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Arabidopsis thaliana responds to colonisation of Piriformospora indica by secretion of symbiosis-specific proteins

Plants interact with a wide variety of fungi in a mutualistic, parasitic or neutral way. The associations formed depend on the exchange of nutrients and signalling molecules between the partners. This includes a diverse set of protein classes involved in defence, nutrient uptake or establishing a sy...

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Autores principales: Thürich, Johannes, Meichsner, Doreen, Furch, Alexandra C. U., Pfalz, Jeannette, Krüger, Thomas, Kniemeyer, Olaf, Brakhage, Axel, Oelmüller, Ralf
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6307754/
https://www.ncbi.nlm.nih.gov/pubmed/30589877
http://dx.doi.org/10.1371/journal.pone.0209658
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author Thürich, Johannes
Meichsner, Doreen
Furch, Alexandra C. U.
Pfalz, Jeannette
Krüger, Thomas
Kniemeyer, Olaf
Brakhage, Axel
Oelmüller, Ralf
author_facet Thürich, Johannes
Meichsner, Doreen
Furch, Alexandra C. U.
Pfalz, Jeannette
Krüger, Thomas
Kniemeyer, Olaf
Brakhage, Axel
Oelmüller, Ralf
author_sort Thürich, Johannes
collection PubMed
description Plants interact with a wide variety of fungi in a mutualistic, parasitic or neutral way. The associations formed depend on the exchange of nutrients and signalling molecules between the partners. This includes a diverse set of protein classes involved in defence, nutrient uptake or establishing a symbiotic relationship. Here, we have analysed the secretomes of the mutualistic, root-endophytic fungus Piriformospora indica and Arabidopsis thaliana when cultivated alone or in a co-culture. More than one hundred proteins were identified as differentially secreted, including proteins associated with growth, development, abiotic and biotic stress response and mucilage. While some of the proteins have been associated before to be involved in plant-microbial interaction, other proteins are newly described in this context. One plant protein found in the co-culture is PLAT1 (Polycystin, Lipoxygenase, Alpha-toxin and Triacylglycerol lipase). PLAT1 has not been associated with plant-fungal-interaction and is known to play a role in abiotic stress responses. In colonised roots PLAT1 shows an altered gene expression in a stage specific manner and plat1 knock-out plants are colonised stronger. It co-localises with Brassicaceae-specific endoplasmic reticulum bodies (ER-bodies) which are involved in the formation of the defence compound scopolin. We observed degraded ER-bodies in infected Arabidopsis roots and a change in the scopolin level in response to the presence of the fungus.
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spelling pubmed-63077542019-01-08 Arabidopsis thaliana responds to colonisation of Piriformospora indica by secretion of symbiosis-specific proteins Thürich, Johannes Meichsner, Doreen Furch, Alexandra C. U. Pfalz, Jeannette Krüger, Thomas Kniemeyer, Olaf Brakhage, Axel Oelmüller, Ralf PLoS One Research Article Plants interact with a wide variety of fungi in a mutualistic, parasitic or neutral way. The associations formed depend on the exchange of nutrients and signalling molecules between the partners. This includes a diverse set of protein classes involved in defence, nutrient uptake or establishing a symbiotic relationship. Here, we have analysed the secretomes of the mutualistic, root-endophytic fungus Piriformospora indica and Arabidopsis thaliana when cultivated alone or in a co-culture. More than one hundred proteins were identified as differentially secreted, including proteins associated with growth, development, abiotic and biotic stress response and mucilage. While some of the proteins have been associated before to be involved in plant-microbial interaction, other proteins are newly described in this context. One plant protein found in the co-culture is PLAT1 (Polycystin, Lipoxygenase, Alpha-toxin and Triacylglycerol lipase). PLAT1 has not been associated with plant-fungal-interaction and is known to play a role in abiotic stress responses. In colonised roots PLAT1 shows an altered gene expression in a stage specific manner and plat1 knock-out plants are colonised stronger. It co-localises with Brassicaceae-specific endoplasmic reticulum bodies (ER-bodies) which are involved in the formation of the defence compound scopolin. We observed degraded ER-bodies in infected Arabidopsis roots and a change in the scopolin level in response to the presence of the fungus. Public Library of Science 2018-12-27 /pmc/articles/PMC6307754/ /pubmed/30589877 http://dx.doi.org/10.1371/journal.pone.0209658 Text en © 2018 Thürich et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Thürich, Johannes
Meichsner, Doreen
Furch, Alexandra C. U.
Pfalz, Jeannette
Krüger, Thomas
Kniemeyer, Olaf
Brakhage, Axel
Oelmüller, Ralf
Arabidopsis thaliana responds to colonisation of Piriformospora indica by secretion of symbiosis-specific proteins
title Arabidopsis thaliana responds to colonisation of Piriformospora indica by secretion of symbiosis-specific proteins
title_full Arabidopsis thaliana responds to colonisation of Piriformospora indica by secretion of symbiosis-specific proteins
title_fullStr Arabidopsis thaliana responds to colonisation of Piriformospora indica by secretion of symbiosis-specific proteins
title_full_unstemmed Arabidopsis thaliana responds to colonisation of Piriformospora indica by secretion of symbiosis-specific proteins
title_short Arabidopsis thaliana responds to colonisation of Piriformospora indica by secretion of symbiosis-specific proteins
title_sort arabidopsis thaliana responds to colonisation of piriformospora indica by secretion of symbiosis-specific proteins
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6307754/
https://www.ncbi.nlm.nih.gov/pubmed/30589877
http://dx.doi.org/10.1371/journal.pone.0209658
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