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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/63722
Ver los metadatos del registro completo
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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 Técnicas2025-09-03T09:50:39Zoai: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:34982025-09-03 09:50:40.285CONICET 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 |
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CONICET Digital (CONICET) |
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CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
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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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13.13397 |