ArticleJournal of virology2013
SCE1, the SUMO-conjugating enzyme in plants that interacts with NIb, the RNA-dependent RNA polymerase of Turnip mosaic virus, is required for viral infection.
Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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.
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.
Who cites it
35 citing papers in PubMed, 82 citations in OpenAlex.
- SUMOylation in plants: A versatile post-translational mechanism responding to environmental stresses.Journal of integrative plant biology · 2026Review
- Potato Virus Y NIb Multifunctional Protein Suppresses Antiviral Defense by Interacting with Several Protein Components of the RNA Silencing Pathway.International journal of molecular sciences · 2026Article
- Viral RNA polymerase as a SUMOylation decoy inhibits RNA quality control to promote potyvirus infection.Nature communications · 2025Article
- Definition and regulatory analysis of the SUMOylation system in Caixin (Brassica rapa var. Parachinensis) during pectobacterium carotovorum infection.BMC plant biology · 2024Article
- The 2 faces of plant SUMOylation against viruses.PLoS pathogens · 2024Article
- The melonPlant direct · 2024Article
- A plant RNA virus inhibits NPR1 sumoylation and subverts NPR1-mediated plant immunity.Nature communications · 2023Article
- A binary interaction map between turnip mosaic virus and Arabidopsis thaliana proteomes.Communications biology · 2023Article
- Maize Lethal Necrosis disease: review of molecular and genetic resistance mechanisms, socio-economic impacts, and mitigation strategies in sub-Saharan Africa.BMC plant biology · 2022Review
- The Role of Protein SUMOylation in Human Hepatocellular Carcinoma: A Potential Target of New Drug Discovery and Development.Cancers · 2021Review
- SUMO conjugating enzyme: a vital player of SUMO pathway in plants.Physiology and molecular biology of plants : an international journal of functional plant biology · 2021Review
- Plant responses to geminivirus infection: guardians of the plant immunity.Virology journal · 2021Review
- SUMOylation in Phytopathogen Interactions: Balancing Invasion and Resistance.Frontiers in cell and developmental biology · 2021Review
- Functional Characterization of Pepper Vein Banding Virus-Encoded Proteins and Their Interactions: Implications inViruses · 2020Review
- Article
- The RNA-Dependent RNA Polymerase NIb of Potyviruses Plays Multifunctional, Contrasting Roles during Viral Infection.Viruses · 2020Review
- The Maize Class-I SUMO Conjugating Enzyme ZmSCE1d Is Involved in Drought Stress Response.International journal of molecular sciences · 2019Article
- Article
- Roles of Small RNAs in Virus-Plant Interactions.Viruses · 2019Review
- SUMO1 Modification Facilitates Avibirnavirus Replication by Stabilizing Polymerase VP1.Journal of virology · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SUMOylation, which is catalyzed by small ubiquitin-like modifier (SUMO) enzymes, is a transient, reversible posttranslational protein modification that regulates diverse cellular processes. Potyviruses, the largest group of known plant viruses, comprise many agriculturally important viruses, such as Turnip mosaic virus (TuMV). The potyviral genome encodes 11 mature proteins. To investigate if SUMOylation plays a role in potyvirus infection, a yeast two-hybrid screen was performed to examine possible interactions of each of the 11 viral proteins of TuMV with AtSCE1, the only SUMO-conjugating enzyme in Arabidopsis thaliana homologous to the key SUMO-conjugating enzyme E2 in mammalian cells or Ubc9 in yeast. A positive reaction was found between AtSCE1 and NIb, the potyviral RNA-dependent RNA polymerase. Further bimolecular fluorescence complementation (BiFC) and fluorescence resonance energy transfer (FRET) assays revealed that the NIb and AtSCE1 interaction occurred in both the cytoplasm and nuclei of epidermal cells of Nicotiana benthamiana. The interaction motif was mapped to a region encompassing NIb amino acids 171 to 300 which contains a potential negatively charged amino acid-dependent SUMOylation motif (NDSM). An Escherichia coli SUMOylation assay showed that NIb can be SUMOylated and that the lysine residue (K172) in the motif is a potent SUMOylation site. A TuMV infectious clone with an arginine (R) substitution mutation at K172 compromised TuMV infectivity in plants. In comparison with wild-type Arabidopsis plants, sce1 knockdown plants exhibited increased resistance to TuMV as well as a nonrelated RNA virus. To the best of our knowledge, this is the first report showing that the host SUMO modification system plays an essential role in infection by plant RNA viruses.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.