Chaperonin, also known as heat shock protein 60 (Hsp60), belongs to an evolutionarily
conserved protein family that enables cells to survive under stressful conditions, including …

Publisher Summary Chaperonins are a group of molecular chaperones that are classified
into the GroEL/HSP60 (heat shock protein 60) family. They are widely distributed from …

Chaperonins are a type of molecular chaperone that assist in the folding of proteins. Group II
chaperonins play an important role in the proteostasis in the cytosol of archaea and eukarya …

Molecular chaperonins are present in all three domains of life and assist the folding of a
considerable portion of nascent proteins in the cell. They are also known to promote the …

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 …

Thermococcus kodakarensis grows optimally at 85° C and possesses two chaperonins, cold-
inducible CpkA and heat-inducible CpkB, which are involved in adaptation to low and high …

Chaperonins (CPN) are ubiquitous oligomeric protein machines that mediate the ATP-
dependent folding of polypeptide chains. These chaperones have not only been assigned …

Abstract In 1973, Christian Anfinsen and coworkers noted that accelerated protein folding in
intact cells and cell extracts suggested that a “disulfide interchange enzyme” might be …

Methanococcoides burtonii is a cold-adapted archaeon isolated from permanently cold (1-
2ºC), methane saturated waters in Ace Lake, Antarctica. M. burtonii is a motile, flagellated …

To study the difference in expression of the chaperonin α‐and β‐subunits in Thermococcus
strain KS‐1 (T. KS‐1), we measured their intracellular contents at various growth …