Abstract
The debate of genomic correlations between sequence conservation, protein connectivity, gene essentiality and gene expression, has generated a number of new hypotheses that are challenging the classical framework of molecular evolution. For instance, the translational selection hypothesis claims that the determination of the rate of protein evolution is the protein stability to avoid the misfolding toxicity. In this short article, we propose that gene pleiotropy, the capacity for affecting multiple phenotypes, may play a vital role in molecular evolution. We discuss several approaches to testing this hypothesis.ReviewersThis article was reviewed by Dr Eugene Koonin, Dr Arcady Mushegian and Dr Claus Wilke.
Highlights
A high controversy in evolutionary genomics is around the pervasive yet weak genomic correlations with the evolutionary rate of protein sequence [1,2]
In spite of a number of controversial issues, the logic of this type of analysis remains roughly the same, that is, statistically establish the correlation between biologically factors and the evolutionary rate. These efforts have generated some interesting hypotheses, but it has been found difficult to be integrated to the theory of molecular evolution [17] based on several population genetics mechanisms and assumptions about the genotype-phenotype mapping
Implications of the hypothesis In this short article, we argue that the solution for what is the main determinant of the rate of protein evolution may depend on how to interpret the functional constraint of protein sequence
Summary
A high controversy in evolutionary genomics is around the pervasive yet weak genomic correlations with the evolutionary rate of protein sequence [1,2]. 2.The distribution of evolutionary rates across genome-wide sets of orthologous protein-coding genes is essentially universal among cellular life forms, from bacteria to mammals [30] This seems to be best compatible with the hypothesis that protein evolution largely depends on the simple physics of folding (baseline selection, ) than on functional features of proteins like pleiotropy which hardly can be universally conserved. In principle we can explain why a protein is (relatively) conserved at the amino acid sequence level in some details, from physiological behavior, biological processes involved or tissue broadness All these factors are highly heterogeneous among genes, and that is why to be a weak genomic correlation.
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