Regulatory role of the 90-kDa-heat-shock protein (Hsp90) and associated factors on gene expression
The term molecular chaperone was first used to describe the ability of nucleoplasmin to prevent the aggregation of histones with DNA during the assembly of nucleosomes. Subsequently, the name was extended to proteins that mediate the post-translational assembly of oligomeric complexes protecting the...
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paper:paper_18749399_v1839_n2_p71_Erlejman2023-06-08T16:30:08Z Regulatory role of the 90-kDa-heat-shock protein (Hsp90) and associated factors on gene expression Lagadari, Mariana HDAC6 Hsp90 Immunophilin Pih1 SmyD Tah1 chaperone DNA heat shock protein 90 histone deacetylase 6 immunophilin protein protein bcl 6 protein kinase SmyD protein unclassified drug cancer therapy epigenetics gene expression genetic stability human molecular evolution nonhuman priority journal protein function protein modification review transcription regulation HDAC6 Hsp90 Immunophilin Pih1 SmyD Tah1 Animals Gene Expression Regulation HSP90 Heat-Shock Proteins Humans Models, Genetic Molecular Chaperones Protein Binding Transcription Factors The term molecular chaperone was first used to describe the ability of nucleoplasmin to prevent the aggregation of histones with DNA during the assembly of nucleosomes. Subsequently, the name was extended to proteins that mediate the post-translational assembly of oligomeric complexes protecting them from denaturation and/or aggregation. Hsp90 is a 90-kDa molecular chaperone that represents the major soluble protein of the cell. In contrast to most conventional chaperones, Hsp90 functions as a refined sensor of protein function and its principal role in the cell is to facilitate biological activity to properly folded client proteins that already have a preserved tertiary structure. Consequently, Hsp90 is related to basic cell functions such as cytoplasmic transport of soluble proteins, translocation of client proteins to organelles, and regulation of the biological activity of key signaling factors such as protein kinases, ubiquitin ligases, steroid receptors, cell cycle regulators, and transcription factors. A growing amount of evidence links the protective action of this molecular chaperone to mechanisms related to posttranslational modifications of soluble nuclear factors as well as histones. In this article, we discuss some aspects of the regulatory action of Hsp90 on transcriptional regulation and how this effect could have impacted genetic assimilation mechanism in some organisms. © 2013 Elsevier B.V. Fil:Lagadari, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2014 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_18749399_v1839_n2_p71_Erlejman http://hdl.handle.net/20.500.12110/paper_18749399_v1839_n2_p71_Erlejman |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
HDAC6 Hsp90 Immunophilin Pih1 SmyD Tah1 chaperone DNA heat shock protein 90 histone deacetylase 6 immunophilin protein protein bcl 6 protein kinase SmyD protein unclassified drug cancer therapy epigenetics gene expression genetic stability human molecular evolution nonhuman priority journal protein function protein modification review transcription regulation HDAC6 Hsp90 Immunophilin Pih1 SmyD Tah1 Animals Gene Expression Regulation HSP90 Heat-Shock Proteins Humans Models, Genetic Molecular Chaperones Protein Binding Transcription Factors |
| spellingShingle |
HDAC6 Hsp90 Immunophilin Pih1 SmyD Tah1 chaperone DNA heat shock protein 90 histone deacetylase 6 immunophilin protein protein bcl 6 protein kinase SmyD protein unclassified drug cancer therapy epigenetics gene expression genetic stability human molecular evolution nonhuman priority journal protein function protein modification review transcription regulation HDAC6 Hsp90 Immunophilin Pih1 SmyD Tah1 Animals Gene Expression Regulation HSP90 Heat-Shock Proteins Humans Models, Genetic Molecular Chaperones Protein Binding Transcription Factors Lagadari, Mariana Regulatory role of the 90-kDa-heat-shock protein (Hsp90) and associated factors on gene expression |
| topic_facet |
HDAC6 Hsp90 Immunophilin Pih1 SmyD Tah1 chaperone DNA heat shock protein 90 histone deacetylase 6 immunophilin protein protein bcl 6 protein kinase SmyD protein unclassified drug cancer therapy epigenetics gene expression genetic stability human molecular evolution nonhuman priority journal protein function protein modification review transcription regulation HDAC6 Hsp90 Immunophilin Pih1 SmyD Tah1 Animals Gene Expression Regulation HSP90 Heat-Shock Proteins Humans Models, Genetic Molecular Chaperones Protein Binding Transcription Factors |
| description |
The term molecular chaperone was first used to describe the ability of nucleoplasmin to prevent the aggregation of histones with DNA during the assembly of nucleosomes. Subsequently, the name was extended to proteins that mediate the post-translational assembly of oligomeric complexes protecting them from denaturation and/or aggregation. Hsp90 is a 90-kDa molecular chaperone that represents the major soluble protein of the cell. In contrast to most conventional chaperones, Hsp90 functions as a refined sensor of protein function and its principal role in the cell is to facilitate biological activity to properly folded client proteins that already have a preserved tertiary structure. Consequently, Hsp90 is related to basic cell functions such as cytoplasmic transport of soluble proteins, translocation of client proteins to organelles, and regulation of the biological activity of key signaling factors such as protein kinases, ubiquitin ligases, steroid receptors, cell cycle regulators, and transcription factors. A growing amount of evidence links the protective action of this molecular chaperone to mechanisms related to posttranslational modifications of soluble nuclear factors as well as histones. In this article, we discuss some aspects of the regulatory action of Hsp90 on transcriptional regulation and how this effect could have impacted genetic assimilation mechanism in some organisms. © 2013 Elsevier B.V. |
| author |
Lagadari, Mariana |
| author_facet |
Lagadari, Mariana |
| author_sort |
Lagadari, Mariana |
| title |
Regulatory role of the 90-kDa-heat-shock protein (Hsp90) and associated factors on gene expression |
| title_short |
Regulatory role of the 90-kDa-heat-shock protein (Hsp90) and associated factors on gene expression |
| title_full |
Regulatory role of the 90-kDa-heat-shock protein (Hsp90) and associated factors on gene expression |
| title_fullStr |
Regulatory role of the 90-kDa-heat-shock protein (Hsp90) and associated factors on gene expression |
| title_full_unstemmed |
Regulatory role of the 90-kDa-heat-shock protein (Hsp90) and associated factors on gene expression |
| title_sort |
regulatory role of the 90-kda-heat-shock protein (hsp90) and associated factors on gene expression |
| publishDate |
2014 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_18749399_v1839_n2_p71_Erlejman http://hdl.handle.net/20.500.12110/paper_18749399_v1839_n2_p71_Erlejman |
| work_keys_str_mv |
AT lagadarimariana regulatoryroleofthe90kdaheatshockproteinhsp90andassociatedfactorsongeneexpression |
| _version_ |
1768543203786489856 |