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bioRxiv · 10.1101/2020.03.24.005363

FSD1: a plastidial, nuclear and cytoplasmic enzyme relocalizing to the plasma membrane under salinity

Dvorak, P.·Krasylenko, Y.·Ovecka, M.·Basheer, J.·Zapletalova, V.·Samaj, J.·Takac, T.
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Abstract

Here, we aimed to resolve the developmental expression and subcellular localization of Arabidopsis iron superoxide dismutase FSD1, which belongs to the family of superoxide dismutases (SODs), prominent enzymes decomposing superoxide anion and determining abiotic stress tolerance. We found that fsd1 knockout mutants exhibit reduced lateral root number and that this phenotype was complemented by proFSD1::GFP:FSD1 and proFSD1::FSD1:GFP constructs. Light sheet fluorescence microscopy revealed a temporary accumulation of FSD1-GFP at the site of endosperm rupture during seed germination. In emerged roots, FSD1-GFP showed the highest abundance in cells of the lateral root cap, columella, and endodermis/cortex initials. The largest subcellular pool of FSD1-GFP was localized in the plastid stroma, while it was also located in the nuclei and cytoplasm. FSD1 is crucial for seed germination and salt stress tolerance, which is tightly coupled with FSD1-GFP subcellular relocation to the plasma membrane. FSD1 is most likely involved in superoxide decomposition in the periplasm. This study suggests a new osmoprotective function of SODs in plants.

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Dvorak, P., Krasylenko, Y., Ovecka, M., Basheer, J., Zapletalova, V., Samaj, J., Takac, T.. 2020-03-25. FSD1: a plastidial, nuclear and cytoplasmic enzyme relocalizing to the plasma membrane under salinity. https://doi.org/10.1101/2020.03.24.005363

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