Protein folding and quinary interactions: creating cellular organisation through functional disorder

Detalhes bibliográficos
Autor(a) principal: Ribeiro, Sara
Data de Publicação: 2018
Outros Autores: Ebbinghaus, Simon, Marcos, João Carlos
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/1822/73053
Resumo: The marginal stability of globular proteins in the cell is determined by the balance between excluded volume effect and soft interactions. Quinary interactions are a type of soft interactions involved in intracellular organisation and known to have stabilising or destabilising effects on globular proteins. Recent studies suggest that globular proteins have structural flexibility, exhibiting more than one functional state. Here, we propose that the quinary-induced destabilisation can be sufficient to produce functional partially unfolded states of globular proteins. The biological relevance of this mechanism is explored, involving intracellular phase separation and regulatory stress response mechanisms.
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spelling Protein folding and quinary interactions: creating cellular organisation through functional disorderintracellular organisationmacromolecular crowdingmembraneless organellesphase separationprotein stabilityCiências Naturais::Ciências QuímicasScience & TechnologyThe marginal stability of globular proteins in the cell is determined by the balance between excluded volume effect and soft interactions. Quinary interactions are a type of soft interactions involved in intracellular organisation and known to have stabilising or destabilising effects on globular proteins. Recent studies suggest that globular proteins have structural flexibility, exhibiting more than one functional state. Here, we propose that the quinary-induced destabilisation can be sufficient to produce functional partially unfolded states of globular proteins. The biological relevance of this mechanism is explored, involving intracellular phase separation and regulatory stress response mechanisms.The authors thank Hernani Geros for useful comments on the manuscript and Michael Smith for language advices. In addition, JCM and SR acknowledge the Foundation for Science and Technology, FCT- Portugal, for financial support through the Centre of Chemistry of the University of Minho (CQ-UM) (projects UID/QUI/00686/2013 and UID/QUI/00686/2016). SE acknowledges funding from the Cluster of Excellence RESOLV (EXC 1069) funded by the German Research Foundation (DFG) and the Human Frontier Science Program Organization Research Grant (Project: RGP0022/2017).WileyUniversidade do MinhoRibeiro, SaraEbbinghaus, SimonMarcos, João Carlos20182018-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/1822/73053eng1873-346810.1002/1873-3468.1321130070686https://febs.onlinelibrary.wiley.com/doi/full/10.1002/1873-3468.13211info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-05-11T07:30:38Zoai:repositorium.sdum.uminho.pt:1822/73053Portal AgregadorONGhttps://www.rcaap.pt/oai/openairemluisa.alvim@gmail.comopendoar:71602024-05-11T07:30:38Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Protein folding and quinary interactions: creating cellular organisation through functional disorder
title Protein folding and quinary interactions: creating cellular organisation through functional disorder
spellingShingle Protein folding and quinary interactions: creating cellular organisation through functional disorder
Ribeiro, Sara
intracellular organisation
macromolecular crowding
membraneless organelles
phase separation
protein stability
Ciências Naturais::Ciências Químicas
Science & Technology
title_short Protein folding and quinary interactions: creating cellular organisation through functional disorder
title_full Protein folding and quinary interactions: creating cellular organisation through functional disorder
title_fullStr Protein folding and quinary interactions: creating cellular organisation through functional disorder
title_full_unstemmed Protein folding and quinary interactions: creating cellular organisation through functional disorder
title_sort Protein folding and quinary interactions: creating cellular organisation through functional disorder
author Ribeiro, Sara
author_facet Ribeiro, Sara
Ebbinghaus, Simon
Marcos, João Carlos
author_role author
author2 Ebbinghaus, Simon
Marcos, João Carlos
author2_role author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv Ribeiro, Sara
Ebbinghaus, Simon
Marcos, João Carlos
dc.subject.por.fl_str_mv intracellular organisation
macromolecular crowding
membraneless organelles
phase separation
protein stability
Ciências Naturais::Ciências Químicas
Science & Technology
topic intracellular organisation
macromolecular crowding
membraneless organelles
phase separation
protein stability
Ciências Naturais::Ciências Químicas
Science & Technology
description The marginal stability of globular proteins in the cell is determined by the balance between excluded volume effect and soft interactions. Quinary interactions are a type of soft interactions involved in intracellular organisation and known to have stabilising or destabilising effects on globular proteins. Recent studies suggest that globular proteins have structural flexibility, exhibiting more than one functional state. Here, we propose that the quinary-induced destabilisation can be sufficient to produce functional partially unfolded states of globular proteins. The biological relevance of this mechanism is explored, involving intracellular phase separation and regulatory stress response mechanisms.
publishDate 2018
dc.date.none.fl_str_mv 2018
2018-01-01T00:00:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/1822/73053
url http://hdl.handle.net/1822/73053
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 1873-3468
10.1002/1873-3468.13211
30070686
https://febs.onlinelibrary.wiley.com/doi/full/10.1002/1873-3468.13211
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley
publisher.none.fl_str_mv Wiley
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
repository.mail.fl_str_mv mluisa.alvim@gmail.com
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