Abstract
SRO1 is an important regulator of stress and hormonal response in plants and functions by interacting with transcription factors and several other proteins involved in abiotic stress response. In the present study, we report OsRBD1, an RNA binding domain 1- containing protein as a novel interacting partner of OsSRO1a from rice. The interaction of OsSRO1a with OsRBD1 was shown in yeast as well as in planta. Domain–domain interaction study revealed that C-terminal RST domain of OsSRO1a interacts with the N-terminal RRM1 domain of OsRBD1 protein. Both the proteins were found to co-localize in nucleus. Transcript profiling under different stress conditions revealed co-regulation of OsSRO1a and OsRBD1 expression under some abiotic stress conditions. Further, co-transformation of both OsSRO1a and OsRBD1 in yeast conferred enhanced tolerance toward salinity, osmotic, and methylglyoxal treatments. Our study suggests that the interaction of OsSRO1a with OsRBD1 confers enhanced stress tolerance in yeast and may play an important role under abiotic stress responses in plants.
Highlights
RCD1 is a nuclear protein that interacts with several transcription factors and other stress responsive proteins and has been shown to protect plants against oxidative damage and other stresses (Belles-Boix et al, 2000; Katiyar-Agarwal et al, 2006; Jaspers et al, 2009, 2010; Vainonen et al, 2012)
Five OsSRO genes were identified from the RGAP 7 database, distributed on chromosome X, III, VI and IV, and named as OsSRO1a_C Full length (OsSRO1a), OsSRO1b, OsSRO1c, OsSRO1d, and OsSRO1e, respectively (Figure 1A) with both OsSRO1b and OsSRO1c located on the chromosome III
Domain search analysis3 showed that all the OsSRO1 proteins contain an N-terminal WWE domain, a catalytic core, comprising poly (ADP-ribose) polymerase (PARP) domain and a C-terminal RST (RCD1-SIMILAR to RCD1 (SRO)-TAF4) domain
Summary
RCD1 is a nuclear protein that interacts with several transcription factors and other stress responsive proteins and has been shown to protect plants against oxidative damage and other stresses (Belles-Boix et al, 2000; Katiyar-Agarwal et al, 2006; Jaspers et al, 2009, 2010; Vainonen et al, 2012). The other RCD1 interacting partner includes a putative protein, similar to the members from the Ethylene Responsive Element Binding Protein (EREBP) subfamily of AP2/EREBP plant transcription factors. Members of this protein sub-family are involved in the induction of defense genes in response to biotic and abiotic stresses (Zhou et al, 1997; Fujimoto et al, 2000). Our results suggest that this interaction may have relevance in stress physiology
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