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Expression of a fungal exo-β-1,3-galactanase in Arabidopsis reveals a role of type II arabinogalactans in the regulation of cell shape
Arabinogalactan-proteins (AGPs) are a family of plant extracellular proteoglycans implicated in many physiological events. AGP is decorated with type II arabinogalactans (AGs) consisting of a β-1,3-galactan backbone and β-1,6-galactan side chains, to which other sugars are attached. Based on the fac...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7501824/ https://www.ncbi.nlm.nih.gov/pubmed/32470141 http://dx.doi.org/10.1093/jxb/eraa236 |
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author | Yoshimi, Yoshihisa Hara, Katsuya Yoshimura, Mami Tanaka, Nobukazu Higaki, Takumi Tsumuraya, Yoichi Kotake, Toshihisa |
author_facet | Yoshimi, Yoshihisa Hara, Katsuya Yoshimura, Mami Tanaka, Nobukazu Higaki, Takumi Tsumuraya, Yoichi Kotake, Toshihisa |
author_sort | Yoshimi, Yoshihisa |
collection | PubMed |
description | Arabinogalactan-proteins (AGPs) are a family of plant extracellular proteoglycans implicated in many physiological events. AGP is decorated with type II arabinogalactans (AGs) consisting of a β-1,3-galactan backbone and β-1,6-galactan side chains, to which other sugars are attached. Based on the fact that a type II AG-specific inhibitor, β-Yariv reagent, perturbs growth and development, it has been proposed that type II AGs participate in the regulation of cell shape and tissue organization. However, the mechanisms by which type II AGs participate have not yet been established. Here, we describe a novel system that causes specific degradation of type II AGs in Arabidopsis, by which a gene encoding a fungal exo-β-1,3-galactanase that specifically hydrolyzes β-1,3-galactan backbones of type II AGs is expressed under the control of a dexamethasone-inducible promoter. Dexamethasone treatment increased the galactanase activity, leading to a decrease in Yariv reagent-reactive AGPs in transgenic Arabidopsis. We detected the typical oligosaccharides released from type II AGs by Il3GAL in the soluble fraction, demonstrating that Il3GAL acted on type II AG in the transgenic plants. Additionally, this resulted in severe tissue disorganization in the hypocotyl and cotyledons, suggesting that the degradation of type II AGs affected the regulation of cell shape. |
format | Online Article Text |
id | pubmed-7501824 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-75018242020-09-25 Expression of a fungal exo-β-1,3-galactanase in Arabidopsis reveals a role of type II arabinogalactans in the regulation of cell shape Yoshimi, Yoshihisa Hara, Katsuya Yoshimura, Mami Tanaka, Nobukazu Higaki, Takumi Tsumuraya, Yoichi Kotake, Toshihisa J Exp Bot Research Papers Arabinogalactan-proteins (AGPs) are a family of plant extracellular proteoglycans implicated in many physiological events. AGP is decorated with type II arabinogalactans (AGs) consisting of a β-1,3-galactan backbone and β-1,6-galactan side chains, to which other sugars are attached. Based on the fact that a type II AG-specific inhibitor, β-Yariv reagent, perturbs growth and development, it has been proposed that type II AGs participate in the regulation of cell shape and tissue organization. However, the mechanisms by which type II AGs participate have not yet been established. Here, we describe a novel system that causes specific degradation of type II AGs in Arabidopsis, by which a gene encoding a fungal exo-β-1,3-galactanase that specifically hydrolyzes β-1,3-galactan backbones of type II AGs is expressed under the control of a dexamethasone-inducible promoter. Dexamethasone treatment increased the galactanase activity, leading to a decrease in Yariv reagent-reactive AGPs in transgenic Arabidopsis. We detected the typical oligosaccharides released from type II AGs by Il3GAL in the soluble fraction, demonstrating that Il3GAL acted on type II AG in the transgenic plants. Additionally, this resulted in severe tissue disorganization in the hypocotyl and cotyledons, suggesting that the degradation of type II AGs affected the regulation of cell shape. Oxford University Press 2020-05-29 /pmc/articles/PMC7501824/ /pubmed/32470141 http://dx.doi.org/10.1093/jxb/eraa236 Text en © The Author(s) 2020. Published by Oxford University Press on behalf of the Society for Experimental Biology. 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 reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Papers Yoshimi, Yoshihisa Hara, Katsuya Yoshimura, Mami Tanaka, Nobukazu Higaki, Takumi Tsumuraya, Yoichi Kotake, Toshihisa Expression of a fungal exo-β-1,3-galactanase in Arabidopsis reveals a role of type II arabinogalactans in the regulation of cell shape |
title | Expression of a fungal exo-β-1,3-galactanase in Arabidopsis reveals a role of type II arabinogalactans in the regulation of cell shape |
title_full | Expression of a fungal exo-β-1,3-galactanase in Arabidopsis reveals a role of type II arabinogalactans in the regulation of cell shape |
title_fullStr | Expression of a fungal exo-β-1,3-galactanase in Arabidopsis reveals a role of type II arabinogalactans in the regulation of cell shape |
title_full_unstemmed | Expression of a fungal exo-β-1,3-galactanase in Arabidopsis reveals a role of type II arabinogalactans in the regulation of cell shape |
title_short | Expression of a fungal exo-β-1,3-galactanase in Arabidopsis reveals a role of type II arabinogalactans in the regulation of cell shape |
title_sort | expression of a fungal exo-β-1,3-galactanase in arabidopsis reveals a role of type ii arabinogalactans in the regulation of cell shape |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7501824/ https://www.ncbi.nlm.nih.gov/pubmed/32470141 http://dx.doi.org/10.1093/jxb/eraa236 |
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