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Evolutionary force in confamiliar marine vertebrates of different temperature realms: adaptive trends in zoarcid fish transcriptomes
- Source :
- BMC Genomics, Vol 13, Iss 1, p 549 (2012), BMC Genomics
- Publisher :
- Springer Nature
-
Abstract
- Background Studies 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. Results By 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. Conclusion Based 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.
- Subjects :
- lcsh:QH426-470
lcsh:Biotechnology
Antarctic Regions
Biology
Evolution, Molecular
Transcriptome
03 medical and health sciences
Protein structure
Species Specificity
Phylogenetics
lcsh:TP248.13-248.65
Genetics
Animals
14. Life underwater
Codon
Ecosystem
Phylogeny
Gene Library
030304 developmental biology
0303 health sciences
Myocardium
030302 biochemistry & molecular biology
Temperature
Protein primary structure
RNA
Adaptation, Physiological
Perciformes
lcsh:Genetics
Liver
Codon usage bias
GC-content
Research Article
Reference genome
Biotechnology
Subjects
Details
- Language :
- English
- ISSN :
- 14712164
- Volume :
- 13
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- BMC Genomics
- Accession number :
- edsair.doi.dedup.....29ee37fceca58e59663d839fb2601ed0
- Full Text :
- https://doi.org/10.1186/1471-2164-13-549