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231226s2023 xx |||||o 00| ||eng c |
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|a 10.1016/j.plantsci.2023.111634
|2 doi
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|a pubmed24n1176.xml
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|a (DE-627)NLM352846623
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|a (NLM)36775071
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|a (PII)S0168-9452(23)00051-1
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
1 |
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|a Liu, Yi-Hsin
|e verfasserin
|4 aut
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| 245 |
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|a Rice OsHsp16.9A interacts with OsHsp101 to confer thermotolerance
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|c 2023
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 31.03.2023
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|a Date Revised 31.03.2023
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2023 Elsevier B.V. All rights reserved.
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|a 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
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|a Journal Article
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|a Pull-down
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|a RBiFC
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|a Seed germination
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|a Small heat shock protein
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|a Thermoprotection
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|a Thermotolerance
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|a Plant Proteins
|2 NLM
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| 650 |
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|a Heat-Shock Proteins, Small
|2 NLM
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| 650 |
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|a Amino Acids
|2 NLM
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| 700 |
1 |
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|a Tseng, Tong-Seung
|e verfasserin
|4 aut
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| 700 |
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|a Wu, Ching-Rong
|e verfasserin
|4 aut
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| 700 |
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|a Cho, Shu-Ting
|e verfasserin
|4 aut
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| 700 |
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|a Kuo, Chih-Horng
|e verfasserin
|4 aut
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| 700 |
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|a Huang, Xin-Jie
|e verfasserin
|4 aut
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| 700 |
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|a Cheng, Jung-Yi
|e verfasserin
|4 aut
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| 700 |
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|a Hsu, Kuo-Hsuan
|e verfasserin
|4 aut
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| 700 |
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|a Lin, Kung-Fu
|e verfasserin
|4 aut
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| 700 |
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|a Liu, Chia-Chin
|e verfasserin
|4 aut
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| 700 |
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|a Yeh, Ching-Hui
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Plant science : an international journal of experimental plant biology
|d 1985
|g 330(2023) vom: 10. Mai, Seite 111634
|w (DE-627)NLM098174193
|x 1873-2259
|7 nnns
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| 773 |
1 |
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|g volume:330
|g year:2023
|g day:10
|g month:05
|g pages:111634
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| 856 |
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|u http://dx.doi.org/10.1016/j.plantsci.2023.111634
|3 Volltext
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|d 330
|j 2023
|b 10
|c 05
|h 111634
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