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Proteomic Analysis of Proteins Responsive to Drought and Low Temperature Stress in a Hard Red Spring Wheat Cultivar
Drought stress is becoming more prevalent with global warming, and has been shown to have large effects on gluten proteins linked to wheat bread making quality. Likewise, low temperature stress can detrimentally affect proteins in wheat. This study was done to determine the differential abundance of...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7144396/ https://www.ncbi.nlm.nih.gov/pubmed/32192150 http://dx.doi.org/10.3390/molecules25061366 |
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author | Labuschagne, Maryke Masci, Stefania Tundo, Silvio Muccilli, Vera Saletti, Rosaria van Biljon, Angeline |
author_facet | Labuschagne, Maryke Masci, Stefania Tundo, Silvio Muccilli, Vera Saletti, Rosaria van Biljon, Angeline |
author_sort | Labuschagne, Maryke |
collection | PubMed |
description | Drought stress is becoming more prevalent with global warming, and has been shown to have large effects on gluten proteins linked to wheat bread making quality. Likewise, low temperature stress can detrimentally affect proteins in wheat. This study was done to determine the differential abundance of high molecular weight (HMW) glutenin proteins in a drought and low temperature stressed high quality hard red spring wheat cultivar (PAN3478), against a control. The treatments were applied in the greenhouse at the soft dough stage. HMW glutenin proteins were extracted from the flour, and were separated by using two-dimensional gel electrophoresis. Protein spots that had p values lower than 0.05 and fold values equal to or greater than 1.2 were considered to be significantly differentially abundant. These proteins were further analyzed by using tandem mass spectrometry. There was a 1.3 to 1.8 fold change in 17 protein spots due to the cold treatment. The drought treatment caused a 1.3 to 3.8 fold change in 19 protein spots. These spots matched either HMW or low molecular weight (LMW) glutenin subunits. In the latter case, the C subunits of LMW glutenins were notably found to be up-regulated under both stress conditions. All the proteins that have been identified can directly influence dough characteristics. Data are available via ProteomeXchange with the identifier PXD017578. |
format | Online Article Text |
id | pubmed-7144396 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-71443962020-04-13 Proteomic Analysis of Proteins Responsive to Drought and Low Temperature Stress in a Hard Red Spring Wheat Cultivar Labuschagne, Maryke Masci, Stefania Tundo, Silvio Muccilli, Vera Saletti, Rosaria van Biljon, Angeline Molecules Article Drought stress is becoming more prevalent with global warming, and has been shown to have large effects on gluten proteins linked to wheat bread making quality. Likewise, low temperature stress can detrimentally affect proteins in wheat. This study was done to determine the differential abundance of high molecular weight (HMW) glutenin proteins in a drought and low temperature stressed high quality hard red spring wheat cultivar (PAN3478), against a control. The treatments were applied in the greenhouse at the soft dough stage. HMW glutenin proteins were extracted from the flour, and were separated by using two-dimensional gel electrophoresis. Protein spots that had p values lower than 0.05 and fold values equal to or greater than 1.2 were considered to be significantly differentially abundant. These proteins were further analyzed by using tandem mass spectrometry. There was a 1.3 to 1.8 fold change in 17 protein spots due to the cold treatment. The drought treatment caused a 1.3 to 3.8 fold change in 19 protein spots. These spots matched either HMW or low molecular weight (LMW) glutenin subunits. In the latter case, the C subunits of LMW glutenins were notably found to be up-regulated under both stress conditions. All the proteins that have been identified can directly influence dough characteristics. Data are available via ProteomeXchange with the identifier PXD017578. MDPI 2020-03-17 /pmc/articles/PMC7144396/ /pubmed/32192150 http://dx.doi.org/10.3390/molecules25061366 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Labuschagne, Maryke Masci, Stefania Tundo, Silvio Muccilli, Vera Saletti, Rosaria van Biljon, Angeline Proteomic Analysis of Proteins Responsive to Drought and Low Temperature Stress in a Hard Red Spring Wheat Cultivar |
title | Proteomic Analysis of Proteins Responsive to Drought and Low Temperature Stress in a Hard Red Spring Wheat Cultivar |
title_full | Proteomic Analysis of Proteins Responsive to Drought and Low Temperature Stress in a Hard Red Spring Wheat Cultivar |
title_fullStr | Proteomic Analysis of Proteins Responsive to Drought and Low Temperature Stress in a Hard Red Spring Wheat Cultivar |
title_full_unstemmed | Proteomic Analysis of Proteins Responsive to Drought and Low Temperature Stress in a Hard Red Spring Wheat Cultivar |
title_short | Proteomic Analysis of Proteins Responsive to Drought and Low Temperature Stress in a Hard Red Spring Wheat Cultivar |
title_sort | proteomic analysis of proteins responsive to drought and low temperature stress in a hard red spring wheat cultivar |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7144396/ https://www.ncbi.nlm.nih.gov/pubmed/32192150 http://dx.doi.org/10.3390/molecules25061366 |
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