A novel aminopeptidase associated with the 60 kDa chaperonin in the thermophilic archaeon Sulfolobus solfataricus
The chaperonins are high‐molecular‐weight protein complexes having a characteristic
double‐ring toroidal shape; they are thought to aid the folding of denatured or newly …
double‐ring toroidal shape; they are thought to aid the folding of denatured or newly …
cpnDB: a chaperonin sequence database
JE Hill, SL Penny, KG Crowell, SH Goh… - Genome …, 2004 - genome.cshlp.org
Type I chaperonins are molecular chaperones present in virtually all bacteria, some archaea
and the plastids and mitochondria of eukaryotes. Sequences of cpn 60 genes, encoding 60 …
and the plastids and mitochondria of eukaryotes. Sequences of cpn 60 genes, encoding 60 …
[图书][B] Prokaryotic Chaperonins: Multiple Copies and Multitude Functions
Chaperonins are a fascinating class of molecular chaperones that form a double toroidal
architecture, consisting of two isologous rings of 7–9 subunits, each with a large central …
architecture, consisting of two isologous rings of 7–9 subunits, each with a large central …
Protein‐Folding Systems
This chapter describes the known members of archaeal protein‐folding pathways, including
not only the heat‐shock‐regulated members, but also the non‐heat‐shock‐regulated protein …
not only the heat‐shock‐regulated members, but also the non‐heat‐shock‐regulated protein …
Isolation and Characterization of a Second Subunit of Molecular Chaperonin from Pyrococcus kodakaraensis KOD1: Analysis of an ATPase-Deficient Mutant Enzyme
M Izumi, S Fujiwara, M Takagi, S Kanaya… - Applied and …, 1999 - Am Soc Microbiol
The cpkA gene encoding a second (α) subunit of archaeal chaperonin from Pyrococcus
kodakaraensis KOD1 was cloned, sequenced, and expressed in Escherichia coli …
kodakaraensis KOD1 was cloned, sequenced, and expressed in Escherichia coli …
Oligomerization of an archaeal group II chaperonin is mediated by N-terminal salt bridges
Group II chaperonins (Cpns) are essential mediators of cellular protein folding in eukaryotes
and archaea. They consist of two back-to-back rings forming symmetrical cavities in which …
and archaea. They consist of two back-to-back rings forming symmetrical cavities in which …
CryoEM reveals the stochastic nature of individual ATP binding events in a group II chaperonin
Y Zhao, MF Schmid, J Frydman, W Chiu - Nature Communications, 2021 - nature.com
Chaperonins are homo-or hetero-oligomeric complexes that use ATP binding and hydrolysis
to facilitate protein folding. ATP hydrolysis exhibits both positive and negative cooperativity …
to facilitate protein folding. ATP hydrolysis exhibits both positive and negative cooperativity …
[HTML][HTML] Properties of the chaperonin complex from the halophilic archaeon Haloferax volcanii
AT Large, E Kovacs, PA Lund - FEBS letters, 2002 - Elsevier
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 …
named cct1, cct2 and cct3. We show here that the three CCT proteins are all expressed but …
Chaperonins: two rings for folding
H Yébenes, P Mesa, IG Muñoz, G Montoya… - Trends in biochemical …, 2011 - cell.com
Chaperonins are ubiquitous chaperones found in Eubacteria, eukaryotic organelles (group
I), Archaea and the eukaryotic cytosol (group II). They all share a common structure and a …
I), Archaea and the eukaryotic cytosol (group II). They all share a common structure and a …
Small heat shock protein of a hyperthermophilic archaeum, Thermococcus sp. strain KS-1, exists as a spherical 24 mer and its expression is highly induced under heat …
Small heat shock proteins (sHsps) are the most ubiquitous molecular chaperones. Several
sHsps have been shown to exhibit chaperone activity and protect proteins from thermal and …
sHsps have been shown to exhibit chaperone activity and protect proteins from thermal and …