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ER stress-induced protein, VIGG, disturbs plant cation homeostasis, which is correlated with growth retardation and robustness to ER stress
Authors:Katoh Hironori  Fujita Keiko  Takuhara Yuki  Ogawa Atsushi  Suzuki Shunji
Affiliation:aLaboratory of Fruit Genetic Engineering, The Institute of Enology and Viticulture, University of Yamanashi, Kofu, Yamanashi 400-0005, Japan;bDepartment of Biological Production, Akita Prefectural University, Shimosinjyou-nakano 241-438, Akita 010-0195, Japan
Abstract:VIGG is a putative endoplasmic reticulum (ER) resident protein induced by virus infection and ER stress, and is correlated with fruit quality in grapevine. The present study was undertaken to determine the biological function of VIGG in grapevine. Experiments using fluorescent protein-VIGG fusion protein demonstrated that VIGG is localized in ER and the ER targeting sequence is in the N-terminus. The overexpression of VIGG in Arabidopsis plant led to growth retardation. The rosette leaves of VIGG-overexpressing plants were smaller than those of the control plants and rolled at 42 days after seeding. VIGG-overexpressing plants revealed robustness to ER stress as well as the low expression of ER stress marker proteins, such as the luminal binding proteins. These characteristics of VIGG-overexpressing plants were supported by a microarray experiment that demonstrated the disruption of genes related to ER stress response and flowering, as well as cation mobility, in the plants. Finally, cation homeostasis in the plants was disturbed by the overexpression of VIGG. Taken together, these results suggest that VIGG may disturb cation homeostasis in plant, which is correlated with the robustness to ER stress and growth retardation.
Keywords:Abbreviations: BiP, luminal binding protein   CAX, cation exchanger   CRT, calreticulin   ECA, endoplasmic reticulum Ca2+-ATPase   ER, endoplasmic reticulum   VIGG, virus-induced grapevine protein
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