Local genic base composition impacts protein production and cellular fitness
| Autor: | Howard Ochman, Erik M. Quandt, Charles C. Traverse |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Evolution lcsh:Medicine Biology G + C content Genome General Biochemistry Genetics and Molecular Biology 03 medical and health sciences Negative selection Genetics Protein biosynthesis Molecular Biology Gene Selection (genetic algorithm) Base composition 2. Zero hunger Translation rate General Neuroscience lcsh:R Translation (biology) General Medicine Evolutionary Studies 030104 developmental biology Codon usage bias Synthetic Biology Protein folding Codon usage General Agricultural and Biological Sciences Biotechnology |
| Zdroj: | PeerJ, Vol 6, p e4286 (2018) PeerJ |
| ISSN: | 2167-8359 |
| DOI: | 10.7717/peerj.4286 |
| Popis: | The maintenance of a G + C content that is higher than the mutational input to a genome provides support for the view that selection serves to increase G + C contents in bacteria. Recent experimental evidence fromEscherichia colidemonstrated that selection for increasing G + C content operates at the level of translation, but the precise mechanism by which this occurs is unknown. To determine the substrate of selection, we asked whether selection on G + C content acts across all sites within a gene or is confined to particular genic regions or nucleotide positions. We systematically altered the G + C contents of the GFP gene and assayed its effects on the fitness of strains harboring each variant. Fitness differences were attributable to the base compositional variation in the terminal portion of the gene, suggesting a connection to the folding of a specific protein feature. Variants containing sequence features that are thought to result in rapid translation, such as low G + C content and high levels of codon adaptation, displayed highly reduced growth rates. Taken together, our results show that purifying selection acting against A and T mutations most likely results from their tendency to increase the rate of translation, which can perturb the dynamics of protein folding. |
| Databáze: | OpenAIRE |
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