ArticleBMC plant biology2019
Overexpression of OsPUB41, a Rice E3 ubiquitin ligase induced by cell wall degrading enzymes, enhances immune responses in Rice and Arabidopsis.
Article in BMC plant biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 28 citations in OpenAlex.
- E3 ubiquitin ligases in plant defense: mechanisms and prospects for resistance breeding.Science China. Life sciences · 2026Review
- Metabolomic and Transcriptomic Responses ofPlants (Basel, Switzerland) · 2026Article
- Ubiquitin-Mediated Proteolysis as a Regulator of the Plant Defense-Growth Balance.Plants (Basel, Switzerland) · 2026Review
- MdPOB1L Positively Regulates Disease Resistance Against Botryosphaeria dothidea by Manipulating MdNPR1 Protein Stability in Malus domestica.Molecular plant pathology · 2025Article
- Elucidating the mechanism of resistance to anthracnose in litchi leaves through transcriptome analysis.BMC plant biology · 2025Article
- Rice E3 ubiquitin ligases: From key modulators of host immunity to potential breeding applications.Plant communications · 2024Review
- Expression Profiling Reveals the Possible Involvement of the Ubiquitin-Proteasome Pathway in Abiotic Stress Regulation inInternational journal of molecular sciences · 2023Article
- Genome and Transcriptome Sequencing Analysis of FusariumMicrobiology spectrum · 2022Article
- Evolutionary and Characteristic Analysis of RING-DUF1117 E3 Ubiquitin Ligase Genes inBiomolecules · 2021Article
- Understanding and Exploiting Post-Translational Modifications for Plant Disease Resistance.Biomolecules · 2021Review
- OsPUB41, a U-box E3 ubiquitin ligase, acts as a negative regulator of drought stress response in rice (Oryza Sativa L.).Plant molecular biology · 2021Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
backgroundCell wall degrading enzymes (CWDEs) induce plant immune responses and E3 ubiquitin ligases are known to play important roles in regulating plant defenses. Expression of the rice E3 ubiquitin ligase, OsPUB41, is enhanced upon treatment of leaves with Xanthomonas oryzae pv. oryzae (Xoo) secreted CWDEs such as Cellulase and Lipase/Esterase. However, it is not reported to have a role in elicitation of immune responses.
resultsExpression of the rice E3 ubiquitin ligase, OsPUB41, is induced when rice leaves are treated with either CWDEs, pathogen associated molecular patterns (PAMPs), damage associated molecular patterns (DAMPs) or pathogens. Overexpression of OsPUB41 leads to induction of callose deposition, enhanced tolerance to Xoo and Rhizoctonia solani infection in rice and Arabidopsis respectively. In rice, transient overexpression of OsPUB41 leads to enhanced expression of PR genes and SA as well as JA biosynthetic and response genes. However, in Arabidopsis, ectopic expression of OsPUB41 results in upregulation of only JA biosynthetic and response genes. Transient overexpression of either of the two biochemically inactive mutants (OsPUB41C40A and OsPUB41V51R) of OsPUB41 in rice and stable transgenics in Arabidopsis ectopically expressing OsPUB41C40A failed to elicit immune responses. This indicates that the E3 ligase activity of OsPUB41 protein is essential for induction of plant defense responses.
conclusionThe results presented here suggest that OsPUB41 is possibly involved in elicitation of CWDE triggered immune responses in rice.
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