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

View ORCID ProfilePetr Dvořák, View ORCID ProfileYuliya Krasylenko, View ORCID ProfileMiroslav Ovečka, View ORCID ProfileJasim Basheer, View ORCID ProfileVeronika Zapletalová, View ORCID ProfileJozef Šamaj, View ORCID ProfileTomáš Takáč
doi: https://doi.org/10.1101/2020.03.24.005363
Petr Dvořák
Department of Cell Biology, Centre of the Region Haná for Biotechnological and Agricultural Research, Faculty of Science, Palacký University Olomouc, Šlechtitelů 27, Olomouc, 783 71, Czech Republic
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Yuliya Krasylenko
Department of Cell Biology, Centre of the Region Haná for Biotechnological and Agricultural Research, Faculty of Science, Palacký University Olomouc, Šlechtitelů 27, Olomouc, 783 71, Czech Republic
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Miroslav Ovečka
Department of Cell Biology, Centre of the Region Haná for Biotechnological and Agricultural Research, Faculty of Science, Palacký University Olomouc, Šlechtitelů 27, Olomouc, 783 71, Czech Republic
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Jasim Basheer
Department of Cell Biology, Centre of the Region Haná for Biotechnological and Agricultural Research, Faculty of Science, Palacký University Olomouc, Šlechtitelů 27, Olomouc, 783 71, Czech Republic
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Veronika Zapletalová
Department of Cell Biology, Centre of the Region Haná for Biotechnological and Agricultural Research, Faculty of Science, Palacký University Olomouc, Šlechtitelů 27, Olomouc, 783 71, Czech Republic
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Jozef Šamaj
Department of Cell Biology, Centre of the Region Haná for Biotechnological and Agricultural Research, Faculty of Science, Palacký University Olomouc, Šlechtitelů 27, Olomouc, 783 71, Czech Republic
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Tomáš Takáč
Department of Cell Biology, Centre of the Region Haná for Biotechnological and Agricultural Research, Faculty of Science, Palacký University Olomouc, Šlechtitelů 27, Olomouc, 783 71, Czech Republic
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  • For correspondence: tomas.takac@upol.cz
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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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Posted March 25, 2020.
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FSD1: a plastidial, nuclear and cytoplasmic enzyme relocalizing to the plasma membrane under salinity
Petr Dvořák, Yuliya Krasylenko, Miroslav Ovečka, Jasim Basheer, Veronika Zapletalová, Jozef Šamaj, Tomáš Takáč
bioRxiv 2020.03.24.005363; doi: https://doi.org/10.1101/2020.03.24.005363
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FSD1: a plastidial, nuclear and cytoplasmic enzyme relocalizing to the plasma membrane under salinity
Petr Dvořák, Yuliya Krasylenko, Miroslav Ovečka, Jasim Basheer, Veronika Zapletalová, Jozef Šamaj, Tomáš Takáč
bioRxiv 2020.03.24.005363; doi: https://doi.org/10.1101/2020.03.24.005363

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