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Proanthocyanidin biosynthesis in the developing wheat seed coat investigated by chemical and RNA‐Seq analysis
The composition of proanthocyanidins in the testa (seed coat) of bread wheat was analyzed by thiolysis of PA oligomers from developing grain and found to consist of (+)‐catechin monomers, with a small amount of (+)‐gallocatechin. The average chain length of soluble PA stayed relatively constant betw...
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/PMC9554643/ https://www.ncbi.nlm.nih.gov/pubmed/36254336 http://dx.doi.org/10.1002/pld3.453 |
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author | Vaughan, Simon P. Baker, John M. Primavesi, Lucia F. Patil, Archana King, Robert Hassani‐Pak, Keywan Kulasekaran, Satish Coghill, Jane Ward, Jane L. Huttly, Alison K. Phillips, Andrew L. |
author_facet | Vaughan, Simon P. Baker, John M. Primavesi, Lucia F. Patil, Archana King, Robert Hassani‐Pak, Keywan Kulasekaran, Satish Coghill, Jane Ward, Jane L. Huttly, Alison K. Phillips, Andrew L. |
author_sort | Vaughan, Simon P. |
collection | PubMed |
description | The composition of proanthocyanidins in the testa (seed coat) of bread wheat was analyzed by thiolysis of PA oligomers from developing grain and found to consist of (+)‐catechin monomers, with a small amount of (+)‐gallocatechin. The average chain length of soluble PA stayed relatively constant between 10 and 20 days post‐anthesis, whereas that of unextractable PA increased over the same period, suggesting that increases in chain length might account for the insolubility of PAs from mature wheat grain. We carried out RNA‐Seq followed by differential expression analysis from dissected tissues of developing grain from red‐ and white‐grained near‐isogenic lines differing in the presence of an active R gene that encodes a MYB transcription factor involved in control of PA biosynthesis. In addition to genes already identified encoding chalcone synthase, chalcone isomerase, flavanone 3‐hydroxylase, and dihydroxyflavonoid 4‐reductase, we showed that wheat genes encoding phenylalanine ammonia lyase, flavonoid 3′,5′‐hydroxylase, leucoanthocyanidin reductase, and a glutathione S‐transferase (the orthologue of maize Bronze‐2) were more highly expressed in the red NIL. We also identified candidate orthologues of other catalytic and regulatory components of flavonoid biosynthesis in wheat. |
format | Online Article Text |
id | pubmed-9554643 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-95546432022-10-16 Proanthocyanidin biosynthesis in the developing wheat seed coat investigated by chemical and RNA‐Seq analysis Vaughan, Simon P. Baker, John M. Primavesi, Lucia F. Patil, Archana King, Robert Hassani‐Pak, Keywan Kulasekaran, Satish Coghill, Jane Ward, Jane L. Huttly, Alison K. Phillips, Andrew L. Plant Direct Original Research The composition of proanthocyanidins in the testa (seed coat) of bread wheat was analyzed by thiolysis of PA oligomers from developing grain and found to consist of (+)‐catechin monomers, with a small amount of (+)‐gallocatechin. The average chain length of soluble PA stayed relatively constant between 10 and 20 days post‐anthesis, whereas that of unextractable PA increased over the same period, suggesting that increases in chain length might account for the insolubility of PAs from mature wheat grain. We carried out RNA‐Seq followed by differential expression analysis from dissected tissues of developing grain from red‐ and white‐grained near‐isogenic lines differing in the presence of an active R gene that encodes a MYB transcription factor involved in control of PA biosynthesis. In addition to genes already identified encoding chalcone synthase, chalcone isomerase, flavanone 3‐hydroxylase, and dihydroxyflavonoid 4‐reductase, we showed that wheat genes encoding phenylalanine ammonia lyase, flavonoid 3′,5′‐hydroxylase, leucoanthocyanidin reductase, and a glutathione S‐transferase (the orthologue of maize Bronze‐2) were more highly expressed in the red NIL. We also identified candidate orthologues of other catalytic and regulatory components of flavonoid biosynthesis in wheat. John Wiley and Sons Inc. 2022-10-12 /pmc/articles/PMC9554643/ /pubmed/36254336 http://dx.doi.org/10.1002/pld3.453 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/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Original Research Vaughan, Simon P. Baker, John M. Primavesi, Lucia F. Patil, Archana King, Robert Hassani‐Pak, Keywan Kulasekaran, Satish Coghill, Jane Ward, Jane L. Huttly, Alison K. Phillips, Andrew L. Proanthocyanidin biosynthesis in the developing wheat seed coat investigated by chemical and RNA‐Seq analysis |
title | Proanthocyanidin biosynthesis in the developing wheat seed coat investigated by chemical and RNA‐Seq analysis |
title_full | Proanthocyanidin biosynthesis in the developing wheat seed coat investigated by chemical and RNA‐Seq analysis |
title_fullStr | Proanthocyanidin biosynthesis in the developing wheat seed coat investigated by chemical and RNA‐Seq analysis |
title_full_unstemmed | Proanthocyanidin biosynthesis in the developing wheat seed coat investigated by chemical and RNA‐Seq analysis |
title_short | Proanthocyanidin biosynthesis in the developing wheat seed coat investigated by chemical and RNA‐Seq analysis |
title_sort | proanthocyanidin biosynthesis in the developing wheat seed coat investigated by chemical and rna‐seq analysis |
topic | Original Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9554643/ https://www.ncbi.nlm.nih.gov/pubmed/36254336 http://dx.doi.org/10.1002/pld3.453 |
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