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A hydrophobic anchor mechanism defines a deacetylase family that suppresses host response against YopJ effectors
Several Pseudomonas and Xanthomonas species are plant pathogens that infect the model organism Arabidopsis thaliana and important crops such as Brassica. Resistant plants contain the infection by rapid cell death of the infected area through the hypersensitive response (HR). A family of highly relat...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5736716/ https://www.ncbi.nlm.nih.gov/pubmed/29259199 http://dx.doi.org/10.1038/s41467-017-02347-w |
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author | Bürger, Marco Willige, Björn C. Chory, Joanne |
author_facet | Bürger, Marco Willige, Björn C. Chory, Joanne |
author_sort | Bürger, Marco |
collection | PubMed |
description | Several Pseudomonas and Xanthomonas species are plant pathogens that infect the model organism Arabidopsis thaliana and important crops such as Brassica. Resistant plants contain the infection by rapid cell death of the infected area through the hypersensitive response (HR). A family of highly related α/β hydrolases is involved in diverse processes in all domains of life. Functional details of their catalytic machinery, however, remained unclear. We report the crystal structures of α/β hydrolases representing two different clades of the family, including the protein SOBER1, which suppresses AvrBsT-incited HR in Arabidopsis. Our results reveal a unique hydrophobic anchor mechanism that defines a previously unknown family of protein deacetylases. Furthermore, this study identifies a lid-loop as general feature for substrate turnover in acyl-protein thioesterases and the described family of deacetylases. Furthermore, we found that SOBER1’s biological function is not restricted to Arabidopsis thaliana and not limited to suppress HR induced by AvrBsT. |
format | Online Article Text |
id | pubmed-5736716 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-57367162017-12-21 A hydrophobic anchor mechanism defines a deacetylase family that suppresses host response against YopJ effectors Bürger, Marco Willige, Björn C. Chory, Joanne Nat Commun Article Several Pseudomonas and Xanthomonas species are plant pathogens that infect the model organism Arabidopsis thaliana and important crops such as Brassica. Resistant plants contain the infection by rapid cell death of the infected area through the hypersensitive response (HR). A family of highly related α/β hydrolases is involved in diverse processes in all domains of life. Functional details of their catalytic machinery, however, remained unclear. We report the crystal structures of α/β hydrolases representing two different clades of the family, including the protein SOBER1, which suppresses AvrBsT-incited HR in Arabidopsis. Our results reveal a unique hydrophobic anchor mechanism that defines a previously unknown family of protein deacetylases. Furthermore, this study identifies a lid-loop as general feature for substrate turnover in acyl-protein thioesterases and the described family of deacetylases. Furthermore, we found that SOBER1’s biological function is not restricted to Arabidopsis thaliana and not limited to suppress HR induced by AvrBsT. Nature Publishing Group UK 2017-12-19 /pmc/articles/PMC5736716/ /pubmed/29259199 http://dx.doi.org/10.1038/s41467-017-02347-w Text en © The Author(s) 2017 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 Bürger, Marco Willige, Björn C. Chory, Joanne A hydrophobic anchor mechanism defines a deacetylase family that suppresses host response against YopJ effectors |
title | A hydrophobic anchor mechanism defines a deacetylase family that suppresses host response against YopJ effectors |
title_full | A hydrophobic anchor mechanism defines a deacetylase family that suppresses host response against YopJ effectors |
title_fullStr | A hydrophobic anchor mechanism defines a deacetylase family that suppresses host response against YopJ effectors |
title_full_unstemmed | A hydrophobic anchor mechanism defines a deacetylase family that suppresses host response against YopJ effectors |
title_short | A hydrophobic anchor mechanism defines a deacetylase family that suppresses host response against YopJ effectors |
title_sort | hydrophobic anchor mechanism defines a deacetylase family that suppresses host response against yopj effectors |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5736716/ https://www.ncbi.nlm.nih.gov/pubmed/29259199 http://dx.doi.org/10.1038/s41467-017-02347-w |
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