Complex stability and dynamic subunit interchange modulates the disparate activities of the yeast moonlighting proteins Hal3 and Vhs3

Saccharomyces cerevisiae Hal3 and Vhs3 are moonlighting proteins, acting both as inhibitors of the serine/threonine protein phosphatase Ppz1 and as subunits (together with Cab3) of the unique heterotrimeric phosphopantothenoylcysteine decarboxylase (PPCDC) enzyme of Hemiascomycetous yeast. Both thes...

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Autores: Abrie, J. Albert, Molero Merinero, Cristina, Ariño Carmona, Joaquín|||0000-0002-6774-2987, Strauss, Erick|||0000-0002-9898-8226
Tipo de recurso: artículo
Fecha de publicación:2015
País:España
Institución:Universitat Autònoma de Barcelona
Repositorio:Dipòsit Digital de Documents de la UAB
Idioma:inglés
OAI Identifier:oai:ddd.uab.cat:203990
Acceso en línea:https://ddd.uab.cat/record/203990
https://dx.doi.org/urn:doi:10.1038/srep15774
Access Level:acceso abierto
Palabra clave:Biocatalysis
Cell Cycle Proteins
Circular Dichroism
Coenzyme A
Flavins
Phosphoprotein Phosphatases
Protein Binding
Protein Multimerization
Protein Stability
Protein Structure, Secondary
Protein Structure, Tertiary
Recombinant Proteins
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Substrate Specificity
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spelling Complex stability and dynamic subunit interchange modulates the disparate activities of the yeast moonlighting proteins Hal3 and Vhs3Abrie, J. AlbertMolero Merinero, CristinaAriño Carmona, Joaquín|||0000-0002-6774-2987Strauss, Erick|||0000-0002-9898-8226BiocatalysisCell Cycle ProteinsCircular DichroismCoenzyme AFlavinsPhosphoprotein PhosphatasesProtein BindingProtein MultimerizationProtein StabilityProtein Structure, SecondaryProtein Structure, TertiaryRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubstrate SpecificitySaccharomyces cerevisiae Hal3 and Vhs3 are moonlighting proteins, acting both as inhibitors of the serine/threonine protein phosphatase Ppz1 and as subunits (together with Cab3) of the unique heterotrimeric phosphopantothenoylcysteine decarboxylase (PPCDC) enzyme of Hemiascomycetous yeast. Both these roles are essential: PPCDC catalyses the third step of coenzyme A biosynthesis, while Ppz1 inhibition is required for regulation of monovalent cation homeostasis. However, the mechanisms by which these proteins € disparate activities are regulated are not well understood. The PPCDC domains (PDs) of Hal3, Vhs3 and Cab3 constitute the minimum requirement for these proteins to show both PPCDC activity and, in the case of Hal3 and Vhs3, to bind to Ppz1. Using these PD proteins as a model system to study the possibility of dynamic interchange between these roles, we provide evidence that Hal3 binds Ppz1 as a monomer (1:1 stoichiometry), requiring it to de-oligomerize from its usual homo- and heterotrimeric states (the latter having PPCDC activity). This de-oligomerization is made possible by structural features that set Hal3 apart from Vhs3, increasing its ability to undergo monomer exchange. These findings suggest that oligomer interchange may be a significant factor in the functional regulation of these proteins and their various unrelated (moonlighting) functions.Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí" 22015-01-0120152015-01-01Articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://ddd.uab.cat/record/203990https://dx.doi.org/urn:doi:10.1038/srep15774reponame:Dipòsit Digital de Documents de la UABinstname:Universitat Autònoma de BarcelonaInglésengMinisterio de Ciencia e Innovación https://doi.org/10.13039/501100004837 BFU2011-30197-C03-01Ministerio de Economía y Competitividad https://doi.org/10.13039/501100003329 BFU2014-54591-C2-1-PAgència de Gestió d'Ajuts Universitaris i de Recerca https://doi.org/10.13039/501100003030 2014/SGR-4open accesshttp://purl.org/coar/access_right/c_abf2Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, fins i tot amb finalitats comercials, sempre i quan es reconegui l'autoria de l'obra original.https://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:ddd.uab.cat:2039902026-06-06T12:50:31Z
dc.title.none.fl_str_mv Complex stability and dynamic subunit interchange modulates the disparate activities of the yeast moonlighting proteins Hal3 and Vhs3
title Complex stability and dynamic subunit interchange modulates the disparate activities of the yeast moonlighting proteins Hal3 and Vhs3
spellingShingle Complex stability and dynamic subunit interchange modulates the disparate activities of the yeast moonlighting proteins Hal3 and Vhs3
Abrie, J. Albert
Biocatalysis
Cell Cycle Proteins
Circular Dichroism
Coenzyme A
Flavins
Phosphoprotein Phosphatases
Protein Binding
Protein Multimerization
Protein Stability
