Rice OsHsp16.9A interacts with OsHsp101 to confer thermotolerance

Copyright © 2023 Elsevier B.V. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant science : an international journal of experimental plant biology. - 1985. - 330(2023) vom: 10. Mai, Seite 111634
1. Verfasser: Liu, Yi-Hsin (VerfasserIn)
Weitere Verfasser: Tseng, Tong-Seung, Wu, Ching-Rong, Cho, Shu-Ting, Kuo, Chih-Horng, Huang, Xin-Jie, Cheng, Jung-Yi, Hsu, Kuo-Hsuan, Lin, Kung-Fu, Liu, Chia-Chin, Yeh, Ching-Hui
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2023
Zugriff auf das übergeordnete Werk:Plant science : an international journal of experimental plant biology
Schlagworte:Journal Article Pull-down RBiFC Seed germination Small heat shock protein Thermoprotection Thermotolerance Plant Proteins Heat-Shock Proteins, Small Amino Acids
Beschreibung
Zusammenfassung:Copyright © 2023 Elsevier B.V. All rights reserved.
Class I small heat shock proteins (CI sHSPs), OsHsp16.9A and OsHsp18.0, share 74% identity in amino acid sequences and accumulate in response to heat shock treatments. Individual rice transformants overexpressing OsHsp16.9A and OsHsp18.0 exhibit distinct thermoprotection/thermotolerance modes. Under high temperature stress, OsHsp16.9A-overexpressing lines showed higher seed germination rate, seedling survival, and pollen germination than wild-type controls, while OsHsp18.0 overexpression provided higher thermoprotection/thermotolerance for seedling survival. To elucidate the functional roles of OsHsp16.9A, mass spectrometry was used to identify OsHsp16.9A-interacting proteins. OsHsp101 was consistently identified in the OsHsp16.9A protein complex in several mass spectrometry analyses of seed proteins from OsHsp16.9A-overexpressing lines. Both OsHsp16.9A and OsHsp101 proteins accumulated during similar developmental stages of rice seeds and formed a heat-stable complex under high temperature treatments in in vitro assays. Co-localization of OsHsp16.9A and OsHsp101 was observed via ratiometric bimolecular fluorescence complementation analyses. Amino acid mutation studies revealed that OsHsp16.9A glutamate residue 74 and amino acid residues 23-36 were essential for OsHsp16.9A-OsHsp101 interaction. Moreover, overexpressing OsHsp16.9A in OsHsp101 knockdown mutants did not increase the seed germination rate under heat stress, which further confirmed the functional roles of OsHsp16.9A-OsHsp101 interaction in conferring thermotolerance to rice plants
Beschreibung:Date Completed 31.03.2023
Date Revised 31.03.2023
published: Print-Electronic
Citation Status MEDLINE
ISSN:1873-2259
DOI:10.1016/j.plantsci.2023.111634