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Molecular dissection of a rice RING finger protein induced by salt and drought treatments
As sessile organisms, plants have evolved mechanisms that allow them to adapt and survive periods of various environmental stresses including high salinity and drought. The ubiquitin-proteasome system (UPS) is an integral player in plant response and adaptation to various abiotic stresses. Understanding UPS function has centered mainly on defining the role of E3 ubiquitin ligases, which are the substrate-recruiting component of the ubiquitination pathway. Here, we report on Ring finger E3 ligase, Oryza sativa salt- and drought-induced RING finger protein1 gene (OsSDRFP1) in defense responses to osmotic stresses. Results of qRT-PCR and In vitro ubiquitination assay demonstrated that OsSDRFP1 act as an E3 ligase in response to salt and drought stresses. in this study, Subcellular localizations showed that the OsSDRFP1 was observed in cytosol (66%) and nucleus (34%) under non-treated conditions. However, the florescence signals of rice protoplasts after salt treatments detected in nucleus (60%) higher than in cytosol (30%). The Arabidopsis plants overexpressing OsSDRFP1 clearly exhibited hypersensitive responses to salt stress. whereas, OsSDRFP1-overexpressing plants were more tolerant to both drought- and ABA-stresses than the wild-type plants. These results might suggest that OsSDRFP1 has a dual function as a regulator of high salt- and drought-stresses.
