The field covered in this review is new; the first sequence of a gene encoding the molecular
chaperone Hsp70 and the first description of a chaperonin in the archaea were reported in …

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

A major finding within the field of archaea and molecular chaperones has been the
demonstration that, while some species have the stress (heat-shock) gene hsp70 (dnaK) …

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 …

[Frontiers in Bioscience 6, d262-283, February 1, 2001] 262 THE MOLECULAR CHAPERONE
SYSTEM AND OTHER ANTI-STRESS MECHANISMS IN A Page 1 [Frontiers in Bioscience 6 …

Acquired thermotolerance, the associated synthesis of heat-shock proteins (HSPs) under
stress conditions, and the role of HSPs as molecular chaperones under normal growth …

The major heat shock proteins in the archaeon Sulfolobus shibatae are similar to the
cytosolic eukaryotic chaperonin and form an 18-subunit bitoroidal complex. Two sequence …

ne of the most abundant proteins in the hyperthermophilic archaeonSulfolobus shibataeis
the 59 kDa heat shock protein (TF55) that is believed to form a homo-oligomeric double ring …

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 …

Chaperonins are multisubunit protein-folding assemblies. They are composed of two distinct
structural classes, which also have a characteristic phylogenetic distribution. Group I …