Abstract
A number of fungal lineages, notably N. crassa, have evolved a novel mechanism of processing genomic duplication events known as repeat-induced point (RIP) mutation. This mechanism appears, on the one hand, to act as a conservative genomic safeguard, by introducing stop codons into duplicated nucleotide sequences, thereby preempting consequences such as dosage effects. However, it also typically performs further nonsynonymous (i.e., amino acid-changing) nucleotide substitutions, the significance of which is unclear. We explore here the possibility that RIP-mutated genes which evade silencing may have some microevolutionary impact on functional sequences. Our approach focuses on structurally important hydrophobic/polar (HP) amino-acid substitutions effected by RIP. We exploit a simple generic protein folding model to predict the associated emergence of increased protein-structural stability and variance within a large population.
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Funding for this work was provided by the Swedish Foundation for Strategic Research. We also acknowledge the reviewers of this paper for some valuable comments.
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Braun, F.N., Liberles, D.A. Repeat-Modulated Population Genetic Effects in Fungal Proteins. J Mol Evol 59, 97–102 (2004). https://doi.org/10.1007/s00239-004-2608-9
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DOI: https://doi.org/10.1007/s00239-004-2608-9