ArticleBMC genomics2012
Evolutionary force in confamiliar marine vertebrates of different temperature realms: adaptive trends in zoarcid fish transcriptomes.
Article in BMC genomics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Molecular Response and Metabolic Reprogramming of the Spleen Coping with Cold Stress in the Chinese Soft-Shelled Turtle (Antioxidants (Basel, Switzerland) · 2025Article
- Evolutionary Adaptation of Protein Turnover in White Muscle of Stenothermal Antarctic Fish: Elevated Cold Compensation at Reduced Thermal Responsiveness.Biomolecules · 2023Article
- Transcriptional Modulation Reveals Physiological Responses to Temperature Adaptation inInternational journal of molecular sciences · 2023Article
- Tracing and exploring the evolutionary origin and systematic function of fish complement C9.Molecular genetics and genomics : MGG · 2021Article
- Antifreeze protein dispersion in eelpouts and related fishes reveals migration and climate alteration within the last 20 Ma.PloS one · 2020Article
- Adaptation of Proteins to the Cold in Antarctic Fish: A Role for Methionine?Genome biology and evolution · 2019Article
- Arabidopsis Heat Stress-Induced Proteins Are Enriched in Electrostatically Charged Amino Acids and Intrinsically Disordered Regions.International journal of molecular sciences · 2018Article
- DNA methylation, epigenetics, and evolution in vertebrates: facts and challenges.International journal of evolutionary biology · 2014Review
- De novo assembly and characterization of tissue specific transcriptomes in the emerald notothen, Trematomus bernacchii.BMC genomics · 2013Article
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3 authors.
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Abstract
backgroundStudies of temperature-induced adaptation on the basis of genomic sequence data were mainly done in extremophiles. Although the general hypothesis of an increased molecular flexibility in the cold is widely accepted, the results of thermal adaptation are still difficult to detect at proteomic down to the genomic sequence level. Approaches towards a more detailed picture emerge with the advent of new sequencing technologies. Only small changes in primary protein structure have been shown to modify kinetic and thermal properties of enzymes, but likewise for interspecies comparisons a high genetic identity is still essential to specify common principles. The present study uses comprehensive transcriptomic sequence information to uncover general patterns of thermal adaptation on the RNA as well as protein primary structure.
resultsBy comparing orthologous sequences of two closely related zoarcid fish inhabiting different latitudinal zones (Antarctica: Pachycara brachycephalum, temperate zone: Zoarces viviparus) we were able to detect significant differences in the codon usage. In the cold-adapted species a lower GC content in the wobble position prevailed for preserved amino acids. We were able to estimate 40-60% coverage of the functions represented within the two compared zoarcid cDNA-libraries on the basis of a reference genome of the phylogenetically closely related fish Gasterosteus aculeatus. A distinct pattern of amino acid substitutions could be identified for the non-synonymous codon exchanges, with a remarkable surplus of serine and reduction of glutamic acid and asparagine for the Antarctic species.
conclusionBased on the differences between orthologous sequences from confamiliar species, distinguished mainly by the temperature regimes of their habitats, we hypothesize that temperature leaves a signature on the composition of biological macromolecules (RNA, proteins) with implications for the transcription and translation level. As the observed pattern of amino acid substitutions only partly support the flexibility hypothesis further evolutionary forces may be effective at the global transcriptome level.
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