Artículo

Erlejman, A.G.; Lagadari, M.; Toneatto, J.; Piwien-Pilipuk, G.; Galigniana, M.D. "Regulatory role of the 90-kDa-heat-shock protein (Hsp90) and associated factors on gene expression" (2014) Biochimica et Biophysica Acta - Gene Regulatory Mechanisms. 1839(2):71-87
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Abstract:

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.

Registro:

Documento: Artículo
Título:Regulatory role of the 90-kDa-heat-shock protein (Hsp90) and associated factors on gene expression
Autor:Erlejman, A.G.; Lagadari, M.; Toneatto, J.; Piwien-Pilipuk, G.; Galigniana, M.D.
Filiación:Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires/IQUIBICEN, Argentina
Laboratorio de Receptores Nucleares, Instituto de Biología y Medicina Experimental/CONICET, Buenos Aires, Argentina
Laboratorio de Arquitectura Nuclear, Instituto de Biología y Medicina Experimental/CONICET, Buenos Aires, Argentina
Idioma: Inglés
Palabras clave:HDAC6; Hsp90; Immunophilin; Pih1; SmyD; Tah1
Año:2014
Volumen:1839
Número:2
Página de inicio:71
Página de fin:87
DOI: http://dx.doi.org/10.1016/j.bbagrm.2013.12.006
Título revista:Biochimica et Biophysica Acta - Gene Regulatory Mechanisms
Título revista abreviado:Biochim. Biophys. Acta Gene Regul. Mech.
ISSN:18749399
Registro:http://digital.bl.fcen.uba.ar/collection/paper/document/paper_18749399_v1839_n2_p71_Erlejman

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Citas:

---------- APA ----------
Erlejman, A.G., Lagadari, M., Toneatto, J., Piwien-Pilipuk, G. & Galigniana, M.D. (2014) . Regulatory role of the 90-kDa-heat-shock protein (Hsp90) and associated factors on gene expression. Biochimica et Biophysica Acta - Gene Regulatory Mechanisms, 1839(2), 71-87.
http://dx.doi.org/10.1016/j.bbagrm.2013.12.006
---------- CHICAGO ----------
Erlejman, A.G., Lagadari, M., Toneatto, J., Piwien-Pilipuk, G., Galigniana, M.D. "Regulatory role of the 90-kDa-heat-shock protein (Hsp90) and associated factors on gene expression" . Biochimica et Biophysica Acta - Gene Regulatory Mechanisms 1839, no. 2 (2014) : 71-87.
http://dx.doi.org/10.1016/j.bbagrm.2013.12.006
---------- MLA ----------
Erlejman, A.G., Lagadari, M., Toneatto, J., Piwien-Pilipuk, G., Galigniana, M.D. "Regulatory role of the 90-kDa-heat-shock protein (Hsp90) and associated factors on gene expression" . Biochimica et Biophysica Acta - Gene Regulatory Mechanisms, vol. 1839, no. 2, 2014, pp. 71-87.
http://dx.doi.org/10.1016/j.bbagrm.2013.12.006
---------- VANCOUVER ----------
Erlejman, A.G., Lagadari, M., Toneatto, J., Piwien-Pilipuk, G., Galigniana, M.D. Regulatory role of the 90-kDa-heat-shock protein (Hsp90) and associated factors on gene expression. Biochim. Biophys. Acta Gene Regul. Mech. 2014;1839(2):71-87.
http://dx.doi.org/10.1016/j.bbagrm.2013.12.006