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 …

In the past decade, the eubacterial group I chaperonin GroEL became the paradigm of a
protein folding machine. More recently, electron microscopy and X-ray crystallography …

Intragenomic and intergenomic comparisons of upstream nucleotide sequences of archaeal
genes were performed with the goal of predicting transcription regulatory sites (operators) …

Thermo (or hyperthermo) philic microorganisms are ubiquitous having a wide range of
habitats from freshly fallen snow to pasteurized milk to geothermal areas like hot springs …

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 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 …

The cpn60 and cpn10 genes from psychrophilic bacterium, Oleispira antarctica RB8,
showed a positive effect in Escherichia coli growth at low temperature, shifting its theoretical …

The hyperthermoacidophilic archaeon Sulfolobus shibatae contains group II chaperonins,
known as rosettasomes, which are two nine‐membered rings composed of three different 60 …

Chaperonins are cylindrical, oligomeric complexes, essential for viability and required for
the folding of other proteins. The GroE (group I) subfamily, found in eubacteria, mitochondria …

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 …