Comparative study of Arabidopsis PBS1 and a wheat PBS1 homolog helps understand the mechanism of PBS1 functioning in innate immunity

Abstract Arabidopsis AVRPPHB SUSCEPTIBLE1 (PBS1) serves as a “decoy” in activating RESISTANCE TO PSEUDOMONAS SYRINGAE5 (RPS5) upon cleavage by Pseudomonas phaseolicola B (AvrPphB), a Pseudomonas syringae effector. The SEMPH motif in PBS1 was thought to allow it to be distinguished by RPS5 from the c...

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Autores principales:	Jianhang Sun, Guozhong Huang, Fenggui Fan, Shuangfeng Wang, Yingying Zhang, Yufang Han, Yanmin Zou, Dongping Lu
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/1bab542ad14d4e879b354d3fd8375cfd
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spelling	oai:doaj.org-article:1bab542ad14d4e879b354d3fd8375cfd2021-12-02T15:04:55ZComparative study of Arabidopsis PBS1 and a wheat PBS1 homolog helps understand the mechanism of PBS1 functioning in innate immunity10.1038/s41598-017-05904-x2045-2322https://doaj.org/article/1bab542ad14d4e879b354d3fd8375cfd2017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-05904-xhttps://doaj.org/toc/2045-2322Abstract Arabidopsis AVRPPHB SUSCEPTIBLE1 (PBS1) serves as a “decoy” in activating RESISTANCE TO PSEUDOMONAS SYRINGAE5 (RPS5) upon cleavage by Pseudomonas phaseolicola B (AvrPphB), a Pseudomonas syringae effector. The SEMPH motif in PBS1 was thought to allow it to be distinguished by RPS5 from the closely related Arabidopsis kinases. However, the underlying mechanism is not fully understood. Here, we isolated and characterized a wheat PBS1 homolog, TaPBS1. Although this plasma membrane-localized kinase could be cleaved by AvrPphB and could associate with RPS5, it failed to trigger RPS5-mediated hypersensitive response (HR) in a transient assay. TaPBS1 harbors a STRPH motif. The association of RPS5 with TaPBS1 was weaker than with PBS1. Change of the STRPH motif to the SEMPH motif allowed TaPBS1 to trigger HR. However, the SEMPH motif is not required for association of PBS1 with RPS5. The difference between “SEMPH” and “STRPH” points to the importance of “EM” in PBS1. Furthermore we found that a negatively charged amino acid at the position of “E” in the SEMPH motif was required for recognition of PBS1 by RPS5. Additionally, both PBS1 and TaPBS1 undergo the flagellin-induced phosphorylation. Therefore, our work will help understand the mechanism of PBS1 functioning in plant innate immunity.Jianhang SunGuozhong HuangFenggui FanShuangfeng WangYingying ZhangYufang HanYanmin ZouDongping LuNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-12 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Jianhang Sun Guozhong Huang Fenggui Fan Shuangfeng Wang Yingying Zhang Yufang Han Yanmin Zou Dongping Lu Comparative study of Arabidopsis PBS1 and a wheat PBS1 homolog helps understand the mechanism of PBS1 functioning in innate immunity
description	Abstract Arabidopsis AVRPPHB SUSCEPTIBLE1 (PBS1) serves as a “decoy” in activating RESISTANCE TO PSEUDOMONAS SYRINGAE5 (RPS5) upon cleavage by Pseudomonas phaseolicola B (AvrPphB), a Pseudomonas syringae effector. The SEMPH motif in PBS1 was thought to allow it to be distinguished by RPS5 from the closely related Arabidopsis kinases. However, the underlying mechanism is not fully understood. Here, we isolated and characterized a wheat PBS1 homolog, TaPBS1. Although this plasma membrane-localized kinase could be cleaved by AvrPphB and could associate with RPS5, it failed to trigger RPS5-mediated hypersensitive response (HR) in a transient assay. TaPBS1 harbors a STRPH motif. The association of RPS5 with TaPBS1 was weaker than with PBS1. Change of the STRPH motif to the SEMPH motif allowed TaPBS1 to trigger HR. However, the SEMPH motif is not required for association of PBS1 with RPS5. The difference between “SEMPH” and “STRPH” points to the importance of “EM” in PBS1. Furthermore we found that a negatively charged amino acid at the position of “E” in the SEMPH motif was required for recognition of PBS1 by RPS5. Additionally, both PBS1 and TaPBS1 undergo the flagellin-induced phosphorylation. Therefore, our work will help understand the mechanism of PBS1 functioning in plant innate immunity.
format	article
author	Jianhang Sun Guozhong Huang Fenggui Fan Shuangfeng Wang Yingying Zhang Yufang Han Yanmin Zou Dongping Lu
author_facet	Jianhang Sun Guozhong Huang Fenggui Fan Shuangfeng Wang Yingying Zhang Yufang Han Yanmin Zou Dongping Lu
author_sort	Jianhang Sun
title	Comparative study of Arabidopsis PBS1 and a wheat PBS1 homolog helps understand the mechanism of PBS1 functioning in innate immunity
title_short	Comparative study of Arabidopsis PBS1 and a wheat PBS1 homolog helps understand the mechanism of PBS1 functioning in innate immunity
title_full	Comparative study of Arabidopsis PBS1 and a wheat PBS1 homolog helps understand the mechanism of PBS1 functioning in innate immunity
title_fullStr	Comparative study of Arabidopsis PBS1 and a wheat PBS1 homolog helps understand the mechanism of PBS1 functioning in innate immunity
title_full_unstemmed	Comparative study of Arabidopsis PBS1 and a wheat PBS1 homolog helps understand the mechanism of PBS1 functioning in innate immunity
title_sort	comparative study of arabidopsis pbs1 and a wheat pbs1 homolog helps understand the mechanism of pbs1 functioning in innate immunity
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/1bab542ad14d4e879b354d3fd8375cfd
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Comparative study of Arabidopsis PBS1 and a wheat PBS1 homolog helps understand the mechanism of PBS1 functioning in innate immunity

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