![]() ![]() (groups A–I and S, and one unnamed group) based on similarities in amino acid sequences and features, and VIP1 belongs to VIP1 is a bZIP transcription factors in Arabidopsis thaliana.Īrabidopsis bZIP proteins have been classified into 11 groups Keywords: Arabidopsis thaliana, bZIP transcription factor, calcium signalling, mechanical stress, nuclearcytoplasmic shuttling, root bending, root touch responses. Their nuclear–cytoplasmic shuttling requires neither MCA1 nor MCA2, but does require calcium signalling. Conclusions VIP1 and its close homologues can interact with calmodulins.Nuclear–cytoplasmic shuttling of VIP1 was observed even in the mca1 mca2 mutant. Either 40 mm CaCl2or 80 mm NaCl enhanced the VIP-SRDX-dependent root bending. ![]() EDTA,ĮGTA and chlorpromazine all inhibited both the nuclear import and the nuclear export of VIP1-GFP, bZIP59-GFPĪnd bZIP29-GFP. Key Results In vitro crosslink products were detected in the presence of CaCl2, but not in its absence.MCA1 and MCA2 are mechanosensitive calciumĬhannels, and the hypo-osmotic stress-dependent nuclear–cytoplasmic shuttling of VIP1-GFP in the mca1 mca2ĭouble knockout mutant background was examined. Medium containing 40 mm CaCl2, 40 mm MgCl2 or 80 mm NaCl. GFP-fused forms of VIP1 and its close homologues (bZIP59 and bZIP29) were submerged in hypotonic solutionsĬontaining divalent cation chelators, EDTA and EGTA, and a potential calmodulin inhibitor, chlorpromazine, toĮxamine their effects on the nuclear–cytoplasmic shuttling of those proteins. In vitro crosslink analysis was performed using a hexahistidinetagged calmodulin and glutathione S-transferase-fused forms of VIP1 and its close homologues. Identified calmodulins as VIP1-GFP interactors. Methods Co-immunoprecipitation analysis using VIP1-GFP fusion protein expressed in Arabidopsis plants.The aim of this study was to identify regulators of these functions of VIP1 in mechanical stress responses. VIP1 (VIP1-SRDXox), suggesting that VIP1, possibly with its close homologues, suppresses touch-induced rootīending. Touch-induced root bending is enhanced in transgenic plants overexpressing a repression domain-fused form of VIP1 and its close homologues transiently accumulate in the nucleus when cells are exposed to hypo-osmotic and/or mechanical stress. Background and Aims VIP1 is a bZIP transcription factor in Arabidopsis thaliana.E-mail: 28 April 2018Įditorial decision: 5 June 2018 Accepted: 12 June 2018 Zhejiang A & F University, Lin’an, Hangzhou 311300, PR China Sapporo-shi, Hokkaido 060-8589, Japan, 2Asian Natural Environmental Science Center, The University of Tokyo,ġ-1-1 Midori-cho, Nishitokyo-shi, Tokyo 188-0002, Japan and 3State Key Laboratory of Subtropical Silviculture, Laboratory of Crop Physiology, Research Faculty of Agriculture, Hokkaido University, Kita 9 Nishi 9 Kita-ku, Doi: 10.1093/aob/mcy125, available online at Calcium signalling regulates the functions of the bZIP protein VIP1 in touchĭaisuke Tsugama1,2*, Shenkui Liu3, Kaien Fujino1 and Tetsuo Takano2 ![]()
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