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Protomers of protein hetero-oligomers tend to resemble each other more than expected

A large fraction of the proteome is made by proteins that are not permanently monomeric but form oligomeric assemblies, which can be either homo- or hetero-oligomeric. Here it is described that protomers of hetero-oligomeric proteins tend to resemble each other more than expected. This is verified b...

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Detalles Bibliográficos
Autor principal: Carugo, Oliviero
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer International Publishing 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4447755/
https://www.ncbi.nlm.nih.gov/pubmed/26034682
http://dx.doi.org/10.1186/2193-1801-3-680
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author Carugo, Oliviero
author_facet Carugo, Oliviero
author_sort Carugo, Oliviero
collection PubMed
description A large fraction of the proteome is made by proteins that are not permanently monomeric but form oligomeric assemblies, which can be either homo- or hetero-oligomeric. Here it is described that protomers of hetero-oligomeric proteins tend to resemble each other more than expected. This is verified by comparing the level of similarity of pairs of hetero-oligomeric protein protomers and of pairs of proteins that do not interact with each other. This observation, interesting per se, might reflect the evolution of hetero-oligomers from ancestral homo-oligomers, through gene duplication and paralogs divergence. However, other hypotheses cannot be excluded and the observed structural similarity might result from several causes. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/2193-1801-3-680) contains supplementary material, which is available to authorized users.
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spelling pubmed-44477552015-06-01 Protomers of protein hetero-oligomers tend to resemble each other more than expected Carugo, Oliviero Springerplus Research A large fraction of the proteome is made by proteins that are not permanently monomeric but form oligomeric assemblies, which can be either homo- or hetero-oligomeric. Here it is described that protomers of hetero-oligomeric proteins tend to resemble each other more than expected. This is verified by comparing the level of similarity of pairs of hetero-oligomeric protein protomers and of pairs of proteins that do not interact with each other. This observation, interesting per se, might reflect the evolution of hetero-oligomers from ancestral homo-oligomers, through gene duplication and paralogs divergence. However, other hypotheses cannot be excluded and the observed structural similarity might result from several causes. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/2193-1801-3-680) contains supplementary material, which is available to authorized users. Springer International Publishing 2014-11-20 /pmc/articles/PMC4447755/ /pubmed/26034682 http://dx.doi.org/10.1186/2193-1801-3-680 Text en © Carugo; licensee Springer. 2014 This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited.
spellingShingle Research
Carugo, Oliviero
Protomers of protein hetero-oligomers tend to resemble each other more than expected
title Protomers of protein hetero-oligomers tend to resemble each other more than expected
title_full Protomers of protein hetero-oligomers tend to resemble each other more than expected
title_fullStr Protomers of protein hetero-oligomers tend to resemble each other more than expected
title_full_unstemmed Protomers of protein hetero-oligomers tend to resemble each other more than expected
title_short Protomers of protein hetero-oligomers tend to resemble each other more than expected
title_sort protomers of protein hetero-oligomers tend to resemble each other more than expected
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4447755/
https://www.ncbi.nlm.nih.gov/pubmed/26034682
http://dx.doi.org/10.1186/2193-1801-3-680
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