Ca2+-dependent protein kinases and their substrate HsfB2a are differently involved in the heat response signaling pathway in Arabidopsis

DOI Web Site 参考文献39件
  • Kanchiswamy Chidananda Nagamangala
    Global COE Program: Evolution and Biodiversity, Graduate School of Science, Kyoto University Center for Ecological Research, Kyoto University Plant Physiology Unit, Department of Plant Biology and Innovation Centre, University of Turin
  • Muroi Atsushi
    Global COE Program: Evolution and Biodiversity, Graduate School of Science, Kyoto University Center for Ecological Research, Kyoto University
  • Maffei Massimo E.
    Plant Physiology Unit, Department of Plant Biology and Innovation Centre, University of Turin
  • Yoshioka Hirofumi
    Graduate School of Bioagricultural Sciences, Nagoya University
  • Sawasaki Tatsuya
    Cell-free Science and Technology Research Center, Ehime University
  • Arimura Gen-ichiro
    Global COE Program: Evolution and Biodiversity, Graduate School of Science, Kyoto University Center for Ecological Research, Kyoto University

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Little is known about the mechanisms by which Ca2+-binding sensory proteins direct the plant heat shock (HS) response. Since two Ca2+-dependent protein kinases (CPK3 and CPK13) were recently shown to phosphorylate the heat shock transcription factor HsfB2a, we assessed in the current study whether these kinases are also involved in HS signal transduction, by monitoring the transcriptional profile of HS protein (Hsp) family genes in Arabidopsis Col-0 plants (WT) and the corresponding mutants. Both with and without HS, the gene transcript levels of Hsp70, Hsp101, Hsp17.4-CIII and Hsp15.7-CI were found to be lower in cpk3 and cpk13 mutants compared to WT, resulting in the impairment of basal thermotolerance in the mutants. To determine the in vivo function of CPKs, CPK3/13 and their substrate HsfB2a (heat shock transcription factor) were co-expressed as cofactors for the transient expression of a reporter (GUS) gene under the control of heat shock element (HSE) in Nicotiana benthamiana leaves. However, CPK3/13-phosphorylated HsfB2a did not function in the suppression/activation of HSE-promoted expression in the transient expression system. Implications for possible signal trafficking via CPKs and Hsfs are discussed.

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