Evolutionary Adaptation of Protein Turnover in White Muscle of Stenothermal Antarctic Fish: Elevated Cold Compensation at Reduced Thermal Responsiveness
Protein turnover is highly energy consuming and overall relates to an organism’s growth performance varying largely between species, e.g., due to pre-adaptation to environmental characteristics such as temperature. Here, we determined protein synthesis rates and capacity of protein degradation in wh...
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2023
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Online Access: | https://epic.awi.de/id/eprint/58903/ https://epic.awi.de/id/eprint/58903/1/Evolutionary%20Adaptation%20of%20Protein%20Turnover%20in%20White%20Muscle%20of%20Stenothermal%20Antarctic%20Fish%20Elevated%20Cold%20Compensation%20at%20Red.pdf https://doi.org/10.3390/biom13101507 https://hdl.handle.net/10013/epic.d51081f1-5d25-45df-8606-2a5ea0180110 |
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ftawi:oai:epic.awi.de:58903 2024-09-15T17:48:14+00:00 Evolutionary Adaptation of Protein Turnover in White Muscle of Stenothermal Antarctic Fish: Elevated Cold Compensation at Reduced Thermal Responsiveness Krebs, Nina Bock, Christian Tebben, Jan Mark, Felix C Lucassen, Magnus Lannig, Gisela Pörtner, Hans-Otto 2023-10-01 application/pdf https://epic.awi.de/id/eprint/58903/ https://epic.awi.de/id/eprint/58903/1/Evolutionary%20Adaptation%20of%20Protein%20Turnover%20in%20White%20Muscle%20of%20Stenothermal%20Antarctic%20Fish%20Elevated%20Cold%20Compensation%20at%20Red.pdf https://doi.org/10.3390/biom13101507 https://hdl.handle.net/10013/epic.d51081f1-5d25-45df-8606-2a5ea0180110 unknown MDPI https://epic.awi.de/id/eprint/58903/1/Evolutionary%20Adaptation%20of%20Protein%20Turnover%20in%20White%20Muscle%20of%20Stenothermal%20Antarctic%20Fish%20Elevated%20Cold%20Compensation%20at%20Red.pdf Krebs, N. , Bock, C. orcid:0000-0003-0052-3090 , Tebben, J. orcid:0000-0002-2780-2236 , Mark, F. C. orcid:0000-0002-5586-6704 , Lucassen, M. orcid:0000-0003-4276-4781 , Lannig, G. orcid:0000-0002-9210-256X and Pörtner, H. O. orcid:0000-0001-6535-6575 (2023) Evolutionary Adaptation of Protein Turnover in White Muscle of Stenothermal Antarctic Fish: Elevated Cold Compensation at Reduced Thermal Responsiveness , Biomolecules, 13 (10), p. 1507 . doi:10.3390/biom13101507 <https://doi.org/10.3390/biom13101507> , hdl:10013/epic.d51081f1-5d25-45df-8606-2a5ea0180110 EPIC3Biomolecules, MDPI, 13(10), pp. 1507-1507, ISSN: 2218-273X Article isiRev 2023 ftawi https://doi.org/10.3390/biom13101507 2024-08-05T14:05:59Z Protein turnover is highly energy consuming and overall relates to an organism’s growth performance varying largely between species, e.g., due to pre-adaptation to environmental characteristics such as temperature. Here, we determined protein synthesis rates and capacity of protein degradation in white muscle of the cold stenothermal Antarctic eelpout (Pachycara brachycephalum) and its closely related temperate counterpart, the eurythermal common eelpout (Zoarces viviparus). Both species were exposed to acute warming (P. brachycephalum, 0 °C + 2 °C day−1; Z. viviparus, 4 °C + 3 °C day−1). The in vivo protein synthesis rate (Ks) was monitored after injection of 13C-phenylalanine, and protein degradation capacity was quantified by measuring the activity of cathepsin D in vitro. Untargeted metabolic profiling by nuclear magnetic resonance (NMR) spectroscopy was used to identify the metabolic processes involved. Independent of temperature, the protein synthesis rate was higher in P. brachycephalum (Ks = 0.38–0.614 % day−1) than in Z. viviparus (Ks= 0.148–0.379% day−1). Whereas protein synthesis remained unaffected by temperature in the Antarctic species, protein synthesis in Z. viviparus increased to near the thermal optimum (16 °C) and tended to fall at higher temperatures. Most strikingly, capacities for protein degradation were about ten times higher in the Antarctic compared to the temperate species. These differences are mirrored in the metabolic profiles, with significantly higher levels of complex and essential amino acids in the free cytosolic pool of the Antarctic congener. Together, the results clearly indicate a highly cold-compensated protein turnover in the Antarctic eelpout compared to its temperate confamilial. Constant versus variable environments are mirrored in rigid versus plastic functional responses of the protein synthesis machinery. Article in Journal/Newspaper Antarc* Antarctic Alfred Wegener Institute for Polar- and Marine Research (AWI): ePIC (electronic Publication Information Center) Biomolecules 13 10 1507 |
institution |
Open Polar |
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Alfred Wegener Institute for Polar- and Marine Research (AWI): ePIC (electronic Publication Information Center) |
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ftawi |
language |
unknown |
description |
