Evolution of networks of protein domain organization

Abstract Domains are the structural, functional and evolutionary units of proteins. They combine to form multidomain proteins. The evolutionary history of this molecular combinatorics has been studied with phylogenomic methods. Here, we construct networks of domain organization and explore their evo...

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Autores principales: M. Fayez Aziz, Gustavo Caetano-Anollés
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Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/5e3ea5d14cda4503a3a348ecdbd00710
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spelling oai:doaj.org-article:5e3ea5d14cda4503a3a348ecdbd007102021-12-02T17:52:31ZEvolution of networks of protein domain organization10.1038/s41598-021-90498-82045-2322https://doaj.org/article/5e3ea5d14cda4503a3a348ecdbd007102021-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-90498-8https://doaj.org/toc/2045-2322Abstract Domains are the structural, functional and evolutionary units of proteins. They combine to form multidomain proteins. The evolutionary history of this molecular combinatorics has been studied with phylogenomic methods. Here, we construct networks of domain organization and explore their evolution. A time series of networks revealed two ancient waves of structural novelty arising from ancient ‘p-loop’ and ‘winged helix’ domains and a massive ‘big bang’ of domain organization. The evolutionary recruitment of domains was highly modular, hierarchical and ongoing. Domain rearrangements elicited non-random and scale-free network structure. Comparative analyses of preferential attachment, randomness and modularity showed yin-and-yang complementary transition and biphasic patterns along the structural chronology. Remarkably, the evolving networks highlighted a central evolutionary role of cofactor-supporting structures of non-ribosomal peptide synthesis pathways, likely crucial to the early development of the genetic code. Some highly modular domains featured dual response regulation in two-component signal transduction systems with DNA-binding activity linked to transcriptional regulation of responses to environmental change. Interestingly, hub domains across the evolving networks shared the historical role of DNA binding and editing, an ancient protein function in molecular evolution. Our investigation unfolds historical source-sink patterns of evolutionary recruitment that further our understanding of protein architectures and functions.M. Fayez AzizGustavo Caetano-AnollésNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-18 (2021)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
M. Fayez Aziz
Gustavo Caetano-Anollés
Evolution of networks of protein domain organization
description Abstract Domains are the structural, functional and evolutionary units of proteins. They combine to form multidomain proteins. The evolutionary history of this molecular combinatorics has been studied with phylogenomic methods. Here, we construct networks of domain organization and explore their evolution. A time series of networks revealed two ancient waves of structural novelty arising from ancient ‘p-loop’ and ‘winged helix’ domains and a massive ‘big bang’ of domain organization. The evolutionary recruitment of domains was highly modular, hierarchical and ongoing. Domain rearrangements elicited non-random and scale-free network structure. Comparative analyses of preferential attachment, randomness and modularity showed yin-and-yang complementary transition and biphasic patterns along the structural chronology. Remarkably, the evolving networks highlighted a central evolutionary role of cofactor-supporting structures of non-ribosomal peptide synthesis pathways, likely crucial to the early development of the genetic code. Some highly modular domains featured dual response regulation in two-component signal transduction systems with DNA-binding activity linked to transcriptional regulation of responses to environmental change. Interestingly, hub domains across the evolving networks shared the historical role of DNA binding and editing, an ancient protein function in molecular evolution. Our investigation unfolds historical source-sink patterns of evolutionary recruitment that further our understanding of protein architectures and functions.
format article
author M. Fayez Aziz
Gustavo Caetano-Anollés
author_facet M. Fayez Aziz
Gustavo Caetano-Anollés
author_sort M. Fayez Aziz
title Evolution of networks of protein domain organization
title_short Evolution of networks of protein domain organization
title_full Evolution of networks of protein domain organization
title_fullStr Evolution of networks of protein domain organization
title_full_unstemmed Evolution of networks of protein domain organization
title_sort evolution of networks of protein domain organization
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/5e3ea5d14cda4503a3a348ecdbd00710
work_keys_str_mv AT mfayezaziz evolutionofnetworksofproteindomainorganization
AT gustavocaetanoanolles evolutionofnetworksofproteindomainorganization
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