Temperature differentially affects adenosine triphosphatase activity in Hsc70 orthologs from Antarctic and New Zealand notothenioid fishes
To test the temperature sensitivity of molecular chaperones in poikilothermic animals, we purified the molecular chaperone Hsc70 from 2 closely related notothenioid fishes—the Antarctic species Trematomus bernacchii and the temperate New Zealand species Notothenia angustata—and characterized the eff...
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Online Access: | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1176469 http://www.ncbi.nlm.nih.gov/pubmed/16038407 https://doi.org/10.1379/CSC-82R.1 |
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ftpubmed:oai:pubmedcentral.nih.gov:1176469 2023-05-15T13:45:33+02:00 Temperature differentially affects adenosine triphosphatase activity in Hsc70 orthologs from Antarctic and New Zealand notothenioid fishes Place, Sean P. Hofmann, Gretchen E. 2005-06 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1176469 http://www.ncbi.nlm.nih.gov/pubmed/16038407 https://doi.org/10.1379/CSC-82R.1 en eng Cell Stress Society International http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1176469 http://www.ncbi.nlm.nih.gov/pubmed/16038407 http://dx.doi.org/10.1379/CSC-82R.1 Copyright © 2005, Cell Stress Society International Original Articles Text 2005 ftpubmed https://doi.org/10.1379/CSC-82R.1 2013-08-30T11:52:49Z To test the temperature sensitivity of molecular chaperones in poikilothermic animals, we purified the molecular chaperone Hsc70 from 2 closely related notothenioid fishes—the Antarctic species Trematomus bernacchii and the temperate New Zealand species Notothenia angustata—and characterized the effect of temperature on Hsc70 adenosine triphosphatase (ATPase) activity. Hsc70 ATPase activity was measured using [α-32P]-adenosine triphosphate (ATP)–based in vitro assays followed by separation of adenylates by thin-layer chromatography. For both species, a significant increase in Hsc70 ATPase activity was observed across a range of temperatures that was ecologically relevant for each respective species. Hsc70 from T bernacchii hydrolyzed 2-fold more ATP than did N angustata Hsc70 at 0°C, suggesting that the Antarctic molecular chaperone may be adapted to function more efficiently at extreme cold temperatures. In addition, Q10 measurements indicate differential temperature sensitivity of the ATPase activity of Hsc70 from these differentially adapted fish that correlates with the temperature niche inhabited by each species. Hsc70 from T bernacchii was relatively temperature insensitive, as indicated by Q10 values calculated near 1.0 across each temperature range measured. In the case of Hsc70 purified from N angustata, Q10 values indicated thermal sensitivity across the temperature range of 0°C to 10°C, with a Q10 of 2.714. However, Hsc70 from both T bernacchii and N angustata exhibited unusually high thermal stabilities with ATPase activity at temperatures that far exceeded temperatures encountered by these fish in nature. Overall, as evidenced by in vitro ATP hydrolysis, Hsc70 from T bernacchii and N angustata displayed biochemical characteristics that were supportive of molecular chaperone function at ecologically relevant temperatures. Text Antarc* Antarctic PubMed Central (PMC) Antarctic New Zealand The Antarctic Cell Stress & Chaperones 10 2 104 |
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Original Articles Place, Sean P. Hofmann, Gretchen E. Temperature differentially affects adenosine triphosphatase activity in Hsc70 orthologs from Antarctic and New Zealand notothenioid fishes |
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Original Articles |
description |
To test the temperature sensitivity of molecular chaperones in poikilothermic animals, we purified the molecular chaperone Hsc70 from 2 closely related notothenioid fishes—the Antarctic species Trematomus bernacchii and the temperate New Zealand species Notothenia angustata—and characterized the effect of temperature on Hsc70 adenosine triphosphatase (ATPase) activity. Hsc70 ATPase activity was measured using [α-32P]-adenosine triphosphate (ATP)–based in vitro assays followed by separation of adenylates by thin-layer chromatography. For both species, a significant increase in Hsc70 ATPase activity was observed across a range of temperatures that was ecologically relevant for each respective species. Hsc70 from T bernacchii hydrolyzed 2-fold more ATP than did N angustata Hsc70 at 0°C, suggesting that the Antarctic molecular chaperone may be adapted to function more efficiently at extreme cold temperatures. In addition, Q10 measurements indicate differential temperature sensitivity of the ATPase activity of Hsc70 from these differentially adapted fish that correlates with the temperature niche inhabited by each species. Hsc70 from T bernacchii was relatively temperature insensitive, as indicated by Q10 values calculated near 1.0 across each temperature range measured. In the case of Hsc70 purified from N angustata, Q10 values indicated thermal sensitivity across the temperature range of 0°C to 10°C, with a Q10 of 2.714. However, Hsc70 from both T bernacchii and N angustata exhibited unusually high thermal stabilities with ATPase activity at temperatures that far exceeded temperatures encountered by these fish in nature. Overall, as evidenced by in vitro ATP hydrolysis, Hsc70 from T bernacchii and N angustata displayed biochemical characteristics that were supportive of molecular chaperone function at ecologically relevant temperatures. |
format |
Text |
author |
Place, Sean P. Hofmann, Gretchen E. |
author_facet |
Place, Sean P. Hofmann, Gretchen E. |
author_sort |
Place, Sean P. |
title |
Temperature differentially affects adenosine triphosphatase activity in Hsc70 orthologs from Antarctic and New Zealand notothenioid fishes |
title_short |
Temperature differentially affects adenosine triphosphatase activity in Hsc70 orthologs from Antarctic and New Zealand notothenioid fishes |
title_full |
Temperature differentially affects adenosine triphosphatase activity in Hsc70 orthologs from Antarctic and New Zealand notothenioid fishes |
title_fullStr |
Temperature differentially affects adenosine triphosphatase activity in Hsc70 orthologs from Antarctic and New Zealand notothenioid fishes |
title_full_unstemmed |
Temperature differentially affects adenosine triphosphatase activity in Hsc70 orthologs from Antarctic and New Zealand notothenioid fishes |
title_sort |
temperature differentially affects adenosine triphosphatase activity in hsc70 orthologs from antarctic and new zealand notothenioid fishes |
publisher |
Cell Stress Society International |
publishDate |
2005 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1176469 http://www.ncbi.nlm.nih.gov/pubmed/16038407 https://doi.org/10.1379/CSC-82R.1 |
geographic |
Antarctic New Zealand The Antarctic |
geographic_facet |
Antarctic New Zealand The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1176469 http://www.ncbi.nlm.nih.gov/pubmed/16038407 http://dx.doi.org/10.1379/CSC-82R.1 |
op_rights |
Copyright © 2005, Cell Stress Society International |
op_doi |
https://doi.org/10.1379/CSC-82R.1 |
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Cell Stress & Chaperones |
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10 |
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2 |
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104 |
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1766227269453348864 |