Combing Transcriptomes for Secrets of Deep-Sea Survival:Environmental Diversity Drives Patterns of Protein Evolution
| Autor: | Warren R. Francis, Erik V. Thuesen, Steven H. D. Haddock, Jacob R. Winnikoff |
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| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Rossmann fold Hydrostatic pressure Adaptation Biological Mutagenesis (molecular biology technique) Plant Science Biology Evolution Molecular 03 medical and health sciences 0302 clinical medicine Extreme environment Animals 14. Life underwater Amino Acid Sequence Chemical Responses to the Biotic and Abiotic Environment by Early Diverging Metazoans Revealed in the Post-Genomic Age Phylogeny chemistry.chemical_classification Cofactor binding Phylogenetic tree Ctenophora Amino acid 030104 developmental biology chemistry Evolutionary biology Animal Science and Zoology Adaptation Transcriptome Animal Distribution Sequence Alignment 030217 neurology & neurosurgery |
| Zdroj: | Winnikoff, J R, Francis, W R, Thuesen, E V & Haddock, S H D 2019, ' Combing Transcriptomes for Secrets of Deep-Sea Survival : Environmental Diversity Drives Patterns of Protein Evolution ', Integrative and Comparative Biology, vol. 59, no. 4, pp. 786-798 . https://doi.org/10.1093/icb/icz063 Integrative and Comparative Biology |
| Popis: | Ctenophores, also known as comb jellies, live across extremely broad ranges of temperature and hydrostatic pressure in the ocean. Because various ctenophore lineages adapted independently to similar environmental conditions, Phylum Ctenophora is an ideal system for the study of protein adaptation to extreme environments in a comparative framework. We present such a study here, using a phylogenetically-informed method to compare sequences of four essential metabolic enzymes across gradients of habitat depth and temperature. This method predicts convergent adaptation to these environmental parameters at the amino acid level, providing a novel view of protein adaptation to extreme environments and demonstrating the power and relevance of phylogenetic comparison applied to multi-species transcriptomic datasets from early-diverging metazoa. Across all four enzymes analyzed, 46 amino acid sites were associated with depth-adaptation, 59 with temperature-adaptation, and 56 with both. Sites predicted to be depth- and temperature-adaptive occurred consistently near Rossmann fold cofactor binding motifs and disproportionately in solvent-exposed regions of the protein. These results suggest that the hydrophobic effect and ligand binding may mediate efficient enzyme function at different hydrostatic pressures and temperatures. Using predicted adaptive site maps, such mechanistic hypotheses can now be tested via mutagenesis. |
| Databáze: | OpenAIRE |
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