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Optimization of Mutation Pressure in Relation to Properties of Protein-Coding Sequences in Bacterial Genomes

Most mutations are deleterious and require energetically costly repairs. Therefore, it seems that any minimization of mutation rate is beneficial. On the other hand, mutations generate genetic diversity indispensable for evolution and adaptation of organisms to changing environmental conditions. Thu...

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Autores principales: Błażej, Paweł, Miasojedow, Błażej, Grabińska, Małgorzata, Mackiewicz, Paweł
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4488281/
https://www.ncbi.nlm.nih.gov/pubmed/26121655
http://dx.doi.org/10.1371/journal.pone.0130411
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author Błażej, Paweł
Miasojedow, Błażej
Grabińska, Małgorzata
Mackiewicz, Paweł
author_facet Błażej, Paweł
Miasojedow, Błażej
Grabińska, Małgorzata
Mackiewicz, Paweł
author_sort Błażej, Paweł
collection PubMed
description Most mutations are deleterious and require energetically costly repairs. Therefore, it seems that any minimization of mutation rate is beneficial. On the other hand, mutations generate genetic diversity indispensable for evolution and adaptation of organisms to changing environmental conditions. Thus, it is expected that a spontaneous mutational pressure should be an optimal compromise between these two extremes. In order to study the optimization of the pressure, we compared mutational transition probability matrices from bacterial genomes with artificial matrices fulfilling the same general features as the real ones, e.g., the stationary distribution and the speed of convergence to the stationarity. The artificial matrices were optimized on real protein-coding sequences based on Evolutionary Strategies approach to minimize or maximize the probability of non-synonymous substitutions and costs of amino acid replacements depending on their physicochemical properties. The results show that the empirical matrices have a tendency to minimize the effects of mutations rather than maximize their costs on the amino acid level. They were also similar to the optimized artificial matrices in the nucleotide substitution pattern, especially the high transitions/transversions ratio. We observed no substantial differences between the effects of mutational matrices on protein-coding sequences in genomes under study in respect of differently replicated DNA strands, mutational cost types and properties of the referenced artificial matrices. The findings indicate that the empirical mutational matrices are rather adapted to minimize mutational costs in the studied organisms in comparison to other matrices with similar mathematical constraints.
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spelling pubmed-44882812015-07-02 Optimization of Mutation Pressure in Relation to Properties of Protein-Coding Sequences in Bacterial Genomes Błażej, Paweł Miasojedow, Błażej Grabińska, Małgorzata Mackiewicz, Paweł PLoS One Research Article Most mutations are deleterious and require energetically costly repairs. Therefore, it seems that any minimization of mutation rate is beneficial. On the other hand, mutations generate genetic diversity indispensable for evolution and adaptation of organisms to changing environmental conditions. Thus, it is expected that a spontaneous mutational pressure should be an optimal compromise between these two extremes. In order to study the optimization of the pressure, we compared mutational transition probability matrices from bacterial genomes with artificial matrices fulfilling the same general features as the real ones, e.g., the stationary distribution and the speed of convergence to the stationarity. The artificial matrices were optimized on real protein-coding sequences based on Evolutionary Strategies approach to minimize or maximize the probability of non-synonymous substitutions and costs of amino acid replacements depending on their physicochemical properties. The results show that the empirical matrices have a tendency to minimize the effects of mutations rather than maximize their costs on the amino acid level. They were also similar to the optimized artificial matrices in the nucleotide substitution pattern, especially the high transitions/transversions ratio. We observed no substantial differences between the effects of mutational matrices on protein-coding sequences in genomes under study in respect of differently replicated DNA strands, mutational cost types and properties of the referenced artificial matrices. The findings indicate that the empirical mutational matrices are rather adapted to minimize mutational costs in the studied organisms in comparison to other matrices with similar mathematical constraints. Public Library of Science 2015-06-29 /pmc/articles/PMC4488281/ /pubmed/26121655 http://dx.doi.org/10.1371/journal.pone.0130411 Text en © 2015 Błażej et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Błażej, Paweł
Miasojedow, Błażej
Grabińska, Małgorzata
Mackiewicz, Paweł
Optimization of Mutation Pressure in Relation to Properties of Protein-Coding Sequences in Bacterial Genomes
title Optimization of Mutation Pressure in Relation to Properties of Protein-Coding Sequences in Bacterial Genomes
title_full Optimization of Mutation Pressure in Relation to Properties of Protein-Coding Sequences in Bacterial Genomes
title_fullStr Optimization of Mutation Pressure in Relation to Properties of Protein-Coding Sequences in Bacterial Genomes
title_full_unstemmed Optimization of Mutation Pressure in Relation to Properties of Protein-Coding Sequences in Bacterial Genomes
title_short Optimization of Mutation Pressure in Relation to Properties of Protein-Coding Sequences in Bacterial Genomes
title_sort optimization of mutation pressure in relation to properties of protein-coding sequences in bacterial genomes
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4488281/
https://www.ncbi.nlm.nih.gov/pubmed/26121655
http://dx.doi.org/10.1371/journal.pone.0130411
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