Protein Structure, Secondary
Protein Structure, Tertiary
Recombinant Proteins
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Substrate Specificity
title_short Complex stability and dynamic subunit interchange modulates the disparate activities of the yeast moonlighting proteins Hal3 and Vhs3
title_full Complex stability and dynamic subunit interchange modulates the disparate activities of the yeast moonlighting proteins Hal3 and Vhs3
title_fullStr Complex stability and dynamic subunit interchange modulates the disparate activities of the yeast moonlighting proteins Hal3 and Vhs3
title_full_unstemmed Complex stability and dynamic subunit interchange modulates the disparate activities of the yeast moonlighting proteins Hal3 and Vhs3
title_sort Complex stability and dynamic subunit interchange modulates the disparate activities of the yeast moonlighting proteins Hal3 and Vhs3
dc.creator.none.fl_str_mv Abrie, J. Albert
Molero Merinero, Cristina
Ariño Carmona, Joaquín|||0000-0002-6774-2987
Strauss, Erick|||0000-0002-9898-8226
author Abrie, J. Albert
author_facet Abrie, J. Albert
Molero Merinero, Cristina
Ariño Carmona, Joaquín|||0000-0002-6774-2987
Strauss, Erick|||0000-0002-9898-8226
author_role author
author2 Molero Merinero, Cristina
Ariño Carmona, Joaquín|||0000-0002-6774-2987
Strauss, Erick|||0000-0002-9898-8226
author2_role author
author
author
dc.contributor.none.fl_str_mv Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí"
dc.subject.none.fl_str_mv Biocatalysis
Cell Cycle Proteins
Circular Dichroism
Coenzyme A
Flavins
Phosphoprotein Phosphatases
Protein Binding
Protein Multimerization
Protein Stability
Protein Structure, Secondary
Protein Structure, Tertiary
Recombinant Proteins
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Substrate Specificity
topic Biocatalysis
Cell Cycle Proteins
Circular Dichroism
Coenzyme A
Flavins
Phosphoprotein Phosphatases
Protein Binding
Protein Multimerization
Protein Stability
Protein Structure, Secondary
Protein Structure, Tertiary
Recombinant Proteins
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Substrate Specificity
description Saccharomyces cerevisiae Hal3 and Vhs3 are moonlighting proteins, acting both as inhibitors of the serine/threonine protein phosphatase Ppz1 and as subunits (together with Cab3) of the unique heterotrimeric phosphopantothenoylcysteine decarboxylase (PPCDC) enzyme of Hemiascomycetous yeast. Both these roles are essential: PPCDC catalyses the third step of coenzyme A biosynthesis, while Ppz1 inhibition is required for regulation of monovalent cation homeostasis. However, the mechanisms by which these proteins € disparate activities are regulated are not well understood. The PPCDC domains (PDs) of Hal3, Vhs3 and Cab3 constitute the minimum requirement for these proteins to show both PPCDC activity and, in the case of Hal3 and Vhs3, to bind to Ppz1. Using these PD proteins as a model system to study the possibility of dynamic interchange between these roles, we provide evidence that Hal3 binds Ppz1 as a monomer (1:1 stoichiometry), requiring it to de-oligomerize from its usual homo- and heterotrimeric states (the latter having PPCDC activity). This de-oligomerization is made possible by structural features that set Hal3 apart from Vhs3, increasing its ability to undergo monomer exchange. These findings suggest that oligomer interchange may be a significant factor in the functional regulation of these proteins and their various unrelated (moonlighting) functions.
publishDate 2015
dc.date.none.fl_str_mv 2
2015-01-01
2015
2015-01-01
dc.type.none.fl_str_mv Article
http://purl.org/coar/resource_type/c_6501
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://ddd.uab.cat/record/203990
https://dx.doi.org/urn:doi:10.1038/srep15774
url https://ddd.uab.cat/record/203990
https://dx.doi.org/urn:doi:10.1038/srep15774
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.relation.none.fl_str_mv Ministerio de Ciencia e Innovación https://doi.org/10.13039/501100004837 BFU2011-30197-C03-01
Ministerio de Economía y Competitividad https://doi.org/10.13039/501100003329 BFU2014-54591-C2-1-P
Agència de Gestió d'Ajuts Universitaris i de Recerca https://doi.org/10.13039/501100003030 2014/SGR-4
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
https://creativecommons.org/licenses/by/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
https://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Dipòsit Digital de Documents de la UAB
instname:Universitat Autònoma de Barcelona
instname_str Universitat Autònoma de Barcelona
reponame_str Dipòsit Digital de Documents de la UAB
collection Dipòsit Digital de Documents de la UAB
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,300719

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