Gene expression regulation by heat-shock proteins: the cardinal roles of HSF1 and Hsp90

Autores
Mazaira, Gisela Ileana; Daneri Becerra, Cristina del Rosario; Zgajnar, Nadia Romina; Lotufo, Cecilia Maricel; Galigniana, Mario Daniel
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The ability to permit gene expression is managed by a set of relatively well known regulatory mechanisms. Nonetheless, such property can also be acquired during the life span as a consequence of environmental stimuli. Interestingly, some acquired information can be passed to the next generation of individuals without modifying gene information, but instead, the manner cells read and process such information. Molecular chaperones are classically related to the proper preservation of protein folding and anti-aggregation properties, but one of them, Hsp90, is a refined sensor of protein function facilitating the biological activity of properly folded client proteins that already have a preserved tertiary structure. Interestingly, Hsp90 can also function as a critical switch able to regulate biological responses due to its association to key client proteins such as histone deacetylases or DNA methylases. Thus, a growing amount of evidence has connected the action of Hsp90 to post-translational modifications of soluble nuclear factors, DNA, and histones, which epigenetically affects gene expression upon the onset of an unfriendly environment. Such response is commanded by the activation of the transcription factor HSF1. Even though a great number of stresses of diverse nature are known to trigger the stress response by activation of HSF1, it is still unanswered whether there are different types of molecular sensors for each type of stimulus. In this article, we will discuss various aspects of the regulatory action of HSF1 and Hsp90 on transcriptional regulation, and how this regulation may impact genetic assimilation mechanisms and the health of individuals.
Fil: Mazaira, Gisela Ileana. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Fil: Daneri Becerra, Cristina del Rosario. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina
Fil: Zgajnar, Nadia Romina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina
Fil: Lotufo, Cecilia Maricel. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina
Fil: Galigniana, Mario Daniel. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina
Materia
Immunophilins
Hsp90
Hsf1
Chaperones
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/63722
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/63722
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Gene expression regulation by heat-shock proteins: the cardinal roles of HSF1 and Hsp90Mazaira, Gisela IleanaDaneri Becerra, Cristina del RosarioZgajnar, Nadia RominaLotufo, Cecilia MaricelGaligniana, Mario DanielImmunophilinsHsp90Hsf1Chaperoneshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The ability to permit gene expression is managed by a set of relatively well known regulatory mechanisms. Nonetheless, such property can also be acquired during the life span as a consequence of environmental stimuli. Interestingly, some acquired information can be passed to the next generation of individuals without modifying gene information, but instead, the manner cells read and process such information. Molecular chaperones are classically related to the proper preservation of protein folding and anti-aggregation properties, but one of them, Hsp90, is a refined sensor of protein function facilitating the biological activity of properly folded client proteins that already have a preserved tertiary structure. Interestingly, Hsp90 can also function as a critical switch able to regulate biological responses due to its association to key client proteins such as histone deacetylases or DNA methylases. Thus, a growing amount of evidence has connected the action of Hsp90 to post-translational modifications of soluble nuclear factors, DNA, and histones, which epigenetically affects gene expression upon the onset of an unfriendly environment. Such response is commanded by the activation of the transcription factor HSF1. Even though a great number of stresses of diverse nature are known to trigger the stress response by activation of HSF1, it is still unanswered whether there are different types of molecular sensors for each type of stimulus. In this article, we will discuss various aspects of the regulatory action of HSF1 and Hsp90 on transcriptional regulation, and how this regulation may impact genetic assimilation mechanisms and the health of individuals.Fil: Mazaira, Gisela Ileana. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; ArgentinaFil: Daneri Becerra, Cristina del Rosario. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; ArgentinaFil: Zgajnar, Nadia Romina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; ArgentinaFil: Lotufo, Cecilia Maricel. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; ArgentinaFil: Galigniana, Mario Daniel. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; ArgentinaPortland Press2017-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/63722Mazaira, Gisela Ileana; Daneri Becerra, Cristina del Rosario; Zgajnar, Nadia Romina; Lotufo, Cecilia Maricel; Galigniana, Mario Daniel; Gene expression regulation by heat-shock proteins: the cardinal roles of HSF1 and Hsp90; Portland Press; Biochemical Society Transactions; 46; 1; 2-2017; 51-650300-5127CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.biochemsoctrans.org/content/46/1/51info:eu-repo/semantics/altIdentifier/doi/10.1042/BST20170335info:eu-repo/semantics/altIdentifier/url/29273620info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:45:56Zoai:ri.conicet.gov.ar:11336/63722instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:45:57.152CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Gene expression regulation by heat-shock proteins: the cardinal roles of HSF1 and Hsp90
title Gene expression regulation by heat-shock proteins: the cardinal roles of HSF1 and Hsp90
spellingShingle Gene expression regulation by heat-shock proteins: the cardinal roles of HSF1 and Hsp90
Mazaira, Gisela Ileana
Immunophilins
Hsp90
Hsf1
Chaperones
