The prefoldin of the crenarchaeon Sulfolobus solfataricus.
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.
D'Amaro
Anna
A
Institute of Protein Biochemistry, Consiglio Nazionale delle Ricerche, Via P. Castellino 111, 80131 Naples, Italy.
Valenti
Anna
A
Napoli
Alessandra
A
Rossi
Mosè
M
Ciaramella
Maria
M
D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000032:analysis / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001483:Base Sequence; D003001:Cloning, Molecular; D019848:Gene Expression Regulation, Archaeal; D018832:Molecular Chaperones / Q000032:analysis / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D016944:Sulfolobus / Q000235:genetics
D019843:Archaeal Proteins; D018832:Molecular Chaperones; C112806:prefoldin