Structure of importin-α from a filamentous fungus in complex with a classical nuclear localization signal

Detalhes bibliográficos
Autor(a) principal: Bernardes, Natalia E. [UNESP]
Data de Publicação: 2015
Outros Autores: Takeda, Agnes A. S. [UNESP], Dreyer, Thiago R. [UNESP], Freitas, Fernanda Z. [UNESP], Bertolini, Maria Célia [UNESP], Fontes, Marcos R. M. [UNESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1371/journal.pone.0124970
http://hdl.handle.net/11449/228107
Resumo: Neurospora crassa is a filamentous fungus that has been extensively studied as a model organism for eukaryotic biology, providing fundamental insights into cellular processes such as cell signaling, growth and differentiation. To advance in the study of this multicellular organism, an understanding of the specific mechanisms for protein transport into the cell nucleus is essential. Importin-α (Imp-α) is the receptor for cargo proteins that contain specific nuclear localization signals (NLSs) that play a key role in the classical nuclear import pathway. Structures of Imp-α from different organisms (yeast, rice, mouse, and human) have been determined, revealing that this receptor possesses a conserved structural scaffold. However, recent studies have demonstrated that the Impα mechanism of action may vary significantly for different organisms or for different isoforms from the same organism. Therefore, structural, functional, and biophysical characterization of different Impα proteins is necessary to understand the selectivity of nuclear transport. Here, we determined the first crystal structure of an Impα from a filamentous fungus which is also the highest resolution Impα structure already solved to date (1.75 Å). In addition, we performed calorimetric analysis to determine the affinity and thermodynamic parameters of the interaction between Impαand the classical SV40 NLS peptide. The comparison of these data with previous studies on Impα proteins led us to demonstrate that N. crassa Imp-α possess specific features that are distinct from mammalian Imp-α but exhibit important similarities to rice Imp-α, particularly at the minor NLS binding site.
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spelling Structure of importin-α from a filamentous fungus in complex with a classical nuclear localization signalNeurospora crassa is a filamentous fungus that has been extensively studied as a model organism for eukaryotic biology, providing fundamental insights into cellular processes such as cell signaling, growth and differentiation. To advance in the study of this multicellular organism, an understanding of the specific mechanisms for protein transport into the cell nucleus is essential. Importin-α (Imp-α) is the receptor for cargo proteins that contain specific nuclear localization signals (NLSs) that play a key role in the classical nuclear import pathway. Structures of Imp-α from different organisms (yeast, rice, mouse, and human) have been determined, revealing that this receptor possesses a conserved structural scaffold. However, recent studies have demonstrated that the Impα mechanism of action may vary significantly for different organisms or for different isoforms from the same organism. Therefore, structural, functional, and biophysical characterization of different Impα proteins is necessary to understand the selectivity of nuclear transport. Here, we determined the first crystal structure of an Impα from a filamentous fungus which is also the highest resolution Impα structure already solved to date (1.75 Å). In addition, we performed calorimetric analysis to determine the affinity and thermodynamic parameters of the interaction between Impαand the classical SV40 NLS peptide. The comparison of these data with previous studies on Impα proteins led us to demonstrate that N. crassa Imp-α possess specific features that are distinct from mammalian Imp-α but exhibit important similarities to rice Imp-α, particularly at the minor NLS binding site.Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Departamento de Física E Biofísica Instituto de Biociências Universidade Estadual PaulistaDepartamento de Bioquímica E Tecnologia Química Instituto de Química Universidade Estadual PaulistaDepartamento de Física E Biofísica Instituto de Biociências Universidade Estadual PaulistaDepartamento de Bioquímica E Tecnologia Química Instituto de Química Universidade Estadual PaulistaUniversidade Estadual Paulista (UNESP)Bernardes, Natalia E. [UNESP]Takeda, Agnes A. S. [UNESP]Dreyer, Thiago R. [UNESP]Freitas, Fernanda Z. [UNESP]Bertolini, Maria Célia [UNESP]Fontes, Marcos R. M. [UNESP]2022-04-29T07:26:52Z2022-04-29T07:26:52Z2015-06-19info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1371/journal.pone.0124970PLoS ONE, v. 10, n. 6, 2015.1932-6203http://hdl.handle.net/11449/22810710.1371/journal.pone.01249702-s2.0-84956819601Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengPLoS ONEinfo:eu-repo/semantics/openAccess2022-04-29T07:26:52Zoai:repositorio.unesp.br:11449/228107Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T21:07:53.421406Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Structure of importin-α from a filamentous fungus in complex with a classical nuclear localization signal
title Structure of importin-α from a filamentous fungus in complex with a classical nuclear localization signal
spellingShingle Structure of importin-α from a filamentous fungus in complex with a classical nuclear localization signal
Bernardes, Natalia E. [UNESP]
title_short Structure of importin-α from a filamentous fungus in complex with a classical nuclear localization signal
title_full Structure of importin-α from a filamentous fungus in complex with a classical nuclear localization signal
title_fullStr Structure of importin-α from a filamentous fungus in complex with a classical nuclear localization signal
title_full_unstemmed Structure of importin-α from a filamentous fungus in complex with a classical nuclear localization signal
title_sort Structure of importin-α from a filamentous fungus in complex with a classical nuclear localization signal
author Bernardes, Natalia E. [UNESP]
author_facet Bernardes, Natalia E. [UNESP]
Takeda, Agnes A. S. [UNESP]
Dreyer, Thiago R. [UNESP]
Freitas, Fernanda Z. [UNESP]
Bertolini, Maria Célia [UNESP]
Fontes, Marcos R. M. [UNESP]
author_role author
author2 Takeda, Agnes A. S. [UNESP]
Dreyer, Thiago R. [UNESP]
Freitas, Fernanda Z. [UNESP]
Bertolini, Maria Célia [UNESP]
Fontes, Marcos R. M. [UNESP]
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (UNESP)
dc.contributor.author.fl_str_mv Bernardes, Natalia E. [UNESP]
Takeda, Agnes A. S. [UNESP]
Dreyer, Thiago R. [UNESP]
Freitas, Fernanda Z. [UNESP]
Bertolini, Maria Célia [UNESP]
Fontes, Marcos R. M. [UNESP]
description Neurospora crassa is a filamentous fungus that has been extensively studied as a model organism for eukaryotic biology, providing fundamental insights into cellular processes such as cell signaling, growth and differentiation. To advance in the study of this multicellular organism, an understanding of the specific mechanisms for protein transport into the cell nucleus is essential. Importin-α (Imp-α) is the receptor for cargo proteins that contain specific nuclear localization signals (NLSs) that play a key role in the classical nuclear import pathway. Structures of Imp-α from different organisms (yeast, rice, mouse, and human) have been determined, revealing that this receptor possesses a conserved structural scaffold. However, recent studies have demonstrated that the Impα mechanism of action may vary significantly for different organisms or for different isoforms from the same organism. Therefore, structural, functional, and biophysical characterization of different Impα proteins is necessary to understand the selectivity of nuclear transport. Here, we determined the first crystal structure of an Impα from a filamentous fungus which is also the highest resolution Impα structure already solved to date (1.75 Å). In addition, we performed calorimetric analysis to determine the affinity and thermodynamic parameters of the interaction between Impαand the classical SV40 NLS peptide. The comparison of these data with previous studies on Impα proteins led us to demonstrate that N. crassa Imp-α possess specific features that are distinct from mammalian Imp-α but exhibit important similarities to rice Imp-α, particularly at the minor NLS binding site.
publishDate 2015
dc.date.none.fl_str_mv 2015-06-19
2022-04-29T07:26:52Z
2022-04-29T07:26:52Z
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://dx.doi.org/10.1371/journal.pone.0124970
PLoS ONE, v. 10, n. 6, 2015.
1932-6203
http://hdl.handle.net/11449/228107
10.1371/journal.pone.0124970
2-s2.0-84956819601
url http://dx.doi.org/10.1371/journal.pone.0124970
http://hdl.handle.net/11449/228107
identifier_str_mv PLoS ONE, v. 10, n. 6, 2015.
1932-6203
10.1371/journal.pone.0124970
2-s2.0-84956819601
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv PLoS ONE
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
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