Plastid-produced interorgannellar stress signal MEcPP potentiates induction of the unfolded protein response in endoplasmic reticulum

• DOI: 10.1073/pnas.1504828112
• Publication Date: 2015-04-29T02:31:51Z
• Authors: Justin Walley; Yanmei Xiao; Jin-Zheng Wang; Edward E. Baidoo; Jay D. Keasling; Zhouxin Shen; Steven P. Briggs; Katayoon Dehesh
• Keywords: retrograde signaling; Proteomics; 570; Protein Folding; Chloroplasts; Proteome; Arabidopsis; 610; Endoplasmic Reticulum; methylerythritol cyclodiphosphate; 03 medical and health sciences; Gene Expression Regulation, Plant; Genetics; Homeostasis; Plastids; Plant Proteins; 0303 health sciences; Gene Expression Profiling; Plant; interorgannellar communication; unfolded protein response; Biological Sciences; Endoplasmic Reticulum Stress; Microarray Analysis; methylerythritol cyclodiphosphate 3; endoplasmic reticulum; Erythritol; Gene Expression Regulation; Unfolded Protein Response; Biochemistry and Cell Biology; Transcriptome; Signal Transduction

Cellular homeostasis in response to internal and external stimuli requires a tightly coordinated interorgannellar communication network. We recently identified methylerythritol cyclodiphosphate (MEcPP) as novel stress-specific retrograde signaling metabolite that accumulates environmental perturbations relay information from plastids the nucleus. now demonstrate, using combination of transcriptome proteome profiling approaches, mutant plants (ceh1) with high endogenous levels MEcPP display increased transcript protein for subset core unfolded (UPR) genes. The UPR is an adaptive cellular conserved throughout eukaryotes stress conditions perturb endoplasmic reticulum (ER) homeostasis. Our results suggest directly triggers UPR. Exogenous treatment induces rapid transient induction both unspliced spliced forms gene bZIP60. Moreover, compared parent background (P), ceh1 mutants are less sensitive ER-stress-inducing agent tunicamycin (Tm). P treated Tm similar profiles, suggesting although accumulation causes partial selected genes, full triggered by misfolded proteins. This finding refines our perspective providing link between plastidial molecule its targeted ensemble components ER.