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Heat-Responsive Proteomics of a Heat-Sensitive Spinach Variety

High temperatures seriously limit plant growth and productivity. Investigating heat-responsive molecular mechanisms is important for breeding heat-tolerant crops. In this study, heat-responsive mechanisms in leaves from a heat-sensitive spinach (Spinacia oleracea L.) variety Sp73 were investigated u...

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Autores principales: Li, Shanshan, Yu, Juanjuan, Li, Ying, Zhang, Heng, Bao, Xuesong, Bian, Jiayi, Xu, Chenxi, Wang, Xiaoli, Cai, Xiaofeng, Wang, Quanhua, Wang, Pengcheng, Guo, Siyi, Miao, Yuchen, Chen, Sixue, Qin, Zhi, Dai, Shaojun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6720816/
https://www.ncbi.nlm.nih.gov/pubmed/31398909
http://dx.doi.org/10.3390/ijms20163872
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author Li, Shanshan
Yu, Juanjuan
Li, Ying
Zhang, Heng
Bao, Xuesong
Bian, Jiayi
Xu, Chenxi
Wang, Xiaoli
Cai, Xiaofeng
Wang, Quanhua
Wang, Pengcheng
Guo, Siyi
Miao, Yuchen
Chen, Sixue
Qin, Zhi
Dai, Shaojun
author_facet Li, Shanshan
Yu, Juanjuan
Li, Ying
Zhang, Heng
Bao, Xuesong
Bian, Jiayi
Xu, Chenxi
Wang, Xiaoli
Cai, Xiaofeng
Wang, Quanhua
Wang, Pengcheng
Guo, Siyi
Miao, Yuchen
Chen, Sixue
Qin, Zhi
Dai, Shaojun
author_sort Li, Shanshan
collection PubMed
description High temperatures seriously limit plant growth and productivity. Investigating heat-responsive molecular mechanisms is important for breeding heat-tolerant crops. In this study, heat-responsive mechanisms in leaves from a heat-sensitive spinach (Spinacia oleracea L.) variety Sp73 were investigated using two-dimensional gel electrophoresis (2DE)-based and isobaric tags for relative and absolute quantification (iTRAQ)-based proteomics approaches. In total, 257 heat-responsive proteins were identified in the spinach leaves. The abundance patterns of these proteins indicated that the photosynthesis process was inhibited, reactive oxygen species (ROS) scavenging pathways were initiated, and protein synthesis and turnover, carbohydrate and amino acid metabolism were promoted in the spinach Sp73 in response to high temperature. By comparing this with our previous results in the heat-tolerant spinach variety Sp75, we found that heat inhibited photosynthesis, as well as heat-enhanced ROS scavenging, stress defense pathways, carbohydrate and energy metabolism, and protein folding and turnover constituting a conservative strategy for spinach in response to heat stress. However, the heat-decreased biosynthesis of chlorophyll and carotenoid as well as soluble sugar content in the variety Sp73 was quite different from that in the variety Sp75, leading to a lower capability for photosynthetic adaptation and osmotic homeostasis in Sp73 under heat stress. Moreover, the heat-reduced activities of SOD and other heat-activated antioxidant enzymes in the heat-sensitive variety Sp73 were also different from the heat-tolerant variety Sp75, implying that the ROS scavenging strategy is critical for heat tolerance.
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spelling pubmed-67208162019-09-10 Heat-Responsive Proteomics of a Heat-Sensitive Spinach Variety Li, Shanshan Yu, Juanjuan Li, Ying Zhang, Heng Bao, Xuesong Bian, Jiayi Xu, Chenxi Wang, Xiaoli Cai, Xiaofeng Wang, Quanhua Wang, Pengcheng Guo, Siyi Miao, Yuchen Chen, Sixue Qin, Zhi Dai, Shaojun Int J Mol Sci Article High temperatures seriously limit plant growth and productivity. Investigating heat-responsive molecular mechanisms is important for breeding heat-tolerant crops. In this study, heat-responsive mechanisms in leaves from a heat-sensitive spinach (Spinacia oleracea L.) variety Sp73 were investigated using two-dimensional gel electrophoresis (2DE)-based and isobaric tags for relative and absolute quantification (iTRAQ)-based proteomics approaches. In total, 257 heat-responsive proteins were identified in the spinach leaves. The abundance patterns of these proteins indicated that the photosynthesis process was inhibited, reactive oxygen species (ROS) scavenging pathways were initiated, and protein synthesis and turnover, carbohydrate and amino acid metabolism were promoted in the spinach Sp73 in response to high temperature. By comparing this with our previous results in the heat-tolerant spinach variety Sp75, we found that heat inhibited photosynthesis, as well as heat-enhanced ROS scavenging, stress defense pathways, carbohydrate and energy metabolism, and protein folding and turnover constituting a conservative strategy for spinach in response to heat stress. However, the heat-decreased biosynthesis of chlorophyll and carotenoid as well as soluble sugar content in the variety Sp73 was quite different from that in the variety Sp75, leading to a lower capability for photosynthetic adaptation and osmotic homeostasis in Sp73 under heat stress. Moreover, the heat-reduced activities of SOD and other heat-activated antioxidant enzymes in the heat-sensitive variety Sp73 were also different from the heat-tolerant variety Sp75, implying that the ROS scavenging strategy is critical for heat tolerance. MDPI 2019-08-08 /pmc/articles/PMC6720816/ /pubmed/31398909 http://dx.doi.org/10.3390/ijms20163872 Text en © 2019 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
Li, Shanshan
Yu, Juanjuan
Li, Ying
Zhang, Heng
Bao, Xuesong
Bian, Jiayi
Xu, Chenxi
Wang, Xiaoli
Cai, Xiaofeng
Wang, Quanhua
Wang, Pengcheng
Guo, Siyi
Miao, Yuchen
Chen, Sixue
Qin, Zhi
Dai, Shaojun
Heat-Responsive Proteomics of a Heat-Sensitive Spinach Variety
title Heat-Responsive Proteomics of a Heat-Sensitive Spinach Variety
title_full Heat-Responsive Proteomics of a Heat-Sensitive Spinach Variety
title_fullStr Heat-Responsive Proteomics of a Heat-Sensitive Spinach Variety
title_full_unstemmed Heat-Responsive Proteomics of a Heat-Sensitive Spinach Variety
title_short Heat-Responsive Proteomics of a Heat-Sensitive Spinach Variety
title_sort heat-responsive proteomics of a heat-sensitive spinach variety
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6720816/
https://www.ncbi.nlm.nih.gov/pubmed/31398909
http://dx.doi.org/10.3390/ijms20163872
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