Mutations in DMI3 and SUNN Modify the Appressorium-Responsive Root Proteome in Arbuscular Mycorrhiza
Modification of the Medicago truncatula root proteome during the early stage of arbuscular mycorrhizal symbiosis was investigated by comparing, using two-dimensional electrophoresis, the protein patterns obtained from non-inoculated roots and roots synchronized for Glomus intraradices appressorium f...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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The American Phytopathological Society
2006-09-01
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| Series: | Molecular Plant-Microbe Interactions |
| Subjects: | |
| Online Access: | https://apsjournals.apsnet.org/doi/10.1094/MPMI-19-0988 |
| _version_ | 1811290291492093952 |
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| author | Nardjis Amiour Ghislaine Recorbet Franck Robert Silvio Gianinazzi Eliane Dumas-Gaudot |
| author_facet | Nardjis Amiour Ghislaine Recorbet Franck Robert Silvio Gianinazzi Eliane Dumas-Gaudot |
| author_sort | Nardjis Amiour |
| collection | DOAJ |
| description | Modification of the Medicago truncatula root proteome during the early stage of arbuscular mycorrhizal symbiosis was investigated by comparing, using two-dimensional electrophoresis, the protein patterns obtained from non-inoculated roots and roots synchronized for Glomus intraradices appressorium formation. This approach was conducted in wild-type (J5), mycorrhiza-defective (TRV25, dmi3), and autoregulation-defective (TR122, sunn) M. truncatula genotypes. The groups of proteins that responded to appressorium formation were further compared between wild-type and mutant genotypes; few overlaps and major differences were recorded, demonstrating that mutations in DMI3 and SUNN modified the appressorium-responsive root proteome. Except for a chalcone reductase, none of the differentially displayed proteins that could be identified using matrix-assisted laser desorption ionization time-of-flight mass spectrometry previously was known as appressorium responsive. A DMI3-dependent increased accumulation of signal transduction-related proteins (dehydroascorbate reductase, cyclophilin, and actin depolymerization factor) was found to precede mycorrhiza establishment. Differences in the accumulation of proteins related to plant defense reactions, cytoskeleton rearrangements, and auxin signaling upon symbiont contact were recorded between wild-type and hypermycorrhizal genotypes, pointing to some putative pathways by which SUNN may regulate very early arbuscule formation. |
| first_indexed | 2024-04-13T04:10:21Z |
| format | Article |
| id | doaj.art-cd65dc160c0949208efab81db57c3250 |
| institution | Directory Open Access Journal |
| issn | 0894-0282 1943-7706 |
| language | English |
| last_indexed | 2024-04-13T04:10:21Z |
| publishDate | 2006-09-01 |
| publisher | The American Phytopathological Society |
| record_format | Article |
| series | Molecular Plant-Microbe Interactions |
| spelling | doaj.art-cd65dc160c0949208efab81db57c32502022-12-22T03:03:08ZengThe American Phytopathological SocietyMolecular Plant-Microbe Interactions0894-02821943-77062006-09-0119998899710.1094/MPMI-19-0988Mutations in DMI3 and SUNN Modify the Appressorium-Responsive Root Proteome in Arbuscular MycorrhizaNardjis AmiourGhislaine RecorbetFranck RobertSilvio GianinazziEliane Dumas-GaudotModification of the Medicago truncatula root proteome during the early stage of arbuscular mycorrhizal symbiosis was investigated by comparing, using two-dimensional electrophoresis, the protein patterns obtained from non-inoculated roots and roots synchronized for Glomus intraradices appressorium formation. This approach was conducted in wild-type (J5), mycorrhiza-defective (TRV25, dmi3), and autoregulation-defective (TR122, sunn) M. truncatula genotypes. The groups of proteins that responded to appressorium formation were further compared between wild-type and mutant genotypes; few overlaps and major differences were recorded, demonstrating that mutations in DMI3 and SUNN modified the appressorium-responsive root proteome. Except for a chalcone reductase, none of the differentially displayed proteins that could be identified using matrix-assisted laser desorption ionization time-of-flight mass spectrometry previously was known as appressorium responsive. A DMI3-dependent increased accumulation of signal transduction-related proteins (dehydroascorbate reductase, cyclophilin, and actin depolymerization factor) was found to precede mycorrhiza establishment. Differences in the accumulation of proteins related to plant defense reactions, cytoskeleton rearrangements, and auxin signaling upon symbiont contact were recorded between wild-type and hypermycorrhizal genotypes, pointing to some putative pathways by which SUNN may regulate very early arbuscule formation.https://apsjournals.apsnet.org/doi/10.1094/MPMI-19-0988flavodoxinGSTMtAnn1narboninprotease inhibitor |
| spellingShingle | Nardjis Amiour Ghislaine Recorbet Franck Robert Silvio Gianinazzi Eliane Dumas-Gaudot Mutations in DMI3 and SUNN Modify the Appressorium-Responsive Root Proteome in Arbuscular Mycorrhiza Molecular Plant-Microbe Interactions flavodoxin GST MtAnn1 narbonin protease inhibitor |
| title | Mutations in DMI3 and SUNN Modify the Appressorium-Responsive Root Proteome in Arbuscular Mycorrhiza |
| title_full | Mutations in DMI3 and SUNN Modify the Appressorium-Responsive Root Proteome in Arbuscular Mycorrhiza |
| title_fullStr | Mutations in DMI3 and SUNN Modify the Appressorium-Responsive Root Proteome in Arbuscular Mycorrhiza |
| title_full_unstemmed | Mutations in DMI3 and SUNN Modify the Appressorium-Responsive Root Proteome in Arbuscular Mycorrhiza |
| title_short | Mutations in DMI3 and SUNN Modify the Appressorium-Responsive Root Proteome in Arbuscular Mycorrhiza |
| title_sort | mutations in dmi3 and sunn modify the appressorium responsive root proteome in arbuscular mycorrhiza |
| topic | flavodoxin GST MtAnn1 narbonin protease inhibitor |
| url | https://apsjournals.apsnet.org/doi/10.1094/MPMI-19-0988 |
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