Protein flexibility facilitates quaternary structure assembly and evolution.

The intrinsic flexibility of proteins allows them to undergo large conformational fluctuations in solution or upon interaction with other molecules. Proteins also commonly assemble into complexes with diverse quaternary structure arrangements. Here we investigate how the flexibility of individual pr...

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Autores principales:	Joseph A Marsh, Sarah A Teichmann
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/3cc2f684f89048daa8ed385d071c5551
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spelling	oai:doaj.org-article:3cc2f684f89048daa8ed385d071c55512021-11-11T05:37:09ZProtein flexibility facilitates quaternary structure assembly and evolution.1544-91731545-788510.1371/journal.pbio.1001870https://doaj.org/article/3cc2f684f89048daa8ed385d071c55512014-05-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24866000/?tool=EBIhttps://doaj.org/toc/1544-9173https://doaj.org/toc/1545-7885The intrinsic flexibility of proteins allows them to undergo large conformational fluctuations in solution or upon interaction with other molecules. Proteins also commonly assemble into complexes with diverse quaternary structure arrangements. Here we investigate how the flexibility of individual protein chains influences the assembly and evolution of protein complexes. We find that flexibility appears to be particularly conducive to the formation of heterologous (i.e., asymmetric) intersubunit interfaces. This leads to a strong association between subunit flexibility and homomeric complexes with cyclic and asymmetric quaternary structure topologies. Similarly, we also observe that the more nonhomologous subunits that assemble together within a complex, the more flexible those subunits tend to be. Importantly, these findings suggest that subunit flexibility should be closely related to the evolutionary history of a complex. We confirm this by showing that evolutionarily more recent subunits are generally more flexible than evolutionarily older subunits. Finally, we investigate the very different explorations of quaternary structure space that have occurred in different evolutionary lineages. In particular, the increased flexibility of eukaryotic proteins appears to enable the assembly of heteromeric complexes with more unique components.Joseph A MarshSarah A TeichmannPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Biology, Vol 12, Iss 5, p e1001870 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Joseph A Marsh Sarah A Teichmann Protein flexibility facilitates quaternary structure assembly and evolution.
description	The intrinsic flexibility of proteins allows them to undergo large conformational fluctuations in solution or upon interaction with other molecules. Proteins also commonly assemble into complexes with diverse quaternary structure arrangements. Here we investigate how the flexibility of individual protein chains influences the assembly and evolution of protein complexes. We find that flexibility appears to be particularly conducive to the formation of heterologous (i.e., asymmetric) intersubunit interfaces. This leads to a strong association between subunit flexibility and homomeric complexes with cyclic and asymmetric quaternary structure topologies. Similarly, we also observe that the more nonhomologous subunits that assemble together within a complex, the more flexible those subunits tend to be. Importantly, these findings suggest that subunit flexibility should be closely related to the evolutionary history of a complex. We confirm this by showing that evolutionarily more recent subunits are generally more flexible than evolutionarily older subunits. Finally, we investigate the very different explorations of quaternary structure space that have occurred in different evolutionary lineages. In particular, the increased flexibility of eukaryotic proteins appears to enable the assembly of heteromeric complexes with more unique components.
format	article
author	Joseph A Marsh Sarah A Teichmann
author_facet	Joseph A Marsh Sarah A Teichmann
author_sort	Joseph A Marsh
title	Protein flexibility facilitates quaternary structure assembly and evolution.
title_short	Protein flexibility facilitates quaternary structure assembly and evolution.
title_full	Protein flexibility facilitates quaternary structure assembly and evolution.
title_fullStr	Protein flexibility facilitates quaternary structure assembly and evolution.
title_full_unstemmed	Protein flexibility facilitates quaternary structure assembly and evolution.
title_sort	protein flexibility facilitates quaternary structure assembly and evolution.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/3cc2f684f89048daa8ed385d071c5551
work_keys_str_mv	AT josephamarsh proteinflexibilityfacilitatesquaternarystructureassemblyandevolution AT sarahateichmann proteinflexibilityfacilitatesquaternarystructureassemblyandevolution
_version_	1718439477095956480

Protein flexibility facilitates quaternary structure assembly and evolution.

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