Temperature and pH universally govern protein diversity in hydrothermal spring communities, but they do so differently
Rivas-Santisteban, J.; Alcorta, J.; Diez, B.; Tamames, J.; Pedros-Alio, C.
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It has been suggested that temperature and pH are strong explanatory causes of protein evolutionary constraint. However, a general understanding of how changes in temperature and pH may universally impact protein evolution is lacking. While pH is locally regulated in microbial compartments, temperature is not. These variables may act at different rates in a given genome, since there are genes encoding for proteins allocated in different compartments. To test whether this is true, we can use a proxy for the number of evolutionary events. One way is to calculate the diversity of unique sequences assigned to an ortholog across species. The expectation for any ortholog is to be represented by a similar number of sequences. We examine sequence diversity among 17 metagenomes from El Tatio geothermal field (Chile), spanning temperatures of 45-62{degrees}C, and pH values of 7.2-9.3. When controlling for metagenomic abundance, higher temperature increases, while basic pH decreases the expected by-function diversity. We thus provide evidence against temperature-induced random gene loss hypotheses. The inclusion of these variables improved the prediction of sequence diversity from metagenomic abundance. Importantly, between-compartment diversity was more affected by pH than by temperature, partially supporting our initial hypothesis
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