RT Journal Article
SR Electronic
T1 FSD1: a plastidial, nuclear and cytoplasmic enzyme relocalizing to the plasma membrane under salinity
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2020.03.24.005363
DO 10.1101/2020.03.24.005363
A1 Petr Dvořák
A1 Yuliya Krasylenko
A1 Miroslav Ovečka
A1 Jasim Basheer
A1 Veronika Zapletalová
A1 Jozef Šamaj
A1 Tomáš Takáč
YR 2020
UL http://biorxiv.org/content/early/2020/03/25/2020.03.24.005363.abstract
AB 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.