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 …

The proteasome-activating nucleotidase (PAN) from Methanococcus jannaschii is a complex
of relative molecular mass 650,000 that is homologous to the ATPases in the eukaryotic 26S …

Chaperonins are a class of molecular chaperones that assemble into a large double ring
architecture with each ring constituting seven to nine subunits and enclosing a cavity for …

Introduction 3. Water efflux and osmosensors 3.1. Water movement 3.2. Primary sensors of
osmotic stress 3.2. 1. K+ pumps and K+ channels 3.2. 2. Msc's and VAC's 3.3. Exogenous …

[Frontiers in Bioscience 5, d796-812, September 1, 2000] OSMOADAPTATION AND
OSMOREGULATION IN ARCHAEA Mary F. Roberts Merkert Ch Page 1 6/22/2021 [Frontiers 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 …

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

Publisher Summary This chapter describes several experiments that give a qualitative feel
for how Type II chaperonins might facilitate protein folding. Imaging of CCT/actin complexes …

Chaperonins are macromolecular machines that assist in protein folding. The archaeon
Methanosarcina mazei has acquired numerous bacterial genes by horizontal gene transfer …