The prefoldin of the crenarchaeon Sulfolobus solfataricus.

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 alpha- and beta-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.

• Authors: Anna D'Amaro, Anna Valenti, Alessandra Napoli, Mosè Rossi, Maria Ciaramella
• Journal: Protein and peptide letters (Protein Pept Lett) Vol. 15 Issue 10 Pg. 1055-62 ( 2008) ISSN: 0929-8665 [Print] Netherlands
• PMID: 19075815 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Archaeal Proteins
• Molecular Chaperones
• prefoldin

Topics

• Amino Acid Sequence
• Archaeal Proteins (analysis, chemistry, genetics, metabolism)
• Base Sequence
• Cloning, Molecular
• Gene Expression Regulation, Archaeal
• Molecular Chaperones (analysis, chemistry, genetics, metabolism)
• Molecular Sequence Data
• Sequence Alignment
• Sulfolobus (genetics)