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231225s2021 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/eraa489
|2 doi
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|a pubmed24n1055.xml
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|a (DE-627)NLM316641278
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|a (NLM)33095257
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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 Karki, Sujit Jung
|e verfasserin
|4 aut
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| 245 |
1 |
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|a A small secreted protein from Zymoseptoria tritici interacts with a wheat E3 ubiquitin ligase to promote disease
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|c 2021
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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 13.05.2021
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|a Date Revised 13.05.2021
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|a published: Print
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|a Dryad: 10.5061/dryad.9w0vt4bcx
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|a Citation Status MEDLINE
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| 520 |
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|a © The Author(s) 2020. Published by Oxford University Press on behalf of the Society for Experimental Biology.
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|a Septoria tritici blotch (STB), caused by the ascomycete fungus Zymoseptoria tritici, is a major threat to wheat production worldwide. The Z. tritici genome encodes many small secreted proteins (ZtSSPs) that are likely to play a key role in the successful colonization of host tissues. However, few of these ZtSSPs have been functionally characterized for their role during infection. In this study, we identified and characterized a small, conserved cysteine-rich secreted effector from Z. tritici which has homologues in other plant pathogens in the Dothideomycetes. ZtSSP2 was expressed throughout Z. tritici infection in wheat, with the highest levels observed early during infection. A yeast two-hybrid assay revealed an interaction between ZtSSP2 and wheat E3 ubiquitin ligase (TaE3UBQ) in yeast, and this was further confirmed in planta using bimolecular fluorescence complementation and co-immunoprecipitation. Down-regulation of this wheat E3 ligase using virus-induced gene silencing increased the susceptibility of wheat to STB. Together, these results suggest that TaE3UBQ is likely to play a role in plant immunity to defend against Z. tritici
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4 |
|a Journal Article
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| 650 |
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4 |
|a Research Support, Non-U.S. Gov't
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| 650 |
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4 |
|a Zymoseptoria tritici
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| 650 |
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4 |
|a Disease
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| 650 |
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|a E3 ubiquitin ligase
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| 650 |
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4 |
|a effector
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| 650 |
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4 |
|a fungal pathogen
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| 650 |
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4 |
|a wheat
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| 650 |
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7 |
|a Ubiquitin-Protein Ligases
|2 NLM
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| 650 |
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7 |
|a EC 2.3.2.27
|2 NLM
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| 700 |
1 |
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|a Reilly, Aisling
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Zhou, Binbin
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Mascarello, Maurizio
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Burke, James
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Doohan, Fiona
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Douchkov, Dimitar
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Schweizer, Patrick
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Feechan, Angela
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 72(2021), 2 vom: 02. Feb., Seite 733-746
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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| 773 |
1 |
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|g volume:72
|g year:2021
|g number:2
|g day:02
|g month:02
|g pages:733-746
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| 856 |
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|u http://dx.doi.org/10.1093/jxb/eraa489
|3 Volltext
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|a AR
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|d 72
|j 2021
|e 2
|b 02
|c 02
|h 733-746
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