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Differences in glycosyltransferase family 61 accompany variation in seed coat mucilage composition in Plantago spp.
Xylans are the most abundant non-cellulosic polysaccharide found in plant cell walls. A diverse range of xylan structures influence tissue function during growth and development. Despite the abundance of xylans in nature, details of the genes and biochemical pathways controlling their biosynthesis a...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5181589/ https://www.ncbi.nlm.nih.gov/pubmed/27856710 http://dx.doi.org/10.1093/jxb/erw424 |
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author | Phan, Jana L. Tucker, Matthew R. Khor, Shi Fang Shirley, Neil Lahnstein, Jelle Beahan, Cherie Bacic, Antony Burton, Rachel A. |
author_facet | Phan, Jana L. Tucker, Matthew R. Khor, Shi Fang Shirley, Neil Lahnstein, Jelle Beahan, Cherie Bacic, Antony Burton, Rachel A. |
author_sort | Phan, Jana L. |
collection | PubMed |
description | Xylans are the most abundant non-cellulosic polysaccharide found in plant cell walls. A diverse range of xylan structures influence tissue function during growth and development. Despite the abundance of xylans in nature, details of the genes and biochemical pathways controlling their biosynthesis are lacking. In this study we have utilized natural variation within the Plantago genus to examine variation in heteroxylan composition and structure in seed coat mucilage. Compositional assays were combined with analysis of the glycosyltransferase family 61 (GT61) family during seed coat development, with the aim of identifying GT61 sequences participating in xylan backbone substitution. The results reveal natural variation in heteroxylan content and structure, particularly in P. ovata and P. cunninghamii, species which show a similar amount of heteroxylan but different backbone substitution profiles. Analysis of the GT61 family identified specific sequences co-expressed with IRREGULAR XYLEM 10 genes, which encode putative xylan synthases, revealing a close temporal association between xylan synthesis and substitution. Moreover, in P. ovata, several abundant GT61 sequences appear to lack orthologues in P. cunninghamii. Our results indicate that natural variation in Plantago species can be exploited to reveal novel details of seed coat development and polysaccharide biosynthetic pathways. |
format | Online Article Text |
id | pubmed-5181589 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-51815892016-12-27 Differences in glycosyltransferase family 61 accompany variation in seed coat mucilage composition in Plantago spp. Phan, Jana L. Tucker, Matthew R. Khor, Shi Fang Shirley, Neil Lahnstein, Jelle Beahan, Cherie Bacic, Antony Burton, Rachel A. J Exp Bot Research Paper Xylans are the most abundant non-cellulosic polysaccharide found in plant cell walls. A diverse range of xylan structures influence tissue function during growth and development. Despite the abundance of xylans in nature, details of the genes and biochemical pathways controlling their biosynthesis are lacking. In this study we have utilized natural variation within the Plantago genus to examine variation in heteroxylan composition and structure in seed coat mucilage. Compositional assays were combined with analysis of the glycosyltransferase family 61 (GT61) family during seed coat development, with the aim of identifying GT61 sequences participating in xylan backbone substitution. The results reveal natural variation in heteroxylan content and structure, particularly in P. ovata and P. cunninghamii, species which show a similar amount of heteroxylan but different backbone substitution profiles. Analysis of the GT61 family identified specific sequences co-expressed with IRREGULAR XYLEM 10 genes, which encode putative xylan synthases, revealing a close temporal association between xylan synthesis and substitution. Moreover, in P. ovata, several abundant GT61 sequences appear to lack orthologues in P. cunninghamii. Our results indicate that natural variation in Plantago species can be exploited to reveal novel details of seed coat development and polysaccharide biosynthetic pathways. Oxford University Press 2016-12 2016-11-17 /pmc/articles/PMC5181589/ /pubmed/27856710 http://dx.doi.org/10.1093/jxb/erw424 Text en © The Author 2016. Published by Oxford University Press on behalf of the Society for Experimental Biology. http://creativecommons.org/licenses/by/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Paper Phan, Jana L. Tucker, Matthew R. Khor, Shi Fang Shirley, Neil Lahnstein, Jelle Beahan, Cherie Bacic, Antony Burton, Rachel A. Differences in glycosyltransferase family 61 accompany variation in seed coat mucilage composition in Plantago spp. |
title | Differences in glycosyltransferase family 61 accompany variation in seed coat mucilage composition in Plantago spp. |
title_full | Differences in glycosyltransferase family 61 accompany variation in seed coat mucilage composition in Plantago spp. |
title_fullStr | Differences in glycosyltransferase family 61 accompany variation in seed coat mucilage composition in Plantago spp. |
title_full_unstemmed | Differences in glycosyltransferase family 61 accompany variation in seed coat mucilage composition in Plantago spp. |
title_short | Differences in glycosyltransferase family 61 accompany variation in seed coat mucilage composition in Plantago spp. |
title_sort | differences in glycosyltransferase family 61 accompany variation in seed coat mucilage composition in plantago spp. |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5181589/ https://www.ncbi.nlm.nih.gov/pubmed/27856710 http://dx.doi.org/10.1093/jxb/erw424 |
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