title_short Gene expression regulation by heat-shock proteins: the cardinal roles of HSF1 and Hsp90
title_full Gene expression regulation by heat-shock proteins: the cardinal roles of HSF1 and Hsp90
title_fullStr Gene expression regulation by heat-shock proteins: the cardinal roles of HSF1 and Hsp90
title_full_unstemmed Gene expression regulation by heat-shock proteins: the cardinal roles of HSF1 and Hsp90
title_sort Gene expression regulation by heat-shock proteins: the cardinal roles of HSF1 and Hsp90
dc.creator.none.fl_str_mv Mazaira, Gisela Ileana
Daneri Becerra, Cristina del Rosario
Zgajnar, Nadia Romina
Lotufo, Cecilia Maricel
Galigniana, Mario Daniel
author Mazaira, Gisela Ileana
author_facet Mazaira, Gisela Ileana
Daneri Becerra, Cristina del Rosario
Zgajnar, Nadia Romina
Lotufo, Cecilia Maricel
Galigniana, Mario Daniel
author_role author
author2 Daneri Becerra, Cristina del Rosario
Zgajnar, Nadia Romina
Lotufo, Cecilia Maricel
Galigniana, Mario Daniel
author2_role author
author
author
author
dc.subject.none.fl_str_mv Immunophilins
Hsp90
Hsf1
Chaperones
topic Immunophilins
Hsp90
Hsf1
Chaperones
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The ability to permit gene expression is managed by a set of relatively well known regulatory mechanisms. Nonetheless, such property can also be acquired during the life span as a consequence of environmental stimuli. Interestingly, some acquired information can be passed to the next generation of individuals without modifying gene information, but instead, the manner cells read and process such information. Molecular chaperones are classically related to the proper preservation of protein folding and anti-aggregation properties, but one of them, Hsp90, is a refined sensor of protein function facilitating the biological activity of properly folded client proteins that already have a preserved tertiary structure. Interestingly, Hsp90 can also function as a critical switch able to regulate biological responses due to its association to key client proteins such as histone deacetylases or DNA methylases. Thus, a growing amount of evidence has connected the action of Hsp90 to post-translational modifications of soluble nuclear factors, DNA, and histones, which epigenetically affects gene expression upon the onset of an unfriendly environment. Such response is commanded by the activation of the transcription factor HSF1. Even though a great number of stresses of diverse nature are known to trigger the stress response by activation of HSF1, it is still unanswered whether there are different types of molecular sensors for each type of stimulus. In this article, we will discuss various aspects of the regulatory action of HSF1 and Hsp90 on transcriptional regulation, and how this regulation may impact genetic assimilation mechanisms and the health of individuals.
Fil: Mazaira, Gisela Ileana. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Fil: Daneri Becerra, Cristina del Rosario. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina
Fil: Zgajnar, Nadia Romina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina
Fil: Lotufo, Cecilia Maricel. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina
Fil: Galigniana, Mario Daniel. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina
description The ability to permit gene expression is managed by a set of relatively well known regulatory mechanisms. Nonetheless, such property can also be acquired during the life span as a consequence of environmental stimuli. Interestingly, some acquired information can be passed to the next generation of individuals without modifying gene information, but instead, the manner cells read and process such information. Molecular chaperones are classically related to the proper preservation of protein folding and anti-aggregation properties, but one of them, Hsp90, is a refined sensor of protein function facilitating the biological activity of properly folded client proteins that already have a preserved tertiary structure. Interestingly, Hsp90 can also function as a critical switch able to regulate biological responses due to its association to key client proteins such as histone deacetylases or DNA methylases. Thus, a growing amount of evidence has connected the action of Hsp90 to post-translational modifications of soluble nuclear factors, DNA, and histones, which epigenetically affects gene expression upon the onset of an unfriendly environment. Such response is commanded by the activation of the transcription factor HSF1. Even though a great number of stresses of diverse nature are known to trigger the stress response by activation of HSF1, it is still unanswered whether there are different types of molecular sensors for each type of stimulus. In this article, we will discuss various aspects of the regulatory action of HSF1 and Hsp90 on transcriptional regulation, and how this regulation may impact genetic assimilation mechanisms and the health of individuals.
publishDate 2017
dc.date.none.fl_str_mv 2017-02
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/63722
Mazaira, Gisela Ileana; Daneri Becerra, Cristina del Rosario; Zgajnar, Nadia Romina; Lotufo, Cecilia Maricel; Galigniana, Mario Daniel; Gene expression regulation by heat-shock proteins: the cardinal roles of HSF1 and Hsp90; Portland Press; Biochemical Society Transactions; 46; 1; 2-2017; 51-65
0300-5127
CONICET Digital
CONICET
url http://hdl.handle.net/11336/63722
identifier_str_mv Mazaira, Gisela Ileana; Daneri Becerra, Cristina del Rosario; Zgajnar, Nadia Romina; Lotufo, Cecilia Maricel; Galigniana, Mario Daniel; Gene expression regulation by heat-shock proteins: the cardinal roles of HSF1 and Hsp90; Portland Press; Biochemical Society Transactions; 46; 1; 2-2017; 51-65
0300-5127
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.biochemsoctrans.org/content/46/1/51
info:eu-repo/semantics/altIdentifier/doi/10.1042/BST20170335
info:eu-repo/semantics/altIdentifier/url/29273620
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Portland Press
publisher.none.fl_str_mv Portland Press
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.070432

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