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231225s2018 xx |||||o 00| ||eng c |
| 024 |
7 |
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|a 10.1093/jxb/ery131
|2 doi
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|a pubmed24n1224.xml
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|a (DE-627)NLM283083662
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|a (NLM)29659986
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Sun, Qian
|e verfasserin
|4 aut
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| 245 |
1 |
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|a Brassica yellows virus P0 protein impairs the antiviral activity of NbRAF2 in Nicotiana benthamiana
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| 264 |
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|c 2018
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| 336 |
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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| 338 |
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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| 500 |
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|a Date Completed 15.10.2019
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| 500 |
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|a Date Revised 13.12.2023
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|a published: Print
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|a Citation Status MEDLINE
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| 520 |
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|a In interactions between poleroviruses and their hosts, few cellular proteins have been identified that directly interact with the multifunctional virus P0 protein. To help explore the functions of P0, we identified a Brassica yellows virus genotype A (BrYV-A) P0BrA-interacting protein from Nicotiana benthamiana, Rubisco assembly factor 2 (NbRAF2), which localizes in the nucleus, cell periphery, chloroplasts, and stromules. We found that its C-terminal domain (amino acids 183-211) is required for self-interaction. A split ubiquitin membrane-bound yeast two-hybrid system and co-immunoprecipitation assays showed that NbRAF2 interacted with P0BrA, and co-localized in the nucleus and at the cell periphery. Interestingly, the nuclear pool of NbRAF2 decreased in the presence of P0BrA and during BrYV-A infection, and the P0BrA-mediated reduction of nuclear NbRAF2 required dual localization of NbRAF2 in the chloroplasts and nucleus. Tobacco rattle virus-based virus-induced gene silencing of NbRAF2 promoted BrYV-A infection in N. benthamiana, and the overexpression of nuclear NbRAF2 inhibited BrYV-A accumulation. Potato leafroll virus P0PL also interacted with NbRAF2 and decreased its nuclear accumulation, indicating that NbRAF2 may be a common target of poleroviruses. These results suggest that nuclear NbRAF2 possesses antiviral activity against BrYV-A infection, and that BrYV-A P0BrA interacts with NbRAF2 and alters its localization pattern to facilitate virus infection
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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| 650 |
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7 |
|a Antiviral Agents
|2 NLM
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| 650 |
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7 |
|a Plant Proteins
|2 NLM
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| 650 |
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7 |
|a Viral Proteins
|2 NLM
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| 700 |
1 |
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|a Li, Yuan-Yuan
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Wang, Ying
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Zhao, Hang-Hai
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Zhao, Tian-Yu
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Zhang, Zong-Ying
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Li, Da-Wei
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Yu, Jia-Lin
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Wang, Xian-Bing
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Zhang, Yong-Liang
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Han, Cheng-Gui
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 69(2018), 12 vom: 25. Mai, Seite 3127-3139
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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| 773 |
1 |
8 |
|g volume:69
|g year:2018
|g number:12
|g day:25
|g month:05
|g pages:3127-3139
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| 856 |
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|u http://dx.doi.org/10.1093/jxb/ery131
|3 Volltext
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|d 69
|j 2018
|e 12
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|c 05
|h 3127-3139
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