Adaptation of Proteins to the Cold in Antarctic Fish: A Role for Methionine?. (29th November 2018)
- Record Type:
- Journal Article
- Title:
- Adaptation of Proteins to the Cold in Antarctic Fish: A Role for Methionine?. (29th November 2018)
- Main Title:
- Adaptation of Proteins to the Cold in Antarctic Fish: A Role for Methionine?
- Authors:
- Berthelot, Camille
Clarke, Jane
Desvignes, Thomas
William Detrich, H
Flicek, Paul
Peck, Lloyd S
Peters, Michael
Postlethwait, John H
Clark, Melody S - Editors:
- Venkatesh, B
- Abstract:
- Abstract: The evolution of antifreeze glycoproteins has enabled notothenioid fish to flourish in the freezing waters of the Southern Ocean. Whereas successful at the biodiversity level to life in the cold, paradoxically at the cellular level these stenothermal animals have problems producing, folding, and degrading proteins at their ambient temperatures of –1.86 °C. In this first multi-species transcriptome comparison of the amino acid composition of notothenioid proteins with temperate teleost proteins, we show that, unlike psychrophilic bacteria, Antarctic fish provide little evidence for the mass alteration of protein amino acid composition to enhance protein folding and reduce protein denaturation in the cold. The exception was the significant overrepresentation of positions where leucine in temperate fish proteins was replaced by methionine in the notothenioid orthologues. We hypothesize that these extra methionines have been preferentially assimilated into the genome to act as redox sensors in the highly oxygenated waters of the Southern Ocean. This redox hypothesis is supported by analyses of notothenioids showing enrichment of genes associated with responses to environmental stress, particularly reactive oxygen species. So overall, although notothenioid fish show cold-associated problems with protein homeostasis, they may have modified only a selected number of biochemical pathways to work efficiently below 0 °C. Even a slight warming of the Southern Ocean mightAbstract: The evolution of antifreeze glycoproteins has enabled notothenioid fish to flourish in the freezing waters of the Southern Ocean. Whereas successful at the biodiversity level to life in the cold, paradoxically at the cellular level these stenothermal animals have problems producing, folding, and degrading proteins at their ambient temperatures of –1.86 °C. In this first multi-species transcriptome comparison of the amino acid composition of notothenioid proteins with temperate teleost proteins, we show that, unlike psychrophilic bacteria, Antarctic fish provide little evidence for the mass alteration of protein amino acid composition to enhance protein folding and reduce protein denaturation in the cold. The exception was the significant overrepresentation of positions where leucine in temperate fish proteins was replaced by methionine in the notothenioid orthologues. We hypothesize that these extra methionines have been preferentially assimilated into the genome to act as redox sensors in the highly oxygenated waters of the Southern Ocean. This redox hypothesis is supported by analyses of notothenioids showing enrichment of genes associated with responses to environmental stress, particularly reactive oxygen species. So overall, although notothenioid fish show cold-associated problems with protein homeostasis, they may have modified only a selected number of biochemical pathways to work efficiently below 0 °C. Even a slight warming of the Southern Ocean might disrupt the critical functions of this handful of key pathways with considerable impacts for the functioning of this ecosystem in the future. … (more)
- Is Part Of:
- Genome biology and evolution. Volume 11:Number 1(2019)
- Journal:
- Genome biology and evolution
- Issue:
- Volume 11:Number 1(2019)
- Issue Display:
- Volume 11, Issue 1 (2019)
- Year:
- 2019
- Volume:
- 11
- Issue:
- 1
- Issue Sort Value:
- 2019-0011-0001-0000
- Page Start:
- 220
- Page End:
- 231
- Publication Date:
- 2018-11-29
- Subjects:
- protein folding -- gene duplication -- positive selection -- map kinases -- environmental stress response -- reactive oxygen species
Genomics -- Periodicals
Genes -- Periodicals
572.8605 - Journal URLs:
- http://gbe.oxfordjournals.org/ ↗
http://ukcatalogue.oup.com/ ↗ - DOI:
- 10.1093/gbe/evy262 ↗
- Languages:
- English
- ISSNs:
- 1759-6653
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 11988.xml