Thermotolerance and molecular chaperone function of an SGT1-like protein from the psychrophilic yeast, Glaciozyma antarctica
The ability of eukaryotes to adapt to an extreme range of temperatures is critically important for survival. Although adaptation to extreme high temperatures is well understood, reflecting the action of molecular chaperones, it is unclear whether these molecules play a role in survival at extremely...
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ftpubmed:oai:pubmedcentral.nih.gov:4908002 2023-05-15T13:31:04+02:00 Thermotolerance and molecular chaperone function of an SGT1-like protein from the psychrophilic yeast, Glaciozyma antarctica Yusof, Nur Athirah Hashim, Noor Haza Fazlin Beddoe, Travis Mahadi, Nor Muhammad Illias, Rosli Md Bakar, Farah Diba Abu Murad, Abdul Munir Abdul 2016-05-06 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4908002/ http://www.ncbi.nlm.nih.gov/pubmed/27154490 https://doi.org/10.1007/s12192-016-0696-2 en eng Springer Netherlands http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4908002/ http://www.ncbi.nlm.nih.gov/pubmed/27154490 http://dx.doi.org/10.1007/s12192-016-0696-2 © Cell Stress Society International 2016 Original Paper Text 2016 ftpubmed https://doi.org/10.1007/s12192-016-0696-2 2017-01-08T01:15:17Z The ability of eukaryotes to adapt to an extreme range of temperatures is critically important for survival. Although adaptation to extreme high temperatures is well understood, reflecting the action of molecular chaperones, it is unclear whether these molecules play a role in survival at extremely low temperatures. The recent genome sequencing of the yeast Glaciozyma antarctica, isolated from Antarctic sea ice near Casey Station, provides an opportunity to investigate the role of molecular chaperones in adaptation to cold temperatures. We isolated a G. antarctica homologue of small heat shock protein 20 (HSP20), GaSGT1, and observed that the GaSGT1 mRNA expression in G. antarctica was markedly increased following culture exposure at low temperatures. Additionally, we demonstrated that GaSGT1 overexpression in Escherichia coli protected these bacteria from exposure to both high and low temperatures, which are lethal for growth. The recombinant GaSGT1 retained up to 60 % of its native luciferase activity after exposure to luciferase-denaturing temperatures. These results suggest that GaSGT1 promotes cell thermotolerance and employs molecular chaperone-like activity toward temperature assaults. Text Antarc* Antarctic Antarctica Sea ice PubMed Central (PMC) Antarctic Casey Station ENVELOPE(110.528,110.528,-66.282,-66.282) Cell Stress and Chaperones 21 4 707 715 |
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Original Paper Yusof, Nur Athirah Hashim, Noor Haza Fazlin Beddoe, Travis Mahadi, Nor Muhammad Illias, Rosli Md Bakar, Farah Diba Abu Murad, Abdul Munir Abdul Thermotolerance and molecular chaperone function of an SGT1-like protein from the psychrophilic yeast, Glaciozyma antarctica |
topic_facet |
Original Paper |
description |
The ability of eukaryotes to adapt to an extreme range of temperatures is critically important for survival. Although adaptation to extreme high temperatures is well understood, reflecting the action of molecular chaperones, it is unclear whether these molecules play a role in survival at extremely low temperatures. The recent genome sequencing of the yeast Glaciozyma antarctica, isolated from Antarctic sea ice near Casey Station, provides an opportunity to investigate the role of molecular chaperones in adaptation to cold temperatures. We isolated a G. antarctica homologue of small heat shock protein 20 (HSP20), GaSGT1, and observed that the GaSGT1 mRNA expression in G. antarctica was markedly increased following culture exposure at low temperatures. Additionally, we demonstrated that GaSGT1 overexpression in Escherichia coli protected these bacteria from exposure to both high and low temperatures, which are lethal for growth. The recombinant GaSGT1 retained up to 60 % of its native luciferase activity after exposure to luciferase-denaturing temperatures. These results suggest that GaSGT1 promotes cell thermotolerance and employs molecular chaperone-like activity toward temperature assaults. |
format |
Text |
author |
Yusof, Nur Athirah Hashim, Noor Haza Fazlin Beddoe, Travis Mahadi, Nor Muhammad Illias, Rosli Md Bakar, Farah Diba Abu Murad, Abdul Munir Abdul |
author_facet |
Yusof, Nur Athirah Hashim, Noor Haza Fazlin Beddoe, Travis Mahadi, Nor Muhammad Illias, Rosli Md Bakar, Farah Diba Abu Murad, Abdul Munir Abdul |
author_sort |
Yusof, Nur Athirah |
title |
Thermotolerance and molecular chaperone function of an SGT1-like protein from the psychrophilic yeast, Glaciozyma antarctica |
title_short |
Thermotolerance and molecular chaperone function of an SGT1-like protein from the psychrophilic yeast, Glaciozyma antarctica |
title_full |
Thermotolerance and molecular chaperone function of an SGT1-like protein from the psychrophilic yeast, Glaciozyma antarctica |
title_fullStr |
Thermotolerance and molecular chaperone function of an SGT1-like protein from the psychrophilic yeast, Glaciozyma antarctica |
title_full_unstemmed |
Thermotolerance and molecular chaperone function of an SGT1-like protein from the psychrophilic yeast, Glaciozyma antarctica |
title_sort |
thermotolerance and molecular chaperone function of an sgt1-like protein from the psychrophilic yeast, glaciozyma antarctica |
publisher |
Springer Netherlands |
publishDate |
2016 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4908002/ http://www.ncbi.nlm.nih.gov/pubmed/27154490 https://doi.org/10.1007/s12192-016-0696-2 |
long_lat |
ENVELOPE(110.528,110.528,-66.282,-66.282) |
geographic |
Antarctic Casey Station |
geographic_facet |
Antarctic Casey Station |
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Antarc* Antarctic Antarctica Sea ice |
genre_facet |
Antarc* Antarctic Antarctica Sea ice |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4908002/ http://www.ncbi.nlm.nih.gov/pubmed/27154490 http://dx.doi.org/10.1007/s12192-016-0696-2 |
op_rights |
© Cell Stress Society International 2016 |
op_doi |
https://doi.org/10.1007/s12192-016-0696-2 |
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Cell Stress and Chaperones |
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21 |
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4 |
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1766015795683393536 |