not affected on group III-silenced plants. Functional characterization suggested redundancy among group III members for their role in the suppression of plant immunity by AvrPtoB and in PTI and identified UBIQUITIN-CONJUGATING11 (UBC11), UBC28, UBC29, UBC39, and UBC40 as playing a more significant role in PTI than other group III members. Our work builds a foundation for the further characterization of E2s in plant immunity and reveals that AvrPtoB has evolved a strategy for suppressing host immunity that is difficult for the plant to thwart.

Indexed as

Bacterial ProteinsCell DeathGene SilencingGenome, PlantHost-Pathogen InteractionsNicotianaPhylogenyPlant ImmunityPlant ProteinsPlants, Genetically ModifiedProtein Serine-Threonine KinasesPseudomonas syringaeSolanum lycopersicumUbiquitinationUbiquitin-Conjugating EnzymesavrPto protein, Pseudomonas syringaeBacterial ProteinsFen protein, Lycopersicon esculentumPlant ProteinsProtein Serine-Threonine KinasesUbiquitin-Conjugating Enzymes

Identifiers

PMID27909045
PMCPMC5291023
OpenAlexW2559461289

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.