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Human Hsp60 with its mitochondrial import signal occurs in solution as heptamers and tetradecamers remarkably stable over a wide range of concentrations.
Vilasi, Silvia; Carrotta, Rita; Mangione, Maria Rosalia; Campanella, Claudia; Librizzi, Fabio; Randazzo, Loredana; Martorana, Vincenzo; Marino Gammazza, Antonella; Ortore, Maria Grazia; Vilasi, Annalisa; Pocsfalvi, Gabriella; Burgio, Giosalba; Corona, Davide; Palumbo Piccionello, Antonio; Zummo, Giovanni; Bulone, Donatella; Conway de Macario, Everly; Macario, Alberto J L; San Biagio, Pier Luigi; Cappello, Francesco.
Afiliação
  • Vilasi S; Institute of Biophysics, National Research Council, Palermo, Italy.
  • Carrotta R; Institute of Biophysics, National Research Council, Palermo, Italy.
  • Mangione MR; Institute of Biophysics, National Research Council, Palermo, Italy.
  • Campanella C; Department of Experimental Biomedicine and Clinical Neurosciences, University of Palermo, Palermo, Italy; Euro-Mediterranean Institute of Science and Technology, Palermo, Italy.
  • Librizzi F; Institute of Biophysics, National Research Council, Palermo, Italy.
  • Randazzo L; Institute of Biophysics, National Research Council, Palermo, Italy.
  • Martorana V; Institute of Biophysics, National Research Council, Palermo, Italy.
  • Marino Gammazza A; Department of Experimental Biomedicine and Clinical Neurosciences, University of Palermo, Palermo, Italy; Euro-Mediterranean Institute of Science and Technology, Palermo, Italy.
  • Ortore MG; Department of Life and Environmental Sciences and National Interuniversity Consortium for the Physical Sciences of Matter, Marche Polytechnic University, Ancona, Italy.
  • Vilasi A; Institute of Biosciences and Bioresources, National Research Council, Napoli, Italy.
  • Pocsfalvi G; Institute of Biosciences and Bioresources, National Research Council, Napoli, Italy.
  • Burgio G; Department of biological chemical and pharmaceutical sciences and technologies, University of Palermo, Palermo, Italy.
  • Corona D; Department of biological chemical and pharmaceutical sciences and technologies, University of Palermo, Palermo, Italy.
  • Palumbo Piccionello A; Institute of Biophysics, National Research Council, Palermo, Italy; Department of biological chemical and pharmaceutical sciences and technologies, University of Palermo, Palermo, Italy.
  • Zummo G; Department of Experimental Biomedicine and Clinical Neurosciences, University of Palermo, Palermo, Italy.
  • Bulone D; Institute of Biophysics, National Research Council, Palermo, Italy.
  • Conway de Macario E; Department of Microbiology and Immunology, School of Medicine, University of Maryland at Baltimore, and Institute of Marine and Environmental Technology, Columbus Center, Baltimore, Maryland, United States of America.
  • Macario AJ; Euro-Mediterranean Institute of Science and Technology, Palermo, Italy; Department of Microbiology and Immunology, School of Medicine, University of Maryland at Baltimore, and Institute of Marine and Environmental Technology, Columbus Center, Baltimore, Maryland, United States of America.
  • San Biagio PL; Institute of Biophysics, National Research Council, Palermo, Italy.
  • Cappello F; Institute of Biophysics, National Research Council, Palermo, Italy; Department of Experimental Biomedicine and Clinical Neurosciences, University of Palermo, Palermo, Italy; Euro-Mediterranean Institute of Science and Technology, Palermo, Italy.
PLoS One ; 9(5): e97657, 2014.
Article em En | MEDLINE | ID: mdl-24830947
ABSTRACT
It has been established that Hsp60 can accumulate in the cytosol in various pathological conditions, including cancer and chronic inflammatory diseases. Part or all of the cytosolic Hsp60 could be naïve, namely, bear the mitochondrial import signal (MIS), but neither the structure nor the in solution oligomeric organization of this cytosolic molecule has still been elucidated. Here we present a detailed study of the structure and self-organization of naïve cytosolic Hsp60 in solution. Results were obtained by different biophysical methods (light and X ray scattering, single molecule spectroscopy and hydrodynamics) that all together allowed us to assay a wide range of concentrations of Hsp60. We found that Naïve Hsp60 in aqueous solution is assembled in very stable heptamers and tetradecamers at all concentrations assayed, without any trace of monomer presence.
Assuntos

Texto completo: 1 Coleções: 01-internacional Temas: Geral Base de dados: MEDLINE Assunto principal: Chaperonina 60 / Proteínas Mitocondriais / Mitocôndrias Limite: Humans Idioma: En Revista: PLoS One Assunto da revista: CIENCIA / MEDICINA Ano de publicação: 2014 Tipo de documento: Article País de afiliação: Itália

Texto completo: 1 Coleções: 01-internacional Temas: Geral Base de dados: MEDLINE Assunto principal: Chaperonina 60 / Proteínas Mitocondriais / Mitocôndrias Limite: Humans Idioma: En Revista: PLoS One Assunto da revista: CIENCIA / MEDICINA Ano de publicação: 2014 Tipo de documento: Article País de afiliação: Itália