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Proteomic analysis of Potentilla fruticosa L. leaves by iTRAQ reveals responses to heat stress
High temperature is an important environmental factor that affects plant growth and crop yield. Potentilla fruticosa L. has a developed root system and characteristics of resistance to several stresses (e.g., high temperature, cold, drought) that are shared by native shrubs in the north and west of...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5568749/ https://www.ncbi.nlm.nih.gov/pubmed/28829780 http://dx.doi.org/10.1371/journal.pone.0182917 |
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author | Guo, Yingtian Wang, Zhi Guan, Xuelian Hu, Zenghui Zhang, Ze Zheng, Jian Lu, Yizeng |
author_facet | Guo, Yingtian Wang, Zhi Guan, Xuelian Hu, Zenghui Zhang, Ze Zheng, Jian Lu, Yizeng |
author_sort | Guo, Yingtian |
collection | PubMed |
description | High temperature is an important environmental factor that affects plant growth and crop yield. Potentilla fruticosa L. has a developed root system and characteristics of resistance to several stresses (e.g., high temperature, cold, drought) that are shared by native shrubs in the north and west of China. To investigate thermotolerance mechanisms in P. fruticosa, 3-year-old plants were subjected to a high temperature of 42°C for 1, 2, and 3 days respectively before analysis. Then, we studied changes in cell ultrastructure using electron microscopy and investigated physiological changes in the leaves of P. fruticosa. Additionally, we used isobaric tags for relative and absolute quantification (iTRAQ) coupled with liquid chromatography-tandem mass spectrometry (LC-MS/MS) to study proteomic changes in P. fruticosa leaves after 3 d of 42°C heat stress. we found that the cell membrane and structure of chloroplasts, especially the thylakoids in P. fruticosa leaves, was destroyed by a high temperature stress, which might affect the photosynthesis in this species. We identified 35 up-regulated and 23 down-regulated proteins after the heat treatment. Gene Ontology (GO) analysis indicated that these 58 differentially abundant proteins were involved mainly in protein synthesis, protein folding and degradation, abiotic stress defense, photosynthesis, RNA process, signal transduction, and other functions. The 58 proteins fell into different categories based on their subcellular localization mainly in the chloroplast envelope, cytoplasm, nucleus, cytosol, chloroplast, mitochondrion and cell membrane. Five proteins were selected for analysis at the mRNA level; this analysis showed that gene transcription levels were not completely consistent with protein abundance. These results provide valuable information for Potentilla thermotolerance breeding. |
format | Online Article Text |
id | pubmed-5568749 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-55687492017-09-09 Proteomic analysis of Potentilla fruticosa L. leaves by iTRAQ reveals responses to heat stress Guo, Yingtian Wang, Zhi Guan, Xuelian Hu, Zenghui Zhang, Ze Zheng, Jian Lu, Yizeng PLoS One Research Article High temperature is an important environmental factor that affects plant growth and crop yield. Potentilla fruticosa L. has a developed root system and characteristics of resistance to several stresses (e.g., high temperature, cold, drought) that are shared by native shrubs in the north and west of China. To investigate thermotolerance mechanisms in P. fruticosa, 3-year-old plants were subjected to a high temperature of 42°C for 1, 2, and 3 days respectively before analysis. Then, we studied changes in cell ultrastructure using electron microscopy and investigated physiological changes in the leaves of P. fruticosa. Additionally, we used isobaric tags for relative and absolute quantification (iTRAQ) coupled with liquid chromatography-tandem mass spectrometry (LC-MS/MS) to study proteomic changes in P. fruticosa leaves after 3 d of 42°C heat stress. we found that the cell membrane and structure of chloroplasts, especially the thylakoids in P. fruticosa leaves, was destroyed by a high temperature stress, which might affect the photosynthesis in this species. We identified 35 up-regulated and 23 down-regulated proteins after the heat treatment. Gene Ontology (GO) analysis indicated that these 58 differentially abundant proteins were involved mainly in protein synthesis, protein folding and degradation, abiotic stress defense, photosynthesis, RNA process, signal transduction, and other functions. The 58 proteins fell into different categories based on their subcellular localization mainly in the chloroplast envelope, cytoplasm, nucleus, cytosol, chloroplast, mitochondrion and cell membrane. Five proteins were selected for analysis at the mRNA level; this analysis showed that gene transcription levels were not completely consistent with protein abundance. These results provide valuable information for Potentilla thermotolerance breeding. Public Library of Science 2017-08-22 /pmc/articles/PMC5568749/ /pubmed/28829780 http://dx.doi.org/10.1371/journal.pone.0182917 Text en © 2017 Guo et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Guo, Yingtian Wang, Zhi Guan, Xuelian Hu, Zenghui Zhang, Ze Zheng, Jian Lu, Yizeng Proteomic analysis of Potentilla fruticosa L. leaves by iTRAQ reveals responses to heat stress |
title | Proteomic analysis of Potentilla fruticosa L. leaves by iTRAQ reveals responses to heat stress |
title_full | Proteomic analysis of Potentilla fruticosa L. leaves by iTRAQ reveals responses to heat stress |
title_fullStr | Proteomic analysis of Potentilla fruticosa L. leaves by iTRAQ reveals responses to heat stress |
title_full_unstemmed | Proteomic analysis of Potentilla fruticosa L. leaves by iTRAQ reveals responses to heat stress |
title_short | Proteomic analysis of Potentilla fruticosa L. leaves by iTRAQ reveals responses to heat stress |
title_sort | proteomic analysis of potentilla fruticosa l. leaves by itraq reveals responses to heat stress |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5568749/ https://www.ncbi.nlm.nih.gov/pubmed/28829780 http://dx.doi.org/10.1371/journal.pone.0182917 |
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