Evidence map›Paper›PMID 30924604›Full record

ArticleMolecular plant pathology2019

An E3 ubiquitin ligase from Nicotiana benthamiana targets the replicase of Bamboo mosaic virus and restricts its replication.

I-Hsuan Chen, Jui-En Chang, Chen-Yu Wu, Ying-Ping Huang, Yau-Huei Hsu, Ching-Hsiu Tsai

Open access · goldAbstract read
In one paragraph

Article in Molecular plant pathology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.0field-weighted citation impact, top 12% 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

14 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
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  3. Article
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  8. Proviral insights of glycolytic enolase inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Review
  10. Article
  11. The Great Game between Plants and Viruses: A Focus on Protein Homeostasis.International journal of molecular sciences · 2023
    Review
  12. Article
  13. Article
  14. 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

6 authors at 1 institution in 1 country.

I-Hsuan ChenGraduate Institute of Biotechnology, National Chung Hsing University, Taichung, 402, Taiwan.
Jui-En ChangGraduate Institute of Biotechnology, National Chung Hsing University, Taichung, 402, Taiwan.
Chen-Yu WuGraduate Institute of Biotechnology, National Chung Hsing University, Taichung, 402, Taiwan.
Ying-Ping HuangGraduate Institute of Biotechnology, National Chung Hsing University, Taichung, 402, Taiwan.
Yau-Huei HsuGraduate Institute of Biotechnology, National Chung Hsing University, Taichung, 402, Taiwan.
Ching-Hsiu TsaiGraduate Institute of Biotechnology, National Chung Hsing University, Taichung, 402, Taiwan.ORCID 0000-0003-3744-8821
National Chung Hsing University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

One up-regulated host gene identified previously was found involved in the infection process of Bamboo mosaic virus (BaMV), a single-stranded positive-sense RNA virus. The full length cDNA of this gene was cloned by 5' and 3'-rapid amplification of cDNA ends and found to encode a polypeptide containing a conserved really interesting new gene (RING) domain and a transmembrane domain. The gene might function as an ubiquitin E3 ligase. We designated this protein in Nicotiana benthamiana as ubiquitin E3 ligase containing RING domain 1 (NbUbE3R1). Further characterization by using Tobacco rattle virus-based virus-induced gene silencing (loss-of-function) revealed that increased BaMV accumulation was in both knockdown plants and protoplasts. The gene might have a defensive role in the replication step of BaMV infection. To further inspect the functional role of NbUbE3R1 in BaMV accumulation, NbUbE3R1 was expressed in N. benthamiana plants. The wild-type NbUbE3R1-orange fluorescent protein (NbUbE3R1-OFP), NbUbE3R1/△TM-OFP (removal of the transmembrane domain) and NbUbE3R1/mRING-OFP (mutation at the RING domain, the E2 interaction site) were transiently expressed in plants. NbUbE3R1 and its derivatives all functioned in restricting the accumulation of BaMV. The common feature of these constructs was the intact substrate-interacting domain. Yeast two-hybrid and co-immunoprecipitation experiments used to determine the possible viral-encoded substrate of NbUbE3R1 revealed the replicase of BaMV as the possible substrate. In conclusion, we identified an up-regulated gene, NbUbE3R1 that plays a role in BaMV replication.

Indexed as

Capsid ProteinsDNA, ComplementaryGene Expression Regulation, PlantGenes, PlantLeupeptinsNicotianaPlant DiseasesPlant ProteinsPotexvirusProtein BindingProtein StabilityRNA-Dependent RNA PolymeraseSaccharomyces cerevisiaeSubcellular FractionsUbiquitin-Protein LigasesUp-Regulationbenzyloxycarbonylleucyl-leucyl-leucine aldehydeCapsid ProteinsDNA, ComplementaryLeupeptinsPlant ProteinsRNA-Dependent RNA PolymeraseUbiquitin-Protein LigasesBamboo mosaic virusE3 ubiquitin ligaseNicotiana benthamianaprotein-protein interactionRNA-dependent RNA polymeraseviral RNA replicationyeast two-hybrid

Identifiers

PMID30924604
PMCPMC6637893
OpenAlexW2895596143

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.