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Myo-inositol oxygenase is important for the removal of excess myo-inositol from syncytia induced by Heterodera schachtii in Arabidopsis roots

The enzyme myo-inositol oxygenase is the key enzyme of a pathway leading from myo-inositol to UDP-glucuronic acid. In Arabidopsis, myo-inositol oxygenase is encoded by four genes. All genes are strongly expressed in syncytia induced by the beet cyst nematode Heterodera schachtii in Arabidopsis roots...

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Autores principales: Siddique, Shahid, Endres, Stefanie, Sobczak, Miroslaw, Radakovic, Zoran S, Fragner, Lena, Grundler, Florian M W, Weckwerth, Wolfram, Tenhaken, Raimund, Bohlmann, Holger
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BlackWell Publishing Ltd 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4285123/
https://www.ncbi.nlm.nih.gov/pubmed/24117492
http://dx.doi.org/10.1111/nph.12535
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author Siddique, Shahid
Endres, Stefanie
Sobczak, Miroslaw
Radakovic, Zoran S
Fragner, Lena
Grundler, Florian M W
Weckwerth, Wolfram
Tenhaken, Raimund
Bohlmann, Holger
author_facet Siddique, Shahid
Endres, Stefanie
Sobczak, Miroslaw
Radakovic, Zoran S
Fragner, Lena
Grundler, Florian M W
Weckwerth, Wolfram
Tenhaken, Raimund
Bohlmann, Holger
author_sort Siddique, Shahid
collection PubMed
description The enzyme myo-inositol oxygenase is the key enzyme of a pathway leading from myo-inositol to UDP-glucuronic acid. In Arabidopsis, myo-inositol oxygenase is encoded by four genes. All genes are strongly expressed in syncytia induced by the beet cyst nematode Heterodera schachtii in Arabidopsis roots. Here, we studied the effect of a quadruple myo-inositol oxygenase mutant on nematode development. . We performed metabolite profiling of syncytia induced in roots of the myo-inositol oxygenase quadruple mutant. The role of galactinol in syncytia was studied using Arabidopsis lines with elevated galactinol levels and by supplying galactinol to wild-type seedlings. . The quadruple myo-inositol oxygenase mutant showed a significant reduction in susceptibility to H. schachtii, and syncytia had elevated myo-inositol and galactinol levels and an elevated expression level of the antimicrobial thionin gene Thi2.1. This reduction in susceptibility could also be achieved by exogenous application of galactinol to wild-type seedlings. . The primary function of myo-inositol oxygenase for syncytium development is probably not the production of UDP-glucuronic acid as a precursor for cell wall polysaccharides, but the reduction of myo-inositol levels and thereby a reduction in the galactinol level to avoid the induction of defence-related genes. .
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spelling pubmed-42851232015-01-26 Myo-inositol oxygenase is important for the removal of excess myo-inositol from syncytia induced by Heterodera schachtii in Arabidopsis roots Siddique, Shahid Endres, Stefanie Sobczak, Miroslaw Radakovic, Zoran S Fragner, Lena Grundler, Florian M W Weckwerth, Wolfram Tenhaken, Raimund Bohlmann, Holger New Phytol Research The enzyme myo-inositol oxygenase is the key enzyme of a pathway leading from myo-inositol to UDP-glucuronic acid. In Arabidopsis, myo-inositol oxygenase is encoded by four genes. All genes are strongly expressed in syncytia induced by the beet cyst nematode Heterodera schachtii in Arabidopsis roots. Here, we studied the effect of a quadruple myo-inositol oxygenase mutant on nematode development. . We performed metabolite profiling of syncytia induced in roots of the myo-inositol oxygenase quadruple mutant. The role of galactinol in syncytia was studied using Arabidopsis lines with elevated galactinol levels and by supplying galactinol to wild-type seedlings. . The quadruple myo-inositol oxygenase mutant showed a significant reduction in susceptibility to H. schachtii, and syncytia had elevated myo-inositol and galactinol levels and an elevated expression level of the antimicrobial thionin gene Thi2.1. This reduction in susceptibility could also be achieved by exogenous application of galactinol to wild-type seedlings. . The primary function of myo-inositol oxygenase for syncytium development is probably not the production of UDP-glucuronic acid as a precursor for cell wall polysaccharides, but the reduction of myo-inositol levels and thereby a reduction in the galactinol level to avoid the induction of defence-related genes. . BlackWell Publishing Ltd 2014-01 2013-10-01 /pmc/articles/PMC4285123/ /pubmed/24117492 http://dx.doi.org/10.1111/nph.12535 Text en © 2013 The Authors. New Phytologist © 2013 New Phytologist Trust http://creativecommons.org/licenses/by/3.0/ This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research
Siddique, Shahid
Endres, Stefanie
Sobczak, Miroslaw
Radakovic, Zoran S
Fragner, Lena
Grundler, Florian M W
Weckwerth, Wolfram
Tenhaken, Raimund
Bohlmann, Holger
Myo-inositol oxygenase is important for the removal of excess myo-inositol from syncytia induced by Heterodera schachtii in Arabidopsis roots
title Myo-inositol oxygenase is important for the removal of excess myo-inositol from syncytia induced by Heterodera schachtii in Arabidopsis roots
title_full Myo-inositol oxygenase is important for the removal of excess myo-inositol from syncytia induced by Heterodera schachtii in Arabidopsis roots
title_fullStr Myo-inositol oxygenase is important for the removal of excess myo-inositol from syncytia induced by Heterodera schachtii in Arabidopsis roots
title_full_unstemmed Myo-inositol oxygenase is important for the removal of excess myo-inositol from syncytia induced by Heterodera schachtii in Arabidopsis roots
title_short Myo-inositol oxygenase is important for the removal of excess myo-inositol from syncytia induced by Heterodera schachtii in Arabidopsis roots
title_sort myo-inositol oxygenase is important for the removal of excess myo-inositol from syncytia induced by heterodera schachtii in arabidopsis roots
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4285123/
https://www.ncbi.nlm.nih.gov/pubmed/24117492
http://dx.doi.org/10.1111/nph.12535
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