Source:http://linkedlifedata.com/resource/pubmed/id/21377541
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2011-4-25
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pubmed:abstractText |
The monogonont rotifer, Brachionus sp. has been regarded as a potential model for reproductive physiology, evolution, and environmental genomics. To uncover the role of the heat shock protein upon temperature stress and hydrogen peroxide (H?O?) exposure, we cloned heat shock protein 20 (Hsp20) and determined its modulatory response under different temperatures and H?O? concentrations. Under different temperature stresses (10 °C and 37 °C), the rotifer Brachionus sp. Hsp20 (Br-Hsp20) gene was highly expressed over time, and reached the maximum level 90 min after exposure, indicating that Br-Hsp20 gene would be involved in the chaperoning process to protect proteins at both low and high temperatures. To test the ability of thermotolerance of the recombinant Br-Hsp20-containing transformed Escherichia coli, we expressed the recombinant Br-Hsp20 protein with 1mM IPTG for 18 h at 30 °C, exposed them at 54 °C with time course (10 to 60 min), and measured cell survival. In this elevated temperature shock (54 °C), the cell survival was significantly higher at the Br-Hsp20 transformed E. coli, compared to the control (vector only). To analyze the modulatory effect of Br-Hsp20 gene on oxidative stress, we initially exposed 0.1 mM H?O? over time and measured antioxidant enzyme activities along with the expression level of Br-Hsp20 mRNA. Upon H?O? exposure, Br-Hsp20 gene was time-dependently upregulated and glutathione peroxidase (GPx), glutathione S-transferase (GST), and glutathione reductase (GR) activities were also elevated at the 12h-exposed group in a dose-dependent manner, indicating that the Br-Hsp20 gene would be an important gene in response to oxidative and temperature stress. Here, we demonstrated the role of the Hsp20 gene in the rotifer, Brachionus sp. providing a better understanding of the ecophysiology at environmental stress in this species.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Disulfide,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Peroxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Reductase,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/HSP20 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Helminth Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrogen Peroxide,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidants
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1532-0456
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pubmed:author | |
pubmed:copyrightInfo |
Copyright © 2011 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Print
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pubmed:volume |
154
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
19-27
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pubmed:meshHeading |
pubmed-meshheading:21377541-Amino Acid Sequence,
pubmed-meshheading:21377541-Animals,
pubmed-meshheading:21377541-Base Sequence,
pubmed-meshheading:21377541-Escherichia coli,
pubmed-meshheading:21377541-Gene Expression,
pubmed-meshheading:21377541-Glutathione,
pubmed-meshheading:21377541-Glutathione Disulfide,
pubmed-meshheading:21377541-Glutathione Peroxidase,
pubmed-meshheading:21377541-Glutathione Reductase,
pubmed-meshheading:21377541-Glutathione Transferase,
pubmed-meshheading:21377541-HSP20 Heat-Shock Proteins,
pubmed-meshheading:21377541-Helminth Proteins,
pubmed-meshheading:21377541-Hydrogen Peroxide,
pubmed-meshheading:21377541-Microbial Viability,
pubmed-meshheading:21377541-Molecular Sequence Data,
pubmed-meshheading:21377541-Oxidants,
pubmed-meshheading:21377541-Phylogeny,
pubmed-meshheading:21377541-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:21377541-Rotifera,
pubmed-meshheading:21377541-Sequence Homology, Amino Acid,
pubmed-meshheading:21377541-Stress, Physiological,
pubmed-meshheading:21377541-Temperature,
pubmed-meshheading:21377541-Transformation, Genetic
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pubmed:year |
2011
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pubmed:articleTitle |
Molecular and biochemical modulation of heat shock protein 20 (Hsp20) gene by temperature stress and hydrogen peroxide (H?O?) in the monogonont rotifer, Brachionus sp.
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pubmed:affiliation |
Department of Molecular and Environmental Bioscience, Graduate School, Hanyang University, Seoul 133-791, South Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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