ArticleCommunications biology2024
Structural basis for the regulation of plant transcription factor WRKY33 by the VQ protein SIB1.
Article in Communications biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Functional and regulatory complexity: challenges and prospects for understanding rice WRKY transcription factors.Journal of experimental botany · 2026Review
- Heterologous Expression of the MelonPlants (Basel, Switzerland) · 2026Article
- How WRKY transcription factors fine-tune specificity in plant stress responses: from W-box to regulatory code.Molecular biology reports · 2026Review
- Functional and Mechanistic Insights into Plant VQ Proteins in Abiotic and Biotic Stress Responses.Plants (Basel, Switzerland) · 2025Review
- Inorganic carbon levels regulate growth via SigC signaling cascade in cyanobacteria.The New phytologist · 2025Article
- Macromolecular crystallography for mammalian body temperature in support of molecular biophysics methods.Biophysical reviews · 2025Review
- Genome-wide identification of HbVQ proteins and their interaction with HbWRKY14 to regulate the expression of HbSRPP in Hevea brasiliensis.BMC genomics · 2025Article
- Comparative insights into soybean and other oilseed crops' defense mechanisms againstFrontiers in plant science · 2025Review
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Authors and funding
11 authors.
Funding
Abstract
The WRKY transcription factors play essential roles in a variety of plant signaling pathways associated with biotic and abiotic stress response. The transcriptional activity of many WRKY members are regulated by a class of intrinsically disordered VQ proteins. While it is known that VQ proteins interact with the WRKY DNA-binding domains (DBDs), also termed as the WRKY domains, structural information regarding VQ-WRKY interaction is lacking and the regulation mechanism remains unknown. Herein we report a solution NMR study of the interaction between Arabidopsis WRKY33 and its regulatory VQ protein partner SIB1. We uncover a SIB1 minimal sequence neccessary for forming a stable complex with WRKY33 DBD, which comprises not only the consensus "FxxhVQxhTG" VQ motif but also its preceding region. We demonstrate that the β
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