Proteomic analysis of salt-responsive proteins in the leaves of mangrove Kandelia candel during short-term stress.

Salt stress is a major abiotic stress that limits crop productivity in many regions of the world. A comparative proteomic approach to identify salt stress-responsive proteins and to understand the molecular mechanisms was carried out in the woody halophyte Kandelia candel. Four-leaf-old K. candel se...

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Main Authors: Lingxia Wang, Xiao Liu, Meng Liang, Fanglin Tan, Wenyu Liang, Yiyong Chen, Yongxiang Lin, Li Huang, Jianhong Xing, Wei Chen
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2014-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3885408?pdf=render
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spelling doaj-61c2df027f644798b4e918f353088d9d2020-11-25T01:17:25ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-0191e8314110.1371/journal.pone.0083141Proteomic analysis of salt-responsive proteins in the leaves of mangrove Kandelia candel during short-term stress.Lingxia WangXiao LiuMeng LiangFanglin TanWenyu LiangYiyong ChenYongxiang LinLi HuangJianhong XingWei ChenSalt stress is a major abiotic stress that limits crop productivity in many regions of the world. A comparative proteomic approach to identify salt stress-responsive proteins and to understand the molecular mechanisms was carried out in the woody halophyte Kandelia candel. Four-leaf-old K. candel seedlings were exposed to 150 (control), 300, 450, and 600 mM NaCl for 3 days. Proteins extracted from the leaves of K. candel seedlings were separated by two-dimensional gel electrophoresis (2-DE). More than 900 protein spots were detected on each gel, and 53 differentially expressed protein spots were located with at least two-fold differences in abundance on 2-DE maps, of which 48 were identified by matrix-assisted laser desorption ionization time-of-flight/time-of-flight mass spectrometry (MALDI-TOF-TOF/MS). The results showed that K. candel could withstand up to 450 mM NaCl stress by up-regulating proteins that are mainly involved in photosynthesis, respiration and energy metabolism, Na(+) compartmentalization, protein folding and assembly, and signal transduction. Physiological data, including superoxide dismutase (SOD) and dehydroascorbate reductase (DHAR) activities, hydrogen peroxide (H2O2) and superoxide anion radicals (O2(-)) contents, as well as Na(+) content and K(+)/Na(+) ratios all correlated well with our proteomic results. This study provides new global insights into woody halophyte salt stress responses. Identification of differentially expressed proteins promotes better understanding of the molecular basis for salt stress reduction in K. candel.http://europepmc.org/articles/PMC3885408?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Lingxia Wang
Xiao Liu
Meng Liang
Fanglin Tan
Wenyu Liang
Yiyong Chen
Yongxiang Lin
Li Huang
Jianhong Xing
Wei Chen
spellingShingle Lingxia Wang
Xiao Liu
Meng Liang
Fanglin Tan
Wenyu Liang
Yiyong Chen
Yongxiang Lin
Li Huang
Jianhong Xing
Wei Chen
Proteomic analysis of salt-responsive proteins in the leaves of mangrove Kandelia candel during short-term stress.
PLoS ONE
author_facet Lingxia Wang
Xiao Liu
Meng Liang
Fanglin Tan
Wenyu Liang
Yiyong Chen
Yongxiang Lin
Li Huang
Jianhong Xing
Wei Chen
author_sort Lingxia Wang
title Proteomic analysis of salt-responsive proteins in the leaves of mangrove Kandelia candel during short-term stress.
title_short Proteomic analysis of salt-responsive proteins in the leaves of mangrove Kandelia candel during short-term stress.
title_full Proteomic analysis of salt-responsive proteins in the leaves of mangrove Kandelia candel during short-term stress.
title_fullStr Proteomic analysis of salt-responsive proteins in the leaves of mangrove Kandelia candel during short-term stress.
title_full_unstemmed Proteomic analysis of salt-responsive proteins in the leaves of mangrove Kandelia candel during short-term stress.
title_sort proteomic analysis of salt-responsive proteins in the leaves of mangrove kandelia candel during short-term stress.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2014-01-01
description Salt stress is a major abiotic stress that limits crop productivity in many regions of the world. A comparative proteomic approach to identify salt stress-responsive proteins and to understand the molecular mechanisms was carried out in the woody halophyte Kandelia candel. Four-leaf-old K. candel seedlings were exposed to 150 (control), 300, 450, and 600 mM NaCl for 3 days. Proteins extracted from the leaves of K. candel seedlings were separated by two-dimensional gel electrophoresis (2-DE). More than 900 protein spots were detected on each gel, and 53 differentially expressed protein spots were located with at least two-fold differences in abundance on 2-DE maps, of which 48 were identified by matrix-assisted laser desorption ionization time-of-flight/time-of-flight mass spectrometry (MALDI-TOF-TOF/MS). The results showed that K. candel could withstand up to 450 mM NaCl stress by up-regulating proteins that are mainly involved in photosynthesis, respiration and energy metabolism, Na(+) compartmentalization, protein folding and assembly, and signal transduction. Physiological data, including superoxide dismutase (SOD) and dehydroascorbate reductase (DHAR) activities, hydrogen peroxide (H2O2) and superoxide anion radicals (O2(-)) contents, as well as Na(+) content and K(+)/Na(+) ratios all correlated well with our proteomic results. This study provides new global insights into woody halophyte salt stress responses. Identification of differentially expressed proteins promotes better understanding of the molecular basis for salt stress reduction in K. candel.
url http://europepmc.org/articles/PMC3885408?pdf=render
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