Many archaea are extremophiles. They thrive at high temperatures, at high pressure and in
concentrated acidic environments. Nevertheless, the largest proportion and greatest …

Prefoldin is a hexameric molecular chaperone found in the cytosol of archaea and
eukaryotes. Its hexameric complex is built from two related classes of subunits and has the …

A global view of the biology of the cold‐adapted archaeon Methanococcoides burtonii was
achieved using proteomics. Proteins specific to growth at 4° C versus Topt (23° C) were …

The crystal structures of the group II chaperonins consisting of the α subunit with amino acid
substitutions of G65C and/or I125T from the hyperthermophilic archaeum Thermococcus …

Prefoldin (PFD) is a molecular chaperone that stabilizes and then delivers unfolded proteins
to a chaperonin for facilitated folding. The PFD hexamer has undergone an evolutionary …

Prefoldin is a jellyfish-shaped hexameric co-chaperone of the group II chaperonins. It
captures a protein folding intermediate and transfers it to a group II chaperonin for …

To elucidate the exact role of the helical protrusion of a group II chaperonin in its molecular
chaperone function, three deletion mutants of the chaperonin from a hyperthermophilic …

Group II chaperonins, found in archaea and in eukaryotic cytosol, do not have a co-
chaperonin corresponding to GroES. Instead, it is suggested that the helical protrusion …

Prefoldin is a molecular chaperone that captures a protein-folding intermediate and transfers
it to a group II chaperonin for correct folding. The manner by which prefoldin interacts with a …

The Hsp60 or chaperonin class of molecular chaperones is divided into two phylogenetic
groups: group I, found in bacteria, mitochondria and chloroplasts, and group II, found in …