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Proteomic analysis of halotolerant proteins under high and low salt stress in Dunaliella salina using two-dimensional differential in-gel electrophoresis

Dunaliella salina, a single-celled marine alga with extreme salt tolerance, is an important model organism for studying fundamental extremophile survival mechanisms and their potential practical applications. In this study, two-dimensional differential in-gel electrophoresis (2D-DIGE) was used to in...

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Autores principales: Jia, Yan-Long, Chen, Hui, Zhang, Chong, Gao, Li-Jie, Wang, Xi-Cheng, Qiu, Le-Le, Wu, Jun-Fang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Sociedade Brasileira de Genética 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4910558/
https://www.ncbi.nlm.nih.gov/pubmed/27192131
http://dx.doi.org/10.1590/1678-4685-GMB-2015-0108
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author Jia, Yan-Long
Chen, Hui
Zhang, Chong
Gao, Li-Jie
Wang, Xi-Cheng
Qiu, Le-Le
Wu, Jun-Fang
author_facet Jia, Yan-Long
Chen, Hui
Zhang, Chong
Gao, Li-Jie
Wang, Xi-Cheng
Qiu, Le-Le
Wu, Jun-Fang
author_sort Jia, Yan-Long
collection PubMed
description Dunaliella salina, a single-celled marine alga with extreme salt tolerance, is an important model organism for studying fundamental extremophile survival mechanisms and their potential practical applications. In this study, two-dimensional differential in-gel electrophoresis (2D-DIGE) was used to investigate the expression of halotolerant proteins under high (3 M NaCl) and low (0.75 M NaCl) salt concentrations. Matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF/TOF MS) and bioinformatics were used to identify and characterize the differences among proteins. 2D-DIGE analysis revealed 141 protein spots that were significantly differentially expressed between the two salinities. Twenty-four differentially expressed protein spots were successfully identified by MALDI-TOF/TOF MS, including proteins in the following important categories: molecular chaperones, proteins involved in photosynthesis, proteins involved in respiration and proteins involved in amino acid synthesis. Expression levels of these proteins changed in response to the stress conditions, which suggests that they may be involved in the maintenance of intracellular osmotic pressure, cellular stress responses, physiological changes in metabolism, continuation of photosynthetic activity and other aspects of salt stress. The findings of this study enhance our understanding of the function and mechanisms of various proteins in salt stress.
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spelling pubmed-49105582016-07-01 Proteomic analysis of halotolerant proteins under high and low salt stress in Dunaliella salina using two-dimensional differential in-gel electrophoresis Jia, Yan-Long Chen, Hui Zhang, Chong Gao, Li-Jie Wang, Xi-Cheng Qiu, Le-Le Wu, Jun-Fang Genet Mol Biol Plant Genetics Dunaliella salina, a single-celled marine alga with extreme salt tolerance, is an important model organism for studying fundamental extremophile survival mechanisms and their potential practical applications. In this study, two-dimensional differential in-gel electrophoresis (2D-DIGE) was used to investigate the expression of halotolerant proteins under high (3 M NaCl) and low (0.75 M NaCl) salt concentrations. Matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF/TOF MS) and bioinformatics were used to identify and characterize the differences among proteins. 2D-DIGE analysis revealed 141 protein spots that were significantly differentially expressed between the two salinities. Twenty-four differentially expressed protein spots were successfully identified by MALDI-TOF/TOF MS, including proteins in the following important categories: molecular chaperones, proteins involved in photosynthesis, proteins involved in respiration and proteins involved in amino acid synthesis. Expression levels of these proteins changed in response to the stress conditions, which suggests that they may be involved in the maintenance of intracellular osmotic pressure, cellular stress responses, physiological changes in metabolism, continuation of photosynthetic activity and other aspects of salt stress. The findings of this study enhance our understanding of the function and mechanisms of various proteins in salt stress. Sociedade Brasileira de Genética 2016-05-13 2016 /pmc/articles/PMC4910558/ /pubmed/27192131 http://dx.doi.org/10.1590/1678-4685-GMB-2015-0108 Text en Copyright © 2016, Sociedade Brasileira de Genética. http://creativecommons.org/licenses/by/4.0/ License information: This is an open-access article distributed under the terms of the Creative Commons Attribution License (type CC-BY), which permits unrestricted use, distribution and reproduction in any medium, provided the original article is properly cited.
spellingShingle Plant Genetics
Jia, Yan-Long
Chen, Hui
Zhang, Chong
Gao, Li-Jie
Wang, Xi-Cheng
Qiu, Le-Le
Wu, Jun-Fang
Proteomic analysis of halotolerant proteins under high and low salt stress in Dunaliella salina using two-dimensional differential in-gel electrophoresis
title Proteomic analysis of halotolerant proteins under high and low salt stress in Dunaliella salina using two-dimensional differential in-gel electrophoresis
title_full Proteomic analysis of halotolerant proteins under high and low salt stress in Dunaliella salina using two-dimensional differential in-gel electrophoresis
title_fullStr Proteomic analysis of halotolerant proteins under high and low salt stress in Dunaliella salina using two-dimensional differential in-gel electrophoresis
title_full_unstemmed Proteomic analysis of halotolerant proteins under high and low salt stress in Dunaliella salina using two-dimensional differential in-gel electrophoresis
title_short Proteomic analysis of halotolerant proteins under high and low salt stress in Dunaliella salina using two-dimensional differential in-gel electrophoresis
title_sort proteomic analysis of halotolerant proteins under high and low salt stress in dunaliella salina using two-dimensional differential in-gel electrophoresis
topic Plant Genetics
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4910558/
https://www.ncbi.nlm.nih.gov/pubmed/27192131
http://dx.doi.org/10.1590/1678-4685-GMB-2015-0108
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