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Enzymatic fingerprinting reveals specific xyloglucan and pectin signatures in the cell wall purified with primary plasmodesmata
Plasmodesmata (PD) pores connect neighbouring plant cells and enable direct transport across the cell wall. Understanding the molecular composition of these structures is essential to address their formation and later dynamic regulation. Here we provide a biochemical characterisation of the cell wal...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9640925/ https://www.ncbi.nlm.nih.gov/pubmed/36388604 http://dx.doi.org/10.3389/fpls.2022.1020506 |
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author | Paterlini, A. Sechet, J. Immel, F. Grison, M. S. Pilard, S. Pelloux, J. Mouille, G. Bayer, E. M. Voxeur, A. |
author_facet | Paterlini, A. Sechet, J. Immel, F. Grison, M. S. Pilard, S. Pelloux, J. Mouille, G. Bayer, E. M. Voxeur, A. |
author_sort | Paterlini, A. |
collection | PubMed |
description | Plasmodesmata (PD) pores connect neighbouring plant cells and enable direct transport across the cell wall. Understanding the molecular composition of these structures is essential to address their formation and later dynamic regulation. Here we provide a biochemical characterisation of the cell wall co-purified with primary PD of Arabidopsis thaliana cell cultures. To achieve this result we combined subcellular fractionation, polysaccharide analyses and enzymatic fingerprinting approaches. Relative to the rest of the cell wall, specific patterns were observed in the PD fraction. Most xyloglucans, although possibly not abundant as a group, were fucosylated. Homogalacturonans displayed short methylated stretches while rhamnogalacturonan I species were remarkably abundant. Full rhamnogalacturonan II forms, highly methyl-acetylated, were also present. We additionally showed that these domains, compared to the broad wall, are less affected by wall modifying activities during a time interval of days. Overall, the protocol and the data presented here open new opportunities for the study of wall polysaccharides associated with PD. |
format | Online Article Text |
id | pubmed-9640925 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-96409252022-11-15 Enzymatic fingerprinting reveals specific xyloglucan and pectin signatures in the cell wall purified with primary plasmodesmata Paterlini, A. Sechet, J. Immel, F. Grison, M. S. Pilard, S. Pelloux, J. Mouille, G. Bayer, E. M. Voxeur, A. Front Plant Sci Plant Science Plasmodesmata (PD) pores connect neighbouring plant cells and enable direct transport across the cell wall. Understanding the molecular composition of these structures is essential to address their formation and later dynamic regulation. Here we provide a biochemical characterisation of the cell wall co-purified with primary PD of Arabidopsis thaliana cell cultures. To achieve this result we combined subcellular fractionation, polysaccharide analyses and enzymatic fingerprinting approaches. Relative to the rest of the cell wall, specific patterns were observed in the PD fraction. Most xyloglucans, although possibly not abundant as a group, were fucosylated. Homogalacturonans displayed short methylated stretches while rhamnogalacturonan I species were remarkably abundant. Full rhamnogalacturonan II forms, highly methyl-acetylated, were also present. We additionally showed that these domains, compared to the broad wall, are less affected by wall modifying activities during a time interval of days. Overall, the protocol and the data presented here open new opportunities for the study of wall polysaccharides associated with PD. Frontiers Media S.A. 2022-10-25 /pmc/articles/PMC9640925/ /pubmed/36388604 http://dx.doi.org/10.3389/fpls.2022.1020506 Text en Copyright © 2022 Paterlini, Sechet, Immel, Grison, Pilard, Pelloux, Mouille, Bayer and Voxeur https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Plant Science Paterlini, A. Sechet, J. Immel, F. Grison, M. S. Pilard, S. Pelloux, J. Mouille, G. Bayer, E. M. Voxeur, A. Enzymatic fingerprinting reveals specific xyloglucan and pectin signatures in the cell wall purified with primary plasmodesmata |
title | Enzymatic fingerprinting reveals specific xyloglucan and pectin signatures in the cell wall purified with primary plasmodesmata |
title_full | Enzymatic fingerprinting reveals specific xyloglucan and pectin signatures in the cell wall purified with primary plasmodesmata |
title_fullStr | Enzymatic fingerprinting reveals specific xyloglucan and pectin signatures in the cell wall purified with primary plasmodesmata |
title_full_unstemmed | Enzymatic fingerprinting reveals specific xyloglucan and pectin signatures in the cell wall purified with primary plasmodesmata |
title_short | Enzymatic fingerprinting reveals specific xyloglucan and pectin signatures in the cell wall purified with primary plasmodesmata |
title_sort | enzymatic fingerprinting reveals specific xyloglucan and pectin signatures in the cell wall purified with primary plasmodesmata |
topic | Plant Science |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9640925/ https://www.ncbi.nlm.nih.gov/pubmed/36388604 http://dx.doi.org/10.3389/fpls.2022.1020506 |
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