Structure and age jointly influence rates of protein evolution.

What factors determine a protein's rate of evolution are actively debated. Especially unclear is the relative role of intrinsic factors of present-day proteins versus historical factors such as protein age. Here we study the interplay of structural properties and evolutionary age, as determinan...

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Autores principales:	Macarena Toll-Riera, David Bostick, M Mar Albà, Joshua B Plotkin
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/c817b52ac75a40afb45ce28b555c6487
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spelling	oai:doaj.org-article:c817b52ac75a40afb45ce28b555c64872021-11-18T05:51:17ZStructure and age jointly influence rates of protein evolution.1553-734X1553-735810.1371/journal.pcbi.1002542https://doaj.org/article/c817b52ac75a40afb45ce28b555c64872012-05-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22693443/pdf/?tool=EBIhttps://doaj.org/toc/1553-734Xhttps://doaj.org/toc/1553-7358What factors determine a protein's rate of evolution are actively debated. Especially unclear is the relative role of intrinsic factors of present-day proteins versus historical factors such as protein age. Here we study the interplay of structural properties and evolutionary age, as determinants of protein evolutionary rate. We use a large set of one-to-one orthologs between human and mouse proteins, with mapped PDB structures. We report that previously observed structural correlations also hold within each age group - including relationships between solvent accessibility, designabililty, and evolutionary rates. However, age also plays a crucial role: age modulates the relationship between solvent accessibility and rate. Additionally, younger proteins, despite being less designable, tend to evolve faster than older proteins. We show that previously reported relationships between age and rate cannot be explained by structural biases among age groups. Finally, we introduce a knowledge-based potential function to study the stability of proteins through large-scale computation. We find that older proteins are more stable for their native structure, and more robust to mutations, than younger ones. Our results underscore that several determinants, both intrinsic and historical, can interact to determine rates of protein evolution.Macarena Toll-RieraDavid BostickM Mar AlbàJoshua B PlotkinPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Computational Biology, Vol 8, Iss 5, p e1002542 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Macarena Toll-Riera David Bostick M Mar Albà Joshua B Plotkin Structure and age jointly influence rates of protein evolution.
description	What factors determine a protein's rate of evolution are actively debated. Especially unclear is the relative role of intrinsic factors of present-day proteins versus historical factors such as protein age. Here we study the interplay of structural properties and evolutionary age, as determinants of protein evolutionary rate. We use a large set of one-to-one orthologs between human and mouse proteins, with mapped PDB structures. We report that previously observed structural correlations also hold within each age group - including relationships between solvent accessibility, designabililty, and evolutionary rates. However, age also plays a crucial role: age modulates the relationship between solvent accessibility and rate. Additionally, younger proteins, despite being less designable, tend to evolve faster than older proteins. We show that previously reported relationships between age and rate cannot be explained by structural biases among age groups. Finally, we introduce a knowledge-based potential function to study the stability of proteins through large-scale computation. We find that older proteins are more stable for their native structure, and more robust to mutations, than younger ones. Our results underscore that several determinants, both intrinsic and historical, can interact to determine rates of protein evolution.
format	article
author	Macarena Toll-Riera David Bostick M Mar Albà Joshua B Plotkin
author_facet	Macarena Toll-Riera David Bostick M Mar Albà Joshua B Plotkin
author_sort	Macarena Toll-Riera
title	Structure and age jointly influence rates of protein evolution.
title_short	Structure and age jointly influence rates of protein evolution.
title_full	Structure and age jointly influence rates of protein evolution.
title_fullStr	Structure and age jointly influence rates of protein evolution.
title_full_unstemmed	Structure and age jointly influence rates of protein evolution.
title_sort	structure and age jointly influence rates of protein evolution.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/c817b52ac75a40afb45ce28b555c6487
work_keys_str_mv	AT macarenatollriera structureandagejointlyinfluenceratesofproteinevolution AT davidbostick structureandagejointlyinfluenceratesofproteinevolution AT mmaralba structureandagejointlyinfluenceratesofproteinevolution AT joshuabplotkin structureandagejointlyinfluenceratesofproteinevolution
_version_	1718424754116886528

Structure and age jointly influence rates of protein evolution.

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