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231225s2021 xx |||||o 00| ||eng c |
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|a 10.1111/nph.17438
|2 doi
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|a eng
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|a Zhao, Hong
|e verfasserin
|4 aut
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|a Primary restriction of S-RNase cytotoxicity by a stepwise ubiquitination and degradation pathway in Petunia hybrida
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|c 2021
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|2 rdamedia
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|a ƒa Online-Ressource
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|a Date Completed 12.07.2021
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|a Date Revised 18.08.2021
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a © 2021 The Authors. New Phytologist © 2021 New Phytologist Foundation.
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|a In self-incompatible Petunia species, the pistil S-RNase acts as cytotoxin to inhibit self-pollination but is polyubiquitinated by the pollen-specific nonself S-locus F-box (SLF) proteins and subsequently degraded by the ubiquitin-proteasome system (UPS), allowing cross-pollination. However, it remains unclear how S-RNase is restricted by the UPS. Using biochemical analyses, we first show that Petunia hybrida S3 -RNase is largely ubiquitinated by K48-linked polyubiquitin chains at three regions, R I, R II and R III. R I is ubiquitinated in unpollinated, self-pollinated and cross-pollinated pistils, indicating its occurrence before PhS3 -RNase uptake into pollen tubes, whereas R II and R III are exclusively ubiquitinated in cross-pollinated pistils. Transgenic analyses showed that removal of R II ubiquitination resulted in significantly reduced seed sets from cross-pollination and that of R I and R III to a lesser extent, indicating their increased cytotoxicity. Consistent with this, the mutated R II of PhS3 -RNase resulted in a marked reduction of its degradation, whereas that of R I and R III resulted in less reduction. Taken together, we demonstrate that PhS3 -RNase R II functions as a major ubiquitination region for its destruction and R I and R III as minor ones, revealing that its cytotoxicity is primarily restricted by a stepwise UPS mechanism for cross-pollination in P. hybrida
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Petunia hybrida
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|a S-RNase
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|a SLF
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|a self-incompatibility
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|a ubiquitination
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|a Plant Proteins
|2 NLM
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|a Ribonucleases
|2 NLM
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|a EC 3.1.-
|2 NLM
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| 700 |
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|a Song, Yanzhai
|e verfasserin
|4 aut
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| 700 |
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|a Li, Junhui
|e verfasserin
|4 aut
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| 700 |
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|a Zhang, Yue
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Huang, Huaqiu
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Li, Qun
|e verfasserin
|4 aut
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|a Zhang, Yu'e
|e verfasserin
|4 aut
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|a Xue, Yongbiao
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t The New phytologist
|d 1984
|g 231(2021), 3 vom: 26. Aug., Seite 1249-1264
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|x 1469-8137
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|g year:2021
|g number:3
|g day:26
|g month:08
|g pages:1249-1264
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|u http://dx.doi.org/10.1111/nph.17438
|3 Volltext
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