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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...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
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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. |
format | Online Article Text |
id | pubmed-6599210 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
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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