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Reduced Polymorphism in Domains Involved in Protein-Protein Interactions

Genome sequencing of various individuals or isolates of the same species allows studying the polymorphism level of specific proteins and protein domains. Here we ask whether domains that are known to be involved in mediating protein-protein interactions show lower polymorphism than other domains. To...

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Detalles Bibliográficos
Autores principales: Itzhaki, Zohar, Margalit, Hanah
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3317993/
https://www.ncbi.nlm.nih.gov/pubmed/22509312
http://dx.doi.org/10.1371/journal.pone.0034503
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author Itzhaki, Zohar
Margalit, Hanah
author_facet Itzhaki, Zohar
Margalit, Hanah
author_sort Itzhaki, Zohar
collection PubMed
description Genome sequencing of various individuals or isolates of the same species allows studying the polymorphism level of specific proteins and protein domains. Here we ask whether domains that are known to be involved in mediating protein-protein interactions show lower polymorphism than other domains. To this end we take advantage of a recent genome sequence dataset of 39 Saccahromyces cerevisiae strains and the experimentally determined protein interaction network of the laboratory strain. We analyze the polymorphism in domain residues involved in interactions at various levels of resolution, depending on their likelihood to be interaction mediators. We find that domains involved in interactions are less polymorphic than other domains. Furthermore, as the likelihood of a residue to be involved in interaction increases, its polymorphism decreases. Our results suggest that purifying selection operates on domains capable of mediating protein interactions to maintain their function.
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spelling pubmed-33179932012-04-16 Reduced Polymorphism in Domains Involved in Protein-Protein Interactions Itzhaki, Zohar Margalit, Hanah PLoS One Research Article Genome sequencing of various individuals or isolates of the same species allows studying the polymorphism level of specific proteins and protein domains. Here we ask whether domains that are known to be involved in mediating protein-protein interactions show lower polymorphism than other domains. To this end we take advantage of a recent genome sequence dataset of 39 Saccahromyces cerevisiae strains and the experimentally determined protein interaction network of the laboratory strain. We analyze the polymorphism in domain residues involved in interactions at various levels of resolution, depending on their likelihood to be interaction mediators. We find that domains involved in interactions are less polymorphic than other domains. Furthermore, as the likelihood of a residue to be involved in interaction increases, its polymorphism decreases. Our results suggest that purifying selection operates on domains capable of mediating protein interactions to maintain their function. Public Library of Science 2012-04-03 /pmc/articles/PMC3317993/ /pubmed/22509312 http://dx.doi.org/10.1371/journal.pone.0034503 Text en Itzhaki, Margalit. 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
Itzhaki, Zohar
Margalit, Hanah
Reduced Polymorphism in Domains Involved in Protein-Protein Interactions
title Reduced Polymorphism in Domains Involved in Protein-Protein Interactions
title_full Reduced Polymorphism in Domains Involved in Protein-Protein Interactions
title_fullStr Reduced Polymorphism in Domains Involved in Protein-Protein Interactions
title_full_unstemmed Reduced Polymorphism in Domains Involved in Protein-Protein Interactions
title_short Reduced Polymorphism in Domains Involved in Protein-Protein Interactions
title_sort reduced polymorphism in domains involved in protein-protein interactions
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3317993/
https://www.ncbi.nlm.nih.gov/pubmed/22509312
http://dx.doi.org/10.1371/journal.pone.0034503
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