GmHsp90A2 is involved in soybean heat stress as a positive regulator

Copyright © 2019 Elsevier B.V. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant science : an international journal of experimental plant biology. - 1985. - 285(2019) vom: 15. Aug., Seite 26-33
1. Verfasser: Huang, Yanzhong (VerfasserIn)
Weitere Verfasser: Xuan, Huidong, Yang, Chengfeng, Guo, Na, Wang, Haitang, Zhao, Jinming, Xing, Han
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2019
Zugriff auf das übergeordnete Werk:Plant science : an international journal of experimental plant biology
Schlagworte:Journal Article GmHsp90A2 Heat stress Protein interactions Soybean [Glycine max (L.) Merr.] Heat-Shock Proteins Plant Proteins Chlorophyll 1406-65-1 Malondialdehyde mehr... 4Y8F71G49Q CRISPR-Associated Protein 9 EC 3.1.-
Beschreibung
Zusammenfassung:Copyright © 2019 Elsevier B.V. All rights reserved.
Heat shock protein 90 s (Hsp90s), one of the most conserved and abundant molecular chaperones, is an essential component of the protective stress response. A previous study reported at least 12 genes in the GmHsp90s family in soybean and that GmHsp90A2 overexpression enhanced thermotolerance in Arabidopsis thaliana. Here, we investigate the roles of GmHsp90A2 in soybean by utilizing stable transgenic soybean lines overexpressing GmHsp90A2 and mutant lines generated by the CRISPR/Cas9 system. The results showed that compared with wild-type plants (WT) and empty vector control plants (VC), T3 transgenic soybean plants overexpressing GmHsp90A2 exhibited increased tolerance to heat stress through higher chlorophyll and lower malondialdehyde (MDA) contents in plants. Conversely, reduced chlorophyll and increased MDA contents in T2 homozygous GmHsp90A2-knockout mutants indicated decreased tolerance to heat stress. GmHsp90A2 was found to interact with GmHsp90A1 in yeast two-hybrid assays. Furthermore, subcellular localization analyses revealed that GmHsp90A2 was localized to the cytoplasm and cell membrane; as shown by bimolecular fluorescence complementation (BiFC) assays, GmHsp90A2 interacted with GmHsp90A1 in the nucleus and cytoplasm and cell membrane. Hence, we conclude that GmHsp90A1 is able to bind to GmHsp90A2 to form a complex and that this complex enters the nucleus. In summary, GmHsp90A2 might respond to heat stress and positively regulate thermotolerance by interacting with GmHsp90A1
Beschreibung:Date Completed 13.08.2019
Date Revised 13.12.2023
published: Print-Electronic
Citation Status MEDLINE
ISSN:1873-2259
DOI:10.1016/j.plantsci.2019.04.016