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Identification of BAHD acyltransferases associated with acylinositol biosynthesis in Solanum quitoense (naranjilla)
Plants make a variety of specialized metabolites that can mediate interactions with animals, microbes, and competitor plants. Understanding how plants synthesize these compounds enables studies of their biological roles by manipulating their synthesis in vivo as well as producing them in vitro. Acyl...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9219006/ https://www.ncbi.nlm.nih.gov/pubmed/35774622 http://dx.doi.org/10.1002/pld3.415 |
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author | Leong, Bryan J. Hurney, Steven Fiesel, Paul Anthony, Thilani M. Moghe, Gaurav Jones, Arthur Daniel Last, Robert L. |
author_facet | Leong, Bryan J. Hurney, Steven Fiesel, Paul Anthony, Thilani M. Moghe, Gaurav Jones, Arthur Daniel Last, Robert L. |
author_sort | Leong, Bryan J. |
collection | PubMed |
description | Plants make a variety of specialized metabolites that can mediate interactions with animals, microbes, and competitor plants. Understanding how plants synthesize these compounds enables studies of their biological roles by manipulating their synthesis in vivo as well as producing them in vitro. Acylsugars are a group of protective metabolites that accumulate in the trichomes of many Solanaceae family plants. Acylinositol biosynthesis is of interest because it appears to be restricted to a subgroup of species within the Solanum genus. Previous work characterized a triacylinositol acetyltransferase involved in acylinositol biosynthesis in the Andean fruit plant Solanum quitoense (lulo or naranjilla). We characterized three additional S. quitoense trichome expressed enzymes and found that virus‐induced gene silencing of each caused changes in acylinositol accumulation. pH was shown to influence the stability and rearrangement of the product of ASAT1H and could potentially play a role in acylinositol biosynthesis. Surprisingly, the in vitro triacylinositol products of these enzymes are distinct from those that accumulate in planta. This suggests that additional enzymes are required in acylinositol biosynthesis. These characterized S. quitoense enzymes, nonetheless, provide opportunities to test the biological impact and properties of these triacylinositols in vitro. |
format | Online Article Text |
id | pubmed-9219006 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-92190062022-06-29 Identification of BAHD acyltransferases associated with acylinositol biosynthesis in Solanum quitoense (naranjilla) Leong, Bryan J. Hurney, Steven Fiesel, Paul Anthony, Thilani M. Moghe, Gaurav Jones, Arthur Daniel Last, Robert L. Plant Direct Original Research Plants make a variety of specialized metabolites that can mediate interactions with animals, microbes, and competitor plants. Understanding how plants synthesize these compounds enables studies of their biological roles by manipulating their synthesis in vivo as well as producing them in vitro. Acylsugars are a group of protective metabolites that accumulate in the trichomes of many Solanaceae family plants. Acylinositol biosynthesis is of interest because it appears to be restricted to a subgroup of species within the Solanum genus. Previous work characterized a triacylinositol acetyltransferase involved in acylinositol biosynthesis in the Andean fruit plant Solanum quitoense (lulo or naranjilla). We characterized three additional S. quitoense trichome expressed enzymes and found that virus‐induced gene silencing of each caused changes in acylinositol accumulation. pH was shown to influence the stability and rearrangement of the product of ASAT1H and could potentially play a role in acylinositol biosynthesis. Surprisingly, the in vitro triacylinositol products of these enzymes are distinct from those that accumulate in planta. This suggests that additional enzymes are required in acylinositol biosynthesis. These characterized S. quitoense enzymes, nonetheless, provide opportunities to test the biological impact and properties of these triacylinositols in vitro. John Wiley and Sons Inc. 2022-06-18 /pmc/articles/PMC9219006/ /pubmed/35774622 http://dx.doi.org/10.1002/pld3.415 Text en © 2022 The Authors. Plant Direct published by American Society of Plant Biologists and the Society for Experimental Biology and John Wiley & Sons Ltd. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ (https://creativecommons.org/licenses/by-nc-nd/4.0/) License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made. |
spellingShingle | Original Research Leong, Bryan J. Hurney, Steven Fiesel, Paul Anthony, Thilani M. Moghe, Gaurav Jones, Arthur Daniel Last, Robert L. Identification of BAHD acyltransferases associated with acylinositol biosynthesis in Solanum quitoense (naranjilla) |
title | Identification of BAHD acyltransferases associated with acylinositol biosynthesis in
Solanum quitoense
(naranjilla) |
title_full | Identification of BAHD acyltransferases associated with acylinositol biosynthesis in
Solanum quitoense
(naranjilla) |
title_fullStr | Identification of BAHD acyltransferases associated with acylinositol biosynthesis in
Solanum quitoense
(naranjilla) |
title_full_unstemmed | Identification of BAHD acyltransferases associated with acylinositol biosynthesis in
Solanum quitoense
(naranjilla) |
title_short | Identification of BAHD acyltransferases associated with acylinositol biosynthesis in
Solanum quitoense
(naranjilla) |
title_sort | identification of bahd acyltransferases associated with acylinositol biosynthesis in
solanum quitoense
(naranjilla) |
topic | Original Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9219006/ https://www.ncbi.nlm.nih.gov/pubmed/35774622 http://dx.doi.org/10.1002/pld3.415 |
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