Signal transduction by IRE1-mediated splicing ofbZIP50and other stress sensors in the endoplasmic reticulum stress response of rice

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Abstract

The endoplasmic reticulum (ER) stress sensor IRE1 transduces signals by inducing the unconventional splicing of mRNAs encoding key transcription factors: HAC1 in yeast and XBP1 in animals. However, no HAC1 or XBP1 homologues have been found in plants, and until recently the substrate for plant IRE1 has remained unknown. This study demonstrates that theOryza sativa(rice) OsbZIP50 transcription factor, an orthologue of Arabidopsis AtbZIP60, is regulated by IRE1-mediated splicing of its RNA. Despite the presence of a transcriptional activation domain, OsbZIP50 protein is not translocated into the nucleus efficiently in the absence ofOsbZIP50mRNA splicing. Unconventional splicing ofOsbZIP50mRNA causes a frame shift, which results in the appearance of a nuclear localization signal in the newly translated OsbZIP50.OsbZIP50mRNA is spliced in a similar manner toHAC1andXBP1mRNAs; however, this splicing has very different effects on the translation products, a finding that shows the diversity of IRE1-related transcription factors in eukaryotes. In addition, the expression of OsbZIP50 is affected by ER stress sensor proteins OsIRE1, OsbZIP39 and OsbZIP60. ER stress-related genes differ with respect to their dependency on OsbZIP50 for their expression. The findings of this study improve our understanding of the molecular mechanisms underlying the plant ER stress response.

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