Abstract
Roots are the frontier of plant body to perceive underground environmental change. Endoplasmic reticulum (ER) stress response represents circumvention of cellular stress caused by various environmental changes; however, a limited number of studies are available on the ER stress responses in roots. Here, we report the tunicamycin (TM) -induced ER stress response in Arabidopsis roots by monitoring expression patterns of immunoglobulin-binding protein 3 (BiP3), a representative marker for the response. Roots promptly responded to the TM-induced ER stress through the induction of similar sets of ER stress-responsive genes. However, not all cells responded uniformly to the TM-induced ER stress in roots, as BiP3 was highly expressed in root tips, an outer layer in elongation zone, and an inner layer in mature zone of roots. We suggest that ER stress response in roots has tissue specificity.
Highlights
Roots are the frontier of plant body to perceive underground environmental change
binding protein 3 (BiP3) is a widely used marker gene for the Endoplasmic reticulum (ER) stress response, whose expression is extremely low at either RNA or protein levels under nonstress conditions but is highly up-regulated upon the ER stress in Arabidopsis young seedlings (Noh et al, 2003; Cho et al, 2015)
This observation suggests that roots respond to TM treatment more rapidly than leaves, and that the vasculatures and root tips are the initial sites of TM-induced ER stress response in Arabidopsis roots
Summary
Roots are the frontier of plant body to perceive underground environmental change. In response to environmental stimuli, a crucial set of molecular processes is induced that maintains cellular homeostasis and circumvents fatal defects caused by the stresses. The ER quality control is wellconserved molecular mechanisms among eukaryotic cells including animals, yeasts and plants (Iwata and Koizumi, 2005, 2012; Howell, 2013). When aberrant proteins are accumulated in the ER, the ER quality control recognizes these aberrant proteins and responds to maintain the ER homeostasis using multiple strategies such as UPR and ER-associated degradation (ERAD) (Kanehara et al, 2007; Walter and Ron, 2011; Ruggiano et al, 2014). The IRE1 senses protein-folding status in the ER and transmits signals into the nuclei by catalyzing unconventional cytoplasmic splicing of bZIP60 mRNA in plants (XBP1 in mammals and HAC1 in yeasts) followed by activation of UPR target genes including a molecular chaperone BiP (Nagashima et al, 2011; Walter and Ron, 2011). BiP is one of the most abundant chaperones in the ER lumen and is thought to bind nascent
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