Abstract
Prefoldin is a hetero-hexameric ATP-independent chaperone, shared by eukaryotes and archaea, which binds non-native proteins preventing them from aggregation. We report the identification and characterization in vivo and in vitro of the first prefoldin from a crenarchaeon, the hyperthermophile Sulfolobus solfataricus. A functional complex was obtained either co-expressing the α- and β-prefoldin subunits in Escherichia coli, or incubating at high temperature the separately expressed subunits. In S. solfataricus, prefoldin expression and apparent molecular weight were not affected by either heat or cold shock.
Keywords: Chaperone, archaea, protein folding, protein synthesis, thermophiles
Protein & Peptide Letters
Title: The Prefoldin of the Crenarchaeon Sulfolobus solfataricus
Volume: 15 Issue: 10
Author(s): Anna D'Amaro, Anna Valenti, Alessandra Napoli, Mose Rossi and Maria Ciaramella
Affiliation:
Keywords: Chaperone, archaea, protein folding, protein synthesis, thermophiles
Abstract: Prefoldin is a hetero-hexameric ATP-independent chaperone, shared by eukaryotes and archaea, which binds non-native proteins preventing them from aggregation. We report the identification and characterization in vivo and in vitro of the first prefoldin from a crenarchaeon, the hyperthermophile Sulfolobus solfataricus. A functional complex was obtained either co-expressing the α- and β-prefoldin subunits in Escherichia coli, or incubating at high temperature the separately expressed subunits. In S. solfataricus, prefoldin expression and apparent molecular weight were not affected by either heat or cold shock.
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Cite this article as:
D'Amaro Anna, Valenti Anna, Napoli Alessandra, Rossi Mose and Ciaramella Maria, The Prefoldin of the Crenarchaeon Sulfolobus solfataricus, Protein & Peptide Letters 2008; 15 (10) . https://dx.doi.org/10.2174/092986608786071094
DOI https://dx.doi.org/10.2174/092986608786071094 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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