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240918s2024 xx |||||o 00| ||eng c |
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|a 10.1111/nph.20142
|2 doi
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|a pubmed25n1258.xml
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|a (DE-627)NLM377770426
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|a (NLM)39290056
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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 Chang, Jiaying
|e verfasserin
|4 aut
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| 245 |
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|a A thaumatin-like effector protein suppresses the rust resistance of wheat and promotes the pathogenicity of Puccinia triticina by targeting TaRCA
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|c 2024
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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 07.11.2024
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|a Date Revised 08.11.2024
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a © 2024 The Author(s). New Phytologist © 2024 New Phytologist Foundation.
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|a Thaumatin-like proteins (TLPs) in plants play a crucial role in combating stress, and they have been proven to possess antifungal properties. However, the role of TLPs in pathogens has not been reported. We identified a effector protein, Pt9029, which contained a Thaumatin domain in Puccinia triticina (Pt), possessing a chloroplast transit peptide and localized in the chloroplasts. Silencing Pt9029 in the Pt physiological race THTT resulted in a notable reduction in virulence and stunted growth and development of Pt hypha in near-isogenic wheat line TcLr2b. Overexpression of Pt9029 in wheat exerted a suppressive effect on H2O2 production, consequently impeding the wheat's disease resistance mechanisms. The TLP domain of Pt9029 targets the Rubisco activase (TaRCA) in chloroplasts. This interaction effectively inhibited the function of TaRCA, subsequently leading to a decrease in Rubisco enzyme activity. Therefore, this indicates that TLPs in Pt can inhibit host defense mechanisms during the pathogenic process of Pt. Moreover, TaRCA silencing resulted in reduced resistance of TcLr2b against Pt race THTT. This clearly demonstrated that TaRCA positively regulates wheat resistance to leaf rust. These findings reveal a novel strategy exploited by Pt to manipulate wheat rust resistance and promote pathogenicity
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|a Journal Article
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|a Puccinia triticina
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|a Rubisco activase
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|a Thaumatin‐like proteins
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|a chloroplast function
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|a disease resistance
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|a effector proteins
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|a Plant Proteins
|2 NLM
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|a thaumatin protein, plant
|2 NLM
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| 650 |
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|a 53850-34-3
|2 NLM
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| 650 |
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|a Ribulose-Bisphosphate Carboxylase
|2 NLM
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| 650 |
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|a EC 4.1.1.39
|2 NLM
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| 650 |
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|a Hydrogen Peroxide
|2 NLM
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| 650 |
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|a BBX060AN9V
|2 NLM
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| 700 |
1 |
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|a Mapuranga, Johannes
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Wang, Xiaodong
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Dong, Haijiao
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Li, Ruolin
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Zhang, Yingdan
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Li, Hao
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Shi, Jie
|e verfasserin
|4 aut
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| 700 |
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|a Yang, Wenxiang
|e verfasserin
|4 aut
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| 773 |
0 |
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|i Enthalten in
|t The New phytologist
|d 1979
|g 244(2024), 5 vom: 17. Dez., Seite 1947-1960
|w (DE-627)NLM09818248X
|x 1469-8137
|7 nnas
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| 773 |
1 |
8 |
|g volume:244
|g year:2024
|g number:5
|g day:17
|g month:12
|g pages:1947-1960
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| 856 |
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|u http://dx.doi.org/10.1111/nph.20142
|3 Volltext
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|d 244
|j 2024
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|c 12
|h 1947-1960
|