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Proteomic and molecular analyses to understand the promotive effect of safranal on soybean growth under salt stress.
Kausar, Rehana; Nishiuchi, Takumi; Komatsu, Setsuko.
Afiliación
  • Kausar R; Department of Botany, University of Azad Jammu and Kashmir, Muzaffarabad 13100, Pakistan.
  • Nishiuchi T; Research Center for Experimental Modeling of Human Disease, Kanazawa University, Kanazawa 920-8640, Japan.
  • Komatsu S; Faculty of Environment and Information Sciences, Fukui University of Technology, Fukui 910-8505, Japan. Electronic address: skomatsu@fukui-ut.ac.jp.
J Proteomics ; 294: 105072, 2024 03 15.
Article en En | MEDLINE | ID: mdl-38218428
ABSTRACT
Safranal is a free radical scavenger and useful as an antioxidant molecule; however, its promotive role in soybean is not explored. Salt stress decreased soybean growth and safranal improved it even if under salt stress. To study the positive mechanism of safranal on soybean growth, a proteomic approach was used. According to functional categorization, oppositely changed proteins were further confirmed using biochemical techniques. Actin and calcium-dependent protein kinase decreased in soybean root and hypocotyl, respectively, under salt stress and increased with safranal application. Xyloglucan endotransglucosylase/ hydrolase increased in soybean root under salt stress but decreased with safranal application. Peroxidase increased under salt stress and further enhanced by safranal application in soybean root. Actin, RuvB-like helicase, and protein kinase domain-containing protein were upregulated under salt stress and further enhanced by safranal application under salt stress. Dynamin GTPase was downregulated under salt stress but recovered with safranal application under salt stress. Glutathione peroxidase and PfkB domain-containing protein were upregulated by safranal application under salt stress in soybean root. These results suggest that safranal improves soybean growth through the regulation of cell wall and nuclear proteins along with reactive­oxygen species scavenging system. Furthermore, it might promote salt-stress tolerance through the regulation of membrane proteins involved in endocytosis and post-Golgi trafficking.

SIGNIFICANCE:

To study the positive mechanism of safranal on soybean growth, a proteomic approach was used. According to functional categorization, oppositely changed proteins were further confirmed using biochemical techniques. Actin and calcium-dependent protein kinase decreased in soybean root and hypocotyl, respectively, under salt stress and increased with safranal application. Xyloglucan endotransglucosylase/ hydrolase increased in soybean root under salt stress but decreased with safranal application. Peroxidase increased under salt stress and further enhanced by safranal application in soybean root. Actin, RuvB-like helicase, and protein kinase domain-containing protein were upregulated under salt stress and further enhanced by safranal application under salt stress. Dynamin GTPase was downregulated under salt stress but recovered with safranal application under salt stress. Glutathione peroxidase and PfkB domain-containing protein were upregulated by safranal application under salt stress in soybean root. These results suggest that safranal improves soybean growth through the regulation of cell wall and nuclear proteins along with reactive­oxygen species scavenging system. Furthermore, it might promote salt-stress tolerance through the regulation of membrane proteins involved in endocytosis and post-Golgi trafficking.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Glycine max / Terpenos / Proteómica / Ciclohexenos Idioma: En Revista: J Proteomics Asunto de la revista: BIOQUIMICA Año: 2024 Tipo del documento: Article País de afiliación: Pakistán

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Glycine max / Terpenos / Proteómica / Ciclohexenos Idioma: En Revista: J Proteomics Asunto de la revista: BIOQUIMICA Año: 2024 Tipo del documento: Article País de afiliación: Pakistán