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Amaral, L. A.

Publications and source records attributed to Amaral, L. A..

2 recordsLinked to original sources

Selection removes Shine-Dalgarno-like sequences from within protein coding genes

The Shine-Dalgarno (SD) sequence motif facilitates translation initiation and is frequently found upstream of bacterial start codons. However, thousands of instances of this motif occur throughout the middle of protein coding genes in a typical bacterial genome. Here, we use comparative evolutionary analysis to test whether SD sequences located within genes are functionally constrained. We measure the conservation of SD sequences across Gammaproteobacteria, and find that they are significantly less conserved than expected. Further, the strongest SD sequences are the least conserved whereas we find evidence of conservation for the weakest possible SD sequences given amino acid constraints. Our findings indicate that most SD sequences within genes are likely to be deleterious and removed via selection. To illustrate the origin of these deleterious costs, we show that ATG start codons are significantly depleted downstream of SD sequences within genes, highlighting the potential for these sequences to promote erroneous translation initiation.

evolutionary biology

Diversity of translation initiation mechanisms across bacterial species is driven by environmental conditions and growth demands

The Shine-Dalgarno (SD) sequence is often found upstream of protein coding genes across the bacterial kingdom, where it enhances start codon recognition via hybridization to the anti-SD (aSD) sequence on the small ribosomal subunit. Despite widespread conservation of the aSD sequence, the proportion of SD-led genes within a genome varies widely across species, and the evolutionary pressures shaping this variation remain largely unknown. Here, we conduct a phylogenetically-informed analysis and show that species capable of rapid growth have a significantly higher proportion of SD-led genes in their genome, suggesting a role for SD sequences in meeting the protein production demands of rapidly growing species. Further, we show that utilization of the SD sequence mechanism co-varies with: i) genomic traits that are indicative of efficient translation, and ii) optimal growth temperatures. In contrast to prior surveys, our results demonstrate that variation in translation initiation mechanisms across genomes is largely predictable, and that SD sequence utilization is part of a larger suite of translation-associated traits whose diversity is driven by the differential growth strategies of individual species.

systems biology