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Site-specific cleavage of bacterial MucD by secreted proteases mediates antibacterial resistance in Arabidopsis

Plant innate immunity restricts growth of bacterial pathogens that threaten global food security. However, the mechanisms by which plant immunity suppresses bacterial growth remain enigmatic. Here we show that Arabidopsis thaliana secreted aspartic protease 1 and 2 (SAP1 and SAP2) cleave the evoluti...

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Autores principales: Wang, Yiming, Garrido-Oter, Ruben, Wu, Jingni, Winkelmüller, Thomas M., Agler, Matthew, Colby, Thomas, Nobori, Tatsuya, Kemen, Eric, Tsuda, Kenichi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6599210/
https://www.ncbi.nlm.nih.gov/pubmed/31253808
http://dx.doi.org/10.1038/s41467-019-10793-x
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author Wang, Yiming
Garrido-Oter, Ruben
Wu, Jingni
Winkelmüller, Thomas M.
Agler, Matthew
Colby, Thomas
Nobori, Tatsuya
Kemen, Eric
Tsuda, Kenichi
author_facet Wang, Yiming
Garrido-Oter, Ruben
Wu, Jingni
Winkelmüller, Thomas M.
Agler, Matthew
Colby, Thomas
Nobori, Tatsuya
Kemen, Eric
Tsuda, Kenichi
author_sort Wang, Yiming
collection PubMed
description Plant innate immunity restricts growth of bacterial pathogens that threaten global food security. However, the mechanisms by which plant immunity suppresses bacterial growth remain enigmatic. Here we show that Arabidopsis thaliana secreted aspartic protease 1 and 2 (SAP1 and SAP2) cleave the evolutionarily conserved bacterial protein MucD to redundantly inhibit the growth of the bacterial pathogen Pseudomonas syringae. Antibacterial activity of SAP1 requires its protease activity in planta and in vitro. Plants overexpressing SAP1 exhibit enhanced MucD cleavage and resistance but incur no penalties in growth and reproduction, while sap1 sap2 double mutant plants exhibit compromised MucD cleavage and resistance against P. syringae. P. syringae lacking mucD shows compromised growth in planta and in vitro. Notably, growth of ΔmucD complemented with the non-cleavable MucD(F106Y) is not affected by SAP activity in planta and in vitro. Our findings identify the genetic factors and biochemical process underlying an antibacterial mechanism in plants.
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spelling pubmed-65992102019-07-01 Site-specific cleavage of bacterial MucD by secreted proteases mediates antibacterial resistance in Arabidopsis Wang, Yiming Garrido-Oter, Ruben Wu, Jingni Winkelmüller, Thomas M. Agler, Matthew Colby, Thomas Nobori, Tatsuya Kemen, Eric Tsuda, Kenichi Nat Commun Article Plant innate immunity restricts growth of bacterial pathogens that threaten global food security. However, the mechanisms by which plant immunity suppresses bacterial growth remain enigmatic. Here we show that Arabidopsis thaliana secreted aspartic protease 1 and 2 (SAP1 and SAP2) cleave the evolutionarily conserved bacterial protein MucD to redundantly inhibit the growth of the bacterial pathogen Pseudomonas syringae. Antibacterial activity of SAP1 requires its protease activity in planta and in vitro. Plants overexpressing SAP1 exhibit enhanced MucD cleavage and resistance but incur no penalties in growth and reproduction, while sap1 sap2 double mutant plants exhibit compromised MucD cleavage and resistance against P. syringae. P. syringae lacking mucD shows compromised growth in planta and in vitro. Notably, growth of ΔmucD complemented with the non-cleavable MucD(F106Y) is not affected by SAP activity in planta and in vitro. Our findings identify the genetic factors and biochemical process underlying an antibacterial mechanism in plants. Nature Publishing Group UK 2019-06-28 /pmc/articles/PMC6599210/ /pubmed/31253808 http://dx.doi.org/10.1038/s41467-019-10793-x Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Wang, Yiming
Garrido-Oter, Ruben
Wu, Jingni
Winkelmüller, Thomas M.
Agler, Matthew
Colby, Thomas
Nobori, Tatsuya
Kemen, Eric
Tsuda, Kenichi
Site-specific cleavage of bacterial MucD by secreted proteases mediates antibacterial resistance in Arabidopsis
title Site-specific cleavage of bacterial MucD by secreted proteases mediates antibacterial resistance in Arabidopsis
title_full Site-specific cleavage of bacterial MucD by secreted proteases mediates antibacterial resistance in Arabidopsis
title_fullStr Site-specific cleavage of bacterial MucD by secreted proteases mediates antibacterial resistance in Arabidopsis
title_full_unstemmed Site-specific cleavage of bacterial MucD by secreted proteases mediates antibacterial resistance in Arabidopsis
title_short Site-specific cleavage of bacterial MucD by secreted proteases mediates antibacterial resistance in Arabidopsis
title_sort site-specific cleavage of bacterial mucd by secreted proteases mediates antibacterial resistance in arabidopsis
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6599210/
https://www.ncbi.nlm.nih.gov/pubmed/31253808
http://dx.doi.org/10.1038/s41467-019-10793-x
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