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A functional 4-hydroxybenzoate degradation pathway in the phytopathogen Xanthomonas campestris is required for full pathogenicity

Plants contain significant levels of natural phenolic compounds essential for reproduction and growth, as well as defense mechanisms against pathogens. Xanthomonas campestris pv. campestris (Xcc) is the causal agent of crucifers black rot. Here we showed that genes required for the synthesis, utiliz...

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Autores principales: Wang, Jia-Yuan, Zhou, Lian, Chen, Bo, Sun, Shuang, Zhang, Wei, Li, Ming, Tang, Hongzhi, Jiang, Bo-Le, Tang, Ji-Liang, He, Ya-Wen
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4682078/
https://www.ncbi.nlm.nih.gov/pubmed/26672484
http://dx.doi.org/10.1038/srep18456
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author Wang, Jia-Yuan
Zhou, Lian
Chen, Bo
Sun, Shuang
Zhang, Wei
Li, Ming
Tang, Hongzhi
Jiang, Bo-Le
Tang, Ji-Liang
He, Ya-Wen
author_facet Wang, Jia-Yuan
Zhou, Lian
Chen, Bo
Sun, Shuang
Zhang, Wei
Li, Ming
Tang, Hongzhi
Jiang, Bo-Le
Tang, Ji-Liang
He, Ya-Wen
author_sort Wang, Jia-Yuan
collection PubMed
description Plants contain significant levels of natural phenolic compounds essential for reproduction and growth, as well as defense mechanisms against pathogens. Xanthomonas campestris pv. campestris (Xcc) is the causal agent of crucifers black rot. Here we showed that genes required for the synthesis, utilization, transportation, and degradation of 4-hydroxybenzoate (4-HBA) are present in Xcc. Xcc rapidly degrades 4-HBA, but has no effect on 2-hydroxybenzoate and 3-hydroxybenzoate when grown in XOLN medium. The genes for 4-HBA degradation are organized in a superoperonic cluster. Bioinformatics, biochemical, and genetic data showed that 4-HBA is hydroxylated by 4-HBA 3-hydroxylase (PobA), which is encoded by Xcc0356, to yield PCA. The resulting PCA is further metabolized via the PCA branches of the β-ketoadipate pathway, including Xcc0364, Xcc0365, and PcaFHGBDCR. Xcc0364 and Xcc0365 encode a new form of β-ketoadipate succinyl-coenzyme A transferase that is required for 4-HBA degradation. pobA expression was induced by 4-HBA via the transcriptional activator, PobR. Radish and cabbage hydrolysates contain 2-HBA, 3-HBA, 4-HBA, and other phenolic compounds. Addition of radish and cabbage hydrolysates to Xcc culture significantly induced the expression of pobA via PobR. The 4-HBA degradation pathway is required for full pathogenicity of Xcc in radish.
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spelling pubmed-46820782015-12-18 A functional 4-hydroxybenzoate degradation pathway in the phytopathogen Xanthomonas campestris is required for full pathogenicity Wang, Jia-Yuan Zhou, Lian Chen, Bo Sun, Shuang Zhang, Wei Li, Ming Tang, Hongzhi Jiang, Bo-Le Tang, Ji-Liang He, Ya-Wen Sci Rep Article Plants contain significant levels of natural phenolic compounds essential for reproduction and growth, as well as defense mechanisms against pathogens. Xanthomonas campestris pv. campestris (Xcc) is the causal agent of crucifers black rot. Here we showed that genes required for the synthesis, utilization, transportation, and degradation of 4-hydroxybenzoate (4-HBA) are present in Xcc. Xcc rapidly degrades 4-HBA, but has no effect on 2-hydroxybenzoate and 3-hydroxybenzoate when grown in XOLN medium. The genes for 4-HBA degradation are organized in a superoperonic cluster. Bioinformatics, biochemical, and genetic data showed that 4-HBA is hydroxylated by 4-HBA 3-hydroxylase (PobA), which is encoded by Xcc0356, to yield PCA. The resulting PCA is further metabolized via the PCA branches of the β-ketoadipate pathway, including Xcc0364, Xcc0365, and PcaFHGBDCR. Xcc0364 and Xcc0365 encode a new form of β-ketoadipate succinyl-coenzyme A transferase that is required for 4-HBA degradation. pobA expression was induced by 4-HBA via the transcriptional activator, PobR. Radish and cabbage hydrolysates contain 2-HBA, 3-HBA, 4-HBA, and other phenolic compounds. Addition of radish and cabbage hydrolysates to Xcc culture significantly induced the expression of pobA via PobR. The 4-HBA degradation pathway is required for full pathogenicity of Xcc in radish. Nature Publishing Group 2015-12-17 /pmc/articles/PMC4682078/ /pubmed/26672484 http://dx.doi.org/10.1038/srep18456 Text en Copyright © 2015, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Wang, Jia-Yuan
Zhou, Lian
Chen, Bo
Sun, Shuang
Zhang, Wei
Li, Ming
Tang, Hongzhi
Jiang, Bo-Le
Tang, Ji-Liang
He, Ya-Wen
A functional 4-hydroxybenzoate degradation pathway in the phytopathogen Xanthomonas campestris is required for full pathogenicity
title A functional 4-hydroxybenzoate degradation pathway in the phytopathogen Xanthomonas campestris is required for full pathogenicity
title_full A functional 4-hydroxybenzoate degradation pathway in the phytopathogen Xanthomonas campestris is required for full pathogenicity
title_fullStr A functional 4-hydroxybenzoate degradation pathway in the phytopathogen Xanthomonas campestris is required for full pathogenicity
title_full_unstemmed A functional 4-hydroxybenzoate degradation pathway in the phytopathogen Xanthomonas campestris is required for full pathogenicity
title_short A functional 4-hydroxybenzoate degradation pathway in the phytopathogen Xanthomonas campestris is required for full pathogenicity
title_sort functional 4-hydroxybenzoate degradation pathway in the phytopathogen xanthomonas campestris is required for full pathogenicity
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4682078/
https://www.ncbi.nlm.nih.gov/pubmed/26672484
http://dx.doi.org/10.1038/srep18456
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