Quantitative Proteomic Analysis of Castor (Ricinus communis L.) Seeds During Early Imbibition Provided Novel Insights into Cold Stress Response
Early planting is one of the strategies used to increase grain yield in temperate regions. However, poor cold tolerance in castor inhibits seed germination, resulting in lower seedling emergence and biomass. Here, the elite castor variety Tongbi 5 was used to identify the differential abundance prot...
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doaj-e763477429264eab81cd0b3e78b3cf682020-11-25T01:38:53ZengMDPI AGInternational Journal of Molecular Sciences1422-00672019-01-0120235510.3390/ijms20020355ijms20020355Quantitative Proteomic Analysis of Castor (Ricinus communis L.) Seeds During Early Imbibition Provided Novel Insights into Cold Stress ResponseXiaoyu Wang0Min Li1Xuming Liu2Lixue Zhang3Qiong Duan4Jixing Zhang5College of Life Science, Inner Mongolia University for Nationalities, Tongliao 028000, ChinaCollege of Agriculture, Inner Mongolia University for Nationalities, Tongliao 028000, ChinaCollege of Life Science, Inner Mongolia University for Nationalities, Tongliao 028000, ChinaCollege of Life Science, Inner Mongolia University for Nationalities, Tongliao 028000, ChinaCollege of Life Science, Inner Mongolia University for Nationalities, Tongliao 028000, ChinaCollege of Life Science, Inner Mongolia University for Nationalities, Tongliao 028000, ChinaEarly planting is one of the strategies used to increase grain yield in temperate regions. However, poor cold tolerance in castor inhibits seed germination, resulting in lower seedling emergence and biomass. Here, the elite castor variety Tongbi 5 was used to identify the differential abundance protein species (DAPS) between cold stress (4 °C) and control conditions (30 °C) imbibed seeds. As a result, 127 DAPS were identified according to isobaric tag for relative and absolute quantification (iTRAQ) strategy. These DAPS were mainly involved in carbohydrate and energy metabolism, translation and posttranslational modification, stress response, lipid transport and metabolism, and signal transduction. Enzyme-linked immunosorbent assays (ELISA) demonstrated that the quantitative proteomics data collected here were reliable. This study provided some invaluable insights into the cold stress responses of early imbibed castor seeds: (1) up-accumulation of all DAPS involved in translation might confer cold tolerance by promoting protein synthesis; (2) stress-related proteins probably protect the cell against damage caused by cold stress; (3) up-accumulation of key DAPS associated with fatty acid biosynthesis might facilitate resistance or adaptation of imbibed castor seeds to cold stress by the increased content of unsaturated fatty acid (UFA). The data has been deposited to the ProteomeXchange with identifier PXD010043.http://www.mdpi.com/1422-0067/20/2/355Ricinus communis L.cold stressseed imbibitioniTRAQproteomics |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Xiaoyu Wang Min Li Xuming Liu Lixue Zhang Qiong Duan Jixing Zhang |
spellingShingle |
Xiaoyu Wang Min Li Xuming Liu Lixue Zhang Qiong Duan Jixing Zhang Quantitative Proteomic Analysis of Castor (Ricinus communis L.) Seeds During Early Imbibition Provided Novel Insights into Cold Stress Response International Journal of Molecular Sciences Ricinus communis L. cold stress seed imbibition iTRAQ proteomics |
author_facet |
Xiaoyu Wang Min Li Xuming Liu Lixue Zhang Qiong Duan Jixing Zhang |
author_sort |
Xiaoyu Wang |
title |
Quantitative Proteomic Analysis of Castor (Ricinus communis L.) Seeds During Early Imbibition Provided Novel Insights into Cold Stress Response |
title_short |
Quantitative Proteomic Analysis of Castor (Ricinus communis L.) Seeds During Early Imbibition Provided Novel Insights into Cold Stress Response |
title_full |
Quantitative Proteomic Analysis of Castor (Ricinus communis L.) Seeds During Early Imbibition Provided Novel Insights into Cold Stress Response |
title_fullStr |
Quantitative Proteomic Analysis of Castor (Ricinus communis L.) Seeds During Early Imbibition Provided Novel Insights into Cold Stress Response |
title_full_unstemmed |
Quantitative Proteomic Analysis of Castor (Ricinus communis L.) Seeds During Early Imbibition Provided Novel Insights into Cold Stress Response |
title_sort |
quantitative proteomic analysis of castor (ricinus communis l.) seeds during early imbibition provided novel insights into cold stress response |
publisher |
MDPI AG |
series |
International Journal of Molecular Sciences |
issn |
1422-0067 |
publishDate |
2019-01-01 |
description |
Early planting is one of the strategies used to increase grain yield in temperate regions. However, poor cold tolerance in castor inhibits seed germination, resulting in lower seedling emergence and biomass. Here, the elite castor variety Tongbi 5 was used to identify the differential abundance protein species (DAPS) between cold stress (4 °C) and control conditions (30 °C) imbibed seeds. As a result, 127 DAPS were identified according to isobaric tag for relative and absolute quantification (iTRAQ) strategy. These DAPS were mainly involved in carbohydrate and energy metabolism, translation and posttranslational modification, stress response, lipid transport and metabolism, and signal transduction. Enzyme-linked immunosorbent assays (ELISA) demonstrated that the quantitative proteomics data collected here were reliable. This study provided some invaluable insights into the cold stress responses of early imbibed castor seeds: (1) up-accumulation of all DAPS involved in translation might confer cold tolerance by promoting protein synthesis; (2) stress-related proteins probably protect the cell against damage caused by cold stress; (3) up-accumulation of key DAPS associated with fatty acid biosynthesis might facilitate resistance or adaptation of imbibed castor seeds to cold stress by the increased content of unsaturated fatty acid (UFA). The data has been deposited to the ProteomeXchange with identifier PXD010043. |
topic |
Ricinus communis L. cold stress seed imbibition iTRAQ proteomics |
url |
http://www.mdpi.com/1422-0067/20/2/355 |
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