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 …

Heat-shock protein (Hsp) 60 chaperones are almost ubiquitous and almost always essential.
They can be divided on the basis of sequence homology into two broad types: group I (found …

A survey of archaeal genomes for the presence of homologues of bacterial and eukaryotic
chaperones reveals several interesting features. All archaea contain chaperonins, also …

Chaperonins are multisubunit double-ring complexes that mediate the folding of nascent
proteins [1, 2]. In bacteria, chaperonins are homo-oligomeric and are composed of seven …

The halophilic archaeon Haloferax volcanii has three genes encoding type II chaperonins,
named cct1, cct2 and cct3. We show here that the three CCT proteins are all expressed but …

Two classes of chaperonins are known in all groups of organisms to participate in the folding
of newly synthesized proteins. Whereas bacterial type I chaperonins use a reversibly …

It is now well understood that, although proteins fold spontaneously (in a thermodynamic
sense), many nevertheless require the assistance of helpers called molecular chaperones to …

The chaperonin from the acidothermopilic archaeon, Sulfolobussp. Strain 7, is composed of
two kinds of subunits designated as Scpα and Scpβ. In this study, we characterized the …

The purification and characterization of a new type of thermostable chaperonin from the
archaebacterium Sulfolobus solfataricus is described. The chaperonin forms a hetero …

Two distantly related classes of cylindrical chaperonin complexes assist in the folding of
newly synthesized and stress-denatured proteins in an ATP-dependent manner. Group I …