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Evolutionary Study of Protein Short Tandem Repeats in Protein Families

Tandem repeats in proteins are patterns of residues repeated directly adjacent to each other. The evolution of these repeats can be assessed by using groups of homologous sequences, which can help pointing to events of unit duplication or deletion. High pressure in a protein family for variation of...

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Autores principales: Mier, Pablo, Andrade-Navarro, Miguel A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10377733/
https://www.ncbi.nlm.nih.gov/pubmed/37509152
http://dx.doi.org/10.3390/biom13071116
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author Mier, Pablo
Andrade-Navarro, Miguel A.
author_facet Mier, Pablo
Andrade-Navarro, Miguel A.
author_sort Mier, Pablo
collection PubMed
description Tandem repeats in proteins are patterns of residues repeated directly adjacent to each other. The evolution of these repeats can be assessed by using groups of homologous sequences, which can help pointing to events of unit duplication or deletion. High pressure in a protein family for variation of a given type of repeat might point to their function. Here, we propose the analysis of protein families to calculate protein short tandem repeats (pSTRs) in each protein sequence and assess their variability within the family in terms of number of units. To facilitate this analysis, we developed the pSTR tool, a method to analyze the evolution of protein short tandem repeats in a given protein family by pairwise comparisons between evolutionarily related protein sequences. We evaluated pSTR unit number variation in protein families of 12 complete metazoan proteomes. We hypothesize that families with more dynamic ensembles of repeats could reflect particular roles of these repeats in processes that require more adaptability.
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spelling pubmed-103777332023-07-29 Evolutionary Study of Protein Short Tandem Repeats in Protein Families Mier, Pablo Andrade-Navarro, Miguel A. Biomolecules Communication Tandem repeats in proteins are patterns of residues repeated directly adjacent to each other. The evolution of these repeats can be assessed by using groups of homologous sequences, which can help pointing to events of unit duplication or deletion. High pressure in a protein family for variation of a given type of repeat might point to their function. Here, we propose the analysis of protein families to calculate protein short tandem repeats (pSTRs) in each protein sequence and assess their variability within the family in terms of number of units. To facilitate this analysis, we developed the pSTR tool, a method to analyze the evolution of protein short tandem repeats in a given protein family by pairwise comparisons between evolutionarily related protein sequences. We evaluated pSTR unit number variation in protein families of 12 complete metazoan proteomes. We hypothesize that families with more dynamic ensembles of repeats could reflect particular roles of these repeats in processes that require more adaptability. MDPI 2023-07-13 /pmc/articles/PMC10377733/ /pubmed/37509152 http://dx.doi.org/10.3390/biom13071116 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Communication
Mier, Pablo
Andrade-Navarro, Miguel A.
Evolutionary Study of Protein Short Tandem Repeats in Protein Families
title Evolutionary Study of Protein Short Tandem Repeats in Protein Families
title_full Evolutionary Study of Protein Short Tandem Repeats in Protein Families
title_fullStr Evolutionary Study of Protein Short Tandem Repeats in Protein Families
title_full_unstemmed Evolutionary Study of Protein Short Tandem Repeats in Protein Families
title_short Evolutionary Study of Protein Short Tandem Repeats in Protein Families
title_sort evolutionary study of protein short tandem repeats in protein families
topic Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10377733/
https://www.ncbi.nlm.nih.gov/pubmed/37509152
http://dx.doi.org/10.3390/biom13071116
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