The role and pathway of VQ family in plant growth, immunity, and stress response

Tian, Jinfu; Zhang, Jiahui; Francis, Frédéric

doi:10.1007/s00425-023-04292-z

Planta

2023

DOI: 10.1007/s00425-023-04292-z

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The role and pathway of VQ family in plant growth, immunity, and stress response

Jinfu Tian,

Jiahui Zhang,

Frédéric Francis

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2024

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Cited by 2 publications

References 178 publications

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Arabidopsis VQ motif-containing proteins VQ1 and VQ10 interact with plastidial 1-deoxy-D-xylulose-5-phosphate synthase

Gayubas,

Castillo,

León

2024

Sci Rep

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VQ1 and VQ10 are largely unstructured homologous proteins with a significant potential for protein–protein interactions. Yeast two-hybrid (Y2H) analysis confirmed that both proteins interact not only with themselves and each other but also with other VQ and WRKY proteins. Screening an Arabidopsis Y2H library with VQ1 as bait identified 287 interacting proteins. Validation of the screening confirmed that interactions with VQ1 also occurred with VQ10, supporting their functional homology. Although VQ1 or VQ10 proteins do not localize in plastids, 47 VQ1-targets were found to be plastidial proteins. In planta interaction with the isoprenoid biosynthetic enzyme 1-deoxy-D-xylulose-5-phosphate synthase (DXS) was confirmed by co-immunoprecipitation. DXS oligomerizes through redox-regulated intermolecular disulfide bond formation, and the interaction with VQ1 or VQ10 do not involve their unique C residues. The VQ-DXS protein interaction did not alter plastid DXS localization or its oligomerization state. Although plants with enhanced or reduced VQ1 and VQ10 expression did not exhibit significantly altered levels of isoprenoids compared to wild-type plants, they did display significantly improved or diminished photosynthesis efficiency, respectively.

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Arabidopsis VQ motif-containing proteins VQ1 and VQ10 interact with plastidial 1-deoxy-D-xylulose-5-phosphate synthase

Gayubas,

Castillo,

León

2024

Sci Rep

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SlWRKY51 regulates proline content to enhance chilling tolerance in tomato

Wang,

Zhang,

et al. 2024

Plant Cell & Environment

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Chilling stress is a major environmental factor that significantly reduces crop production. To adapt to chilling stress, plants activate a series of cellular responses and accumulate an array of metabolites, particularly proline. Here, we report that the transcription factor SlWRKY51 increases proline contents in tomato (Solanum lycopersicum) under chilling stress. SlWRKY51 expression is induced under chilling stress. Knockdown or knockout of SlWRKY51 led to chilling‐sensitive phenotypes, with lower photosynthetic capacity and more reactive oxygen species (ROS) accumulation than the wild type (WT). The proline contents were significantly reduced in SlWRKY51 knockdown and knockout lines under chilling stress, perhaps explaining the phenotypes of these lines. D‐1‐pyrroline‐5‐carboxylate synthetase (P5CS), which catalyses the rate‐limiting step of proline biosynthesis, is encoded by two closely related P5CS genes (P5CS1 and P5CS2). We demonstrate that SlWRKY51 directly activates the expression of P5CS1 under chilling stress. In addition, the VQ (a class of plant‐specific proteins containing the conserved motif FxxhVQxhTG) family member SlVQ10 physically interacts with SlWRKY51 to enhance its activation of P5CS1. Our study reveals that the chilling‐induced transcription factor SlWRKY51 enhances chilling tolerance in tomato by promoting proline accumulation.

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The role and pathway of VQ family in plant growth, immunity, and stress response

Cited by 2 publications

References 178 publications

Arabidopsis VQ motif-containing proteins VQ1 and VQ10 interact with plastidial 1-deoxy-D-xylulose-5-phosphate synthase

Arabidopsis VQ motif-containing proteins VQ1 and VQ10 interact with plastidial 1-deoxy-D-xylulose-5-phosphate synthase

SlWRKY51 regulates proline content to enhance chilling tolerance in tomato

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