Protein turnover is highly energy consuming and overall relates to an organism’s growth performance varying largely between species, e.g., due to pre-adaptation to environmental characteristics such as temperature. Here, we determined protein synthesis rates and capacity of protein degradation in white muscle of the cold stenothermal Antarctic eelpout (Pachycara brachycephalum) and its closely related temperate counterpart, the eurythermal common eelpout (Zoarces viviparus). Both species were exposed to acute warming (P. brachycephalum, 0 °C + 2 °C day−1; Z. viviparus, 4 °C + 3 °C day−1). The in vivo protein synthesis rate (Ks) was monitored after injection of 13C-phenylalanine, and protein degradation capacity was quantified by measuring the activity of cathepsin D in vitro. Untargeted metabolic profiling by nuclear magnetic resonance (NMR) spectroscopy was used to identify the metabolic processes involved. Independent of temperature, the protein synthesis rate was higher in P. brachycephalum (Ks = 0.38–0.614 % day−1) than in Z. viviparus (Ks= 0.148–0.379% day−1). Whereas protein synthesis remained unaffected by temperature in the Antarctic species, protein synthesis in Z. viviparus increased to near the thermal optimum (16 °C) and tended to fall at higher temperatures. Most strikingly, capacities for protein degradation were about ten times higher in the Antarctic compared to the temperate species. These differences are mirrored in the metabolic profiles, with significantly higher levels of complex and essential amino acids in the free cytosolic pool of the Antarctic congener. Together, the results clearly indicate a highly cold-compensated protein turnover in the Antarctic eelpout compared to its temperate confamilial. Constant versus variable environments are mirrored in rigid versus plastic functional responses of the protein synthesis machinery. |
format |
Article in Journal/Newspaper |
author |
Krebs, Nina Bock, Christian Tebben, Jan Mark, Felix C Lucassen, Magnus Lannig, Gisela Pörtner, Hans-Otto |
spellingShingle |
Krebs, Nina Bock, Christian Tebben, Jan Mark, Felix C Lucassen, Magnus Lannig, Gisela Pörtner, Hans-Otto Evolutionary Adaptation of Protein Turnover in White Muscle of Stenothermal Antarctic Fish: Elevated Cold Compensation at Reduced Thermal Responsiveness |
author_facet |
Krebs, Nina Bock, Christian Tebben, Jan Mark, Felix C Lucassen, Magnus Lannig, Gisela Pörtner, Hans-Otto |
author_sort |
Krebs, Nina |
title |
Evolutionary Adaptation of Protein Turnover in White Muscle of Stenothermal Antarctic Fish: Elevated Cold Compensation at Reduced Thermal Responsiveness |
title_short |
Evolutionary Adaptation of Protein Turnover in White Muscle of Stenothermal Antarctic Fish: Elevated Cold Compensation at Reduced Thermal Responsiveness |
title_full |
Evolutionary Adaptation of Protein Turnover in White Muscle of Stenothermal Antarctic Fish: Elevated Cold Compensation at Reduced Thermal Responsiveness |
title_fullStr |
Evolutionary Adaptation of Protein Turnover in White Muscle of Stenothermal Antarctic Fish: Elevated Cold Compensation at Reduced Thermal Responsiveness |
title_full_unstemmed |
Evolutionary Adaptation of Protein Turnover in White Muscle of Stenothermal Antarctic Fish: Elevated Cold Compensation at Reduced Thermal Responsiveness |
title_sort |
evolutionary adaptation of protein turnover in white muscle of stenothermal antarctic fish: elevated cold compensation at reduced thermal responsiveness |
publisher |
MDPI |
publishDate |
2023 |
url |
https://epic.awi.de/id/eprint/58903/ https://epic.awi.de/id/eprint/58903/1/Evolutionary%20Adaptation%20of%20Protein%20Turnover%20in%20White%20Muscle%20of%20Stenothermal%20Antarctic%20Fish%20Elevated%20Cold%20Compensation%20at%20Red.pdf https://doi.org/10.3390/biom13101507 https://hdl.handle.net/10013/epic.d51081f1-5d25-45df-8606-2a5ea0180110 |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
EPIC3Biomolecules, MDPI, 13(10), pp. 1507-1507, ISSN: 2218-273X |
op_relation |
https://epic.awi.de/id/eprint/58903/1/Evolutionary%20Adaptation%20of%20Protein%20Turnover%20in%20White%20Muscle%20of%20Stenothermal%20Antarctic%20Fish%20Elevated%20Cold%20Compensation%20at%20Red.pdf Krebs, N. , Bock, C. orcid:0000-0003-0052-3090 , Tebben, J. orcid:0000-0002-2780-2236 , Mark, F. C. orcid:0000-0002-5586-6704 , Lucassen, M. orcid:0000-0003-4276-4781 , Lannig, G. orcid:0000-0002-9210-256X and Pörtner, H. O. orcid:0000-0001-6535-6575 (2023) Evolutionary Adaptation of Protein Turnover in White Muscle of Stenothermal Antarctic Fish: Elevated Cold Compensation at Reduced Thermal Responsiveness , Biomolecules, 13 (10), p. 1507 . doi:10.3390/biom13101507 <https://doi.org/10.3390/biom13101507> , hdl:10013/epic.d51081f1-5d25-45df-8606-2a5ea0180110 |
op_doi |
https://doi.org/10.3390/biom13101507 |
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Biomolecules |
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13 |
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10 |
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1507 |
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1810289389265223680 |