Life in the freezer: protein metabolism in Antarctic fish

Whole-animal, in vivo protein metabolism rates have been reported in temperate and tropical, but not Antarctic fish. Growth in Antarctic species is generally slower than lower latitude species. Protein metabolism data for Antarctic invertebrates show low rates of protein synthesis and unusually high...

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Published in:Royal Society Open Science
Main Authors: Keiron P. P. Fraser, Lloyd S. Peck, Melody S. Clark, Andrew Clarke, Simeon L. Hill
Format: Article in Journal/Newspaper
Language:English
Published: The Royal Society 2022
Subjects:
Q
Online Access:https://doi.org/10.1098/rsos.211272
https://doaj.org/article/0f4b185df1d64fac865904baeda2a5a7
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spelling ftdoajarticles:oai:doaj.org/article:0f4b185df1d64fac865904baeda2a5a7 2023-05-15T13:54:34+02:00 Life in the freezer: protein metabolism in Antarctic fish Keiron P. P. Fraser Lloyd S. Peck Melody S. Clark Andrew Clarke Simeon L. Hill 2022-03-01T00:00:00Z https://doi.org/10.1098/rsos.211272 https://doaj.org/article/0f4b185df1d64fac865904baeda2a5a7 EN eng The Royal Society https://royalsocietypublishing.org/doi/10.1098/rsos.211272 https://doaj.org/toc/2054-5703 doi:10.1098/rsos.211272 2054-5703 https://doaj.org/article/0f4b185df1d64fac865904baeda2a5a7 Royal Society Open Science, Vol 9, Iss 3 (2022) protein turnover slow growth temperature limitation cryobiology Antarctic protein synthesis Science Q article 2022 ftdoajarticles https://doi.org/10.1098/rsos.211272 2022-12-31T15:33:00Z Whole-animal, in vivo protein metabolism rates have been reported in temperate and tropical, but not Antarctic fish. Growth in Antarctic species is generally slower than lower latitude species. Protein metabolism data for Antarctic invertebrates show low rates of protein synthesis and unusually high rates of protein degradation. Additionally, in Antarctic fish, increasing evidence suggests a lower frequency of successful folding of nascent proteins and reduced protein stability. This study reports the first whole-animal protein metabolism data for an Antarctic fish. Groups of Antarctic, Harpagifer antarcticus, and temperate, Lipophrys pholis, fish were acclimatized to a range of overlapping water temperatures and food consumption, whole-animal growth and protein metabolism measured. The rates of protein synthesis and growth in Antarctic, but not temperate fish, were relatively insensitive to temperature and were significantly lower in H. antarcticus at 3°C than in L. pholis. Protein degradation was independent of temperature in H. antarcticus and not significantly different to L. pholis at 3°C, while protein synthesis retention efficiency was significantly higher in L. pholis than H. antarcticus at 3°C. These results suggest Antarctic fish degrade a significantly larger proportion of synthesized protein than temperate fish, with fundamental energetic implications for growth at low temperatures. Article in Journal/Newspaper Antarc* Antarctic antarcticus Directory of Open Access Journals: DOAJ Articles Antarctic Royal Society Open Science 9 3
institution Open Polar
collection Directory of Open Access Journals: DOAJ Articles
op_collection_id ftdoajarticles
language English
topic protein turnover
slow growth
temperature limitation
cryobiology
Antarctic
protein synthesis
Science
Q
spellingShingle protein turnover
slow growth
temperature limitation
cryobiology
Antarctic
protein synthesis
Science
Q
Keiron P. P. Fraser
Lloyd S. Peck
Melody S. Clark
Andrew Clarke
Simeon L. Hill
Life in the freezer: protein metabolism in Antarctic fish
topic_facet protein turnover
slow growth
temperature limitation
cryobiology
Antarctic
protein synthesis
Science
Q
description Whole-animal, in vivo protein metabolism rates have been reported in temperate and tropical, but not Antarctic fish. Growth in Antarctic species is generally slower than lower latitude species. Protein metabolism data for Antarctic invertebrates show low rates of protein synthesis and unusually high rates of protein degradation. Additionally, in Antarctic fish, increasing evidence suggests a lower frequency of successful folding of nascent proteins and reduced protein stability. This study reports the first whole-animal protein metabolism data for an Antarctic fish. Groups of Antarctic, Harpagifer antarcticus, and temperate, Lipophrys pholis, fish were acclimatized to a range of overlapping water temperatures and food consumption, whole-animal growth and protein metabolism measured. The rates of protein synthesis and growth in Antarctic, but not temperate fish, were relatively insensitive to temperature and were significantly lower in H. antarcticus at 3°C than in L. pholis. Protein degradation was independent of temperature in H. antarcticus and not significantly different to L. pholis at 3°C, while protein synthesis retention efficiency was significantly higher in L. pholis than H. antarcticus at 3°C. These results suggest Antarctic fish degrade a significantly larger proportion of synthesized protein than temperate fish, with fundamental energetic implications for growth at low temperatures.
format Article in Journal/Newspaper
author Keiron P. P. Fraser
Lloyd S. Peck
Melody S. Clark
Andrew Clarke
Simeon L. Hill
author_facet Keiron P. P. Fraser
Lloyd S. Peck
Melody S. Clark
Andrew Clarke
Simeon L. Hill
author_sort Keiron P. P. Fraser
title Life in the freezer: protein metabolism in Antarctic fish
title_short Life in the freezer: protein metabolism in Antarctic fish
title_full Life in the freezer: protein metabolism in Antarctic fish
title_fullStr Life in the freezer: protein metabolism in Antarctic fish
title_full_unstemmed Life in the freezer: protein metabolism in Antarctic fish
title_sort life in the freezer: protein metabolism in antarctic fish
publisher The Royal Society
publishDate 2022
url https://doi.org/10.1098/rsos.211272
https://doaj.org/article/0f4b185df1d64fac865904baeda2a5a7
geographic Antarctic
geographic_facet Antarctic
genre Antarc*
Antarctic
antarcticus
genre_facet Antarc*
Antarctic
antarcticus
op_source Royal Society Open Science, Vol 9, Iss 3 (2022)
op_relation https://royalsocietypublishing.org/doi/10.1098/rsos.211272
https://doaj.org/toc/2054-5703
doi:10.1098/rsos.211272
2054-5703
https://doaj.org/article/0f4b185df1d64fac865904baeda2a5a7
op_doi https://doi.org/10.1098/rsos.211272
container_title Royal Society Open Science
container_volume 9
container_issue 3
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