Orchardgrass ACTIVATOR OF HSP90 ATPASE possesses autonomous chaperone properties and activates Hsp90 transcription to enhance thermotoleranceopen access
- Lee, Changhoon; Youn, Ho Jin; Lee, Sang-Hoon; Kim, Jinwoo; Son, Daeyoung; Cha, Joon-Yung
- Issue Date
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Aha; Co-chaperone; Hsp90; Molecular chaperone; Thermotolerance
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.586, pp.171 - 176
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Start Page
- End Page
- High temperature stress is an environmental factor that negatively affects the growth and development of crops. Hsp90 (90 kDa heat shock protein) is a major molecular chaperone in eukaryotic cells, contributing to the maintenance of cell homeostasis through interaction with co-chaperones. Aha1 (activator of Hsp90 ATPase) is well known as a co-chaperone that activates ATPase activity of Hsp90 in mammals. However, biochemical and physiological evidence relating to Aha has not yet been identified in plants. In this study, we investigated the heat-tolerance function of orchardgrass (Dactylis glomerata L.) Aha (DgAha). Recombinant DgAha interacted with cytosolic DgHsp90s and efficiently protected substrates from thermal denaturation. Furthermore, heterologous expression of DgAha in yeast (Saccharo-myces cerevisiae) cells and Arabidopsis (Arabidopsis thaliana) plants conferred thermotolerance in vivo. Enhanced expression of DgAha in Arabidopsis stimulates the transcription of Hsp90 under heat stress. Our data demonstrate that plant Aha plays a positive role in heat stress tolerance via chaperone properties and/or activation of Hsp90 to protect substrate proteins in plants from thermal injury. (c) 2021 Elsevier Inc. All rights reserved.
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- 농업생명과학대학 > 식물의학과 > Journal Articles
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