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FeSTAR2 interacted by FeSTAR1 alters its subcellular location and regulates Al tolerance in buckwheat
- Xu, Jia Meng, Wang, Zhan Qi, Jin, Jian Feng, Chen, Wei Wei, Fan, Wei, Zheng, Shao Jian, Yang, Jian Li
- Plant and soil 2019 v.436 no.1-2 pp. 489-501
- ABC transporters, Arabidopsis, Fagopyrum esculentum, aluminum, buckwheat, fluorescence, genes, hemicellulose, heterologous gene expression, hypersensitivity, metabolism, mutants, two hybrid system techniques, xyloglucan:xyloglucosyl transferase
- AIMS: Buckwheat (Fagopyrum esculentum) exhibits high Al tolerance, but only a few genes have been functionally characterized. We previously characterized a half-type ABC transporter, Fagopyrum esculentum sensitive to Al rhizotoxicity1 (FeSTAR1), in buckwheat Al tolerance. This study aims to investigate whether and how another half-type ABC transporter (FeSTAR2) plays role in Al tolerance in buckwheat. METHODS: The expression of FeSTAR2 and complementation test in Arabidopsis als3 mutant was examined. The interaction between FeSTAR1 and FeSTAR2 and subcellular location were analyzed by bimolecular fluorescence complementation (BiFC) and yeast two-hybrid (Y2H) assays. RESULTS: Al rapidly and specifically induced FeSTAR2 expression. Having transmembrane domains, FeSTAR2 localizes to membrane. BiFC and Y2H assays showed that FeSTAR2 could interact with FeSTAR1 which contains only nucleotide binding domain. Intriguingly, interaction between FeSTAR1 and FeSTAR2 altered their locations. Both heterologous expression of FeSTAR2 in als3 and exogenous UDP-glucose rescued its Al hypersensitivity of als3 mutant, suggesting that involvement of FeSTAR2 in Al tolerance requires UDP-glucose. Furthermore, Al-induced inhibition of xyloglucan endotransglucosylase (XET) activity in both atstar1 and als3 mutants could be restored by UDP-glucose. CONCLUSION: Our results indicate that FeSTAR2 interacts with FeSTAR1 to form an ABC transporter to regulate Al tolerance by vesicular transport of UDP-glucose which affects hemicellulose metabolism by regulating XET activity.