Cited by 29Ubiquitin and proteasome pathwaysPlant Stress Responses and TolerancePlant Molecular Biology Research

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Wheat RING E3 ubiquitin ligase TaDIS1 degrade TaSTP via the 26S proteasome pathway

Lv, Qian, Zhang, Li, Zan, Ting, Li, Liqun, Li, Xuejun·2020·Plant Science

DOI 10.1016/j.plantsci.2020.110494

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Abstract

Drought stress has a great impact on wheat yields. The ubiquitin/26S proteasome system is one of the most important mechanisms employed by plants for responding to stress. E3 ubiquitin ligase is an important part of the ubiquitin/26S proteasome system. In wheat, the mechanism of E3 ubiquitin ligase TaDIS1 has not been investigated in great detail. In this study, TaSTP was identified as an interacting partner using yeast two-hybrid screening. The results obtained from bimolecular fluorescence complementation, pull-down, and co-immunoprecipitation assays also demonstrated that TaDIS1 interacts with TaSTP. In vitro ubiquitination assays showed that TaDIS1 has an E3 ubiquitin ligase activity and the results based on two TaDIS1 mutants suggested that the RING domain is essential for its E3 ubiquitin ligase activity. In addition, we used MG132 to show that TaSTP can be degraded by TaDIS1 via the 26S proteasome pathway. The transcript levels of TaSTP showed that it can also respond to different abiotic stresses, such as drought, salt, and abscisic acid treatment. RING E3 ubiquitin ligase TaDIS1 may through the posttranslational regulation of TaSTP to play an important role in drought tolerance.

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Authors: Lv, Q., Zhang, L., Zan, T., Li, L., & Li, X.
Affiliations: Northwest A&F University (CN)
Corresponding author: Li, Xuejun
ORCID: Li, Liqun
Venue: Plant Science
Publisher: Elsevier BV
Published: 2020-07
Volume: 296
Pages: 110494
ISSN: 0168-9452 (ISSN-L)
DOI: 10.1016/j.plantsci.2020.110494
OpenAlex: W3018683072
Cited by: 29
References: 46
Citations by year: 2026: 2 · 2025: 4 · 2024: 8 · 2023: 5 · 2022: 5 · 2021: 5
FWCI: 1.22
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Plant Science (publishedVersion)
PubMed (publishedVersion)
Funders: National Key R&D Program of China (2017YFD0100704)
National Special Program for Transgenetic Wheat Breeding (2016ZX08002003)
State Administration of Foreign Experts Affairs (#B18042)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Stress Responses and Tolerance
Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
Keywords: RING E3 ubiquitin ligase, 26S proteasome, protein degradation, drought tolerance, wheat, protein-protein interaction, abiotic stress response, abscisic acid, salt stress, post-translational regulation
MeSH terms: Cloning, Molecular, Dehydration, Plant Proteins, Triticum, Gene Expression Regulation, Plant, Two-Hybrid System Techniques, Ubiquitin-Protein Ligases, Proteasome Endopeptidase Complex, Immunoprecipitation, Metabolic Networks and Pathways

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Wheat RING E3 ubiquitin ligase TaDIS1 degrade TaSTP via the 26S proteasome pathway

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