Physiological adaptation of an Antarctic Na+/K+-ATPase to the cold

Because enzymatic activity is strongly suppressed by the cold, polar poikilotherms face significant adaptive challenges. For example, at 0°C the catalytic activity of a typical enzyme from a temperate organism is reduced by more than 90%. Enzymes embedded in the plasma membrane, such as the Na+/K+-A...

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Published in:Journal of Experimental Biology
Main Authors: Galarza-Muñoz, Gaddiel, Soto-Morales, Sonia I., Holmgren, Miguel, Rosenthal, Joshua J. C.
Format: Text
Language:English
Published: Company of Biologists 2011
Subjects:
Online Access:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3110501
http://www.ncbi.nlm.nih.gov/pubmed/21653810
https://doi.org/10.1242/jeb.048744
id ftpubmed:oai:pubmedcentral.nih.gov:3110501
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spelling ftpubmed:oai:pubmedcentral.nih.gov:3110501 2023-05-15T13:35:52+02:00 Physiological adaptation of an Antarctic Na+/K+-ATPase to the cold Galarza-Muñoz, Gaddiel Soto-Morales, Sonia I. Holmgren, Miguel Rosenthal, Joshua J. C. 2011-07-01 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3110501 http://www.ncbi.nlm.nih.gov/pubmed/21653810 https://doi.org/10.1242/jeb.048744 en eng Company of Biologists http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3110501 http://www.ncbi.nlm.nih.gov/pubmed/21653810 http://dx.doi.org/10.1242/jeb.048744 © 2011. Research Articles Text 2011 ftpubmed https://doi.org/10.1242/jeb.048744 2013-09-03T15:41:12Z Because enzymatic activity is strongly suppressed by the cold, polar poikilotherms face significant adaptive challenges. For example, at 0°C the catalytic activity of a typical enzyme from a temperate organism is reduced by more than 90%. Enzymes embedded in the plasma membrane, such as the Na+/K+-ATPase, may be even more susceptible to the cold because of thermal effects on the lipid bilayer. Accordingly, adaptive changes in response to the cold may include adjustments to the enzyme or the surrounding lipid environment, or synergistic changes to both. To assess the contribution of the enzyme itself, we cloned orthologous Na+/K+-ATPase α-subunits from an Antarctic (Pareledone sp.; –1.8°C) and a temperate octopus (Octopus bimaculatus; ∼18°C), and compared their turnover rates and temperature sensitivities in a heterologous expression system. The primary sequences of the two pumps were found to be highly similar (97% identity), with most differences being conservative changes involving hydrophobic residues. The physiology of the pumps was studied using an electrophysiological approach in intact Xenopus oocytes. The voltage dependence of the pumps was equivalent. However, at room temperature the maximum turnover rate of the Antarctic pump was found to be 25% higher than that of the temperate pump. In addition, the Antarctic pump exhibited a lower temperature sensitivity, leading to significantly higher relative activity at lower temperatures. Orthologous Na+/K+ pumps were then isolated from two tropical and two Arctic octopus. The temperature sensitivities of these pumps closely matched those of the temperate and Antarctic pumps, respectively. Thus, reduced thermal sensitivity appears to be a common mechanism driving cold adaptation in the Na+/K+-ATPase. Text Antarc* Antarctic Arctic PubMed Central (PMC) Antarctic Arctic The Antarctic Journal of Experimental Biology 214 13 2164 2174
institution Open Polar
collection PubMed Central (PMC)
op_collection_id ftpubmed
language English
topic Research Articles
spellingShingle Research Articles
Galarza-Muñoz, Gaddiel
Soto-Morales, Sonia I.
Holmgren, Miguel
Rosenthal, Joshua J. C.
Physiological adaptation of an Antarctic Na+/K+-ATPase to the cold
topic_facet Research Articles
description Because enzymatic activity is strongly suppressed by the cold, polar poikilotherms face significant adaptive challenges. For example, at 0°C the catalytic activity of a typical enzyme from a temperate organism is reduced by more than 90%. Enzymes embedded in the plasma membrane, such as the Na+/K+-ATPase, may be even more susceptible to the cold because of thermal effects on the lipid bilayer. Accordingly, adaptive changes in response to the cold may include adjustments to the enzyme or the surrounding lipid environment, or synergistic changes to both. To assess the contribution of the enzyme itself, we cloned orthologous Na+/K+-ATPase α-subunits from an Antarctic (Pareledone sp.; –1.8°C) and a temperate octopus (Octopus bimaculatus; ∼18°C), and compared their turnover rates and temperature sensitivities in a heterologous expression system. The primary sequences of the two pumps were found to be highly similar (97% identity), with most differences being conservative changes involving hydrophobic residues. The physiology of the pumps was studied using an electrophysiological approach in intact Xenopus oocytes. The voltage dependence of the pumps was equivalent. However, at room temperature the maximum turnover rate of the Antarctic pump was found to be 25% higher than that of the temperate pump. In addition, the Antarctic pump exhibited a lower temperature sensitivity, leading to significantly higher relative activity at lower temperatures. Orthologous Na+/K+ pumps were then isolated from two tropical and two Arctic octopus. The temperature sensitivities of these pumps closely matched those of the temperate and Antarctic pumps, respectively. Thus, reduced thermal sensitivity appears to be a common mechanism driving cold adaptation in the Na+/K+-ATPase.
format Text
author Galarza-Muñoz, Gaddiel
Soto-Morales, Sonia I.
Holmgren, Miguel
Rosenthal, Joshua J. C.
author_facet Galarza-Muñoz, Gaddiel
Soto-Morales, Sonia I.
Holmgren, Miguel
Rosenthal, Joshua J. C.
author_sort Galarza-Muñoz, Gaddiel
title Physiological adaptation of an Antarctic Na+/K+-ATPase to the cold
title_short Physiological adaptation of an Antarctic Na+/K+-ATPase to the cold
title_full Physiological adaptation of an Antarctic Na+/K+-ATPase to the cold
title_fullStr Physiological adaptation of an Antarctic Na+/K+-ATPase to the cold
title_full_unstemmed Physiological adaptation of an Antarctic Na+/K+-ATPase to the cold
title_sort physiological adaptation of an antarctic na+/k+-atpase to the cold
publisher Company of Biologists
publishDate 2011
url http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3110501
http://www.ncbi.nlm.nih.gov/pubmed/21653810
https://doi.org/10.1242/jeb.048744
geographic Antarctic
Arctic
The Antarctic
geographic_facet Antarctic
Arctic
The Antarctic
genre Antarc*
Antarctic
Arctic
genre_facet Antarc*
Antarctic
Arctic
op_relation http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3110501
http://www.ncbi.nlm.nih.gov/pubmed/21653810
http://dx.doi.org/10.1242/jeb.048744
op_rights © 2011.
op_doi https://doi.org/10.1242/jeb.048744
container_title Journal of Experimental Biology
container_volume 214
container_issue 13
container_start_page 2164
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