chaperonin


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Related to chaperonin: GroEL

chaperonin

(shap-ĕr-ō'nin),
A molecular complex composed of multiple heat shock protein subunits that assemble into double ring structures. Chaperonins function within the cytoplasm to refold damaged proteins.
See also: heat shock proteins.
[chaperon + -in]

chaperonin

/chap·er·o·nin/ (shap″er-o´nin) any of various heat shock proteins that act as molecular chaperones in bacteria, plasmids, mitochondria, and eukaryotic cyotsol.

chaperonin

(shăp′ə-rō′nĭn)
n.
Any of a family of large chaperone proteins that function chiefly to assist in the folding of newly synthesized proteins.
Any of a group of 60 kD cytosolic chaperone proteins—e.g., heat shock protein 60, hsp60, GroEL—found in prokaryotes, the equivalent of the eukaryotic hsp60, mitochondria and plastids; chaparonins use energy from ATP hydrolysis to maintain proteins in the necessary folded configuration for proper function, thus having ‘foldase’ activity; other postulated roles for chaperonins include protein transport, oligomer assembly, DNA replication, mRNA turnover, and protection of the cell from various stresses; some chaperonins have auto-foldase activities

chaperonin

a class of chaperone proteins.
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References in periodicals archive ?
Programmed cell death protein 5 interacts with the cytosolic chaperonin containing tailless complex polypeptide 1 (CCT) to regulate [sz]-tubulin folding.
Identification of a groES-like chaperonin in mitochondria that facilitates protein folding.
The most prominent spots were identified as (Table I): thioredoxin peroxidase 2, actin (Sj), HSP70 (Sj), a disulfide isomerase homologue, chaperonin, ATP synthase, enolase, prohibitin, serpin, glyceraldehyde-3-phosphatedehydrogenase (GA3PDH) mayor larval surface antigen, citrate synthase, 14-3,3 protein, Sm21.
Eight induced proteins were identified as DnaK protein, fabG4 protein, DNA-binding protein, hypothetical protein, two 14 kDa antigen and two 10 kDa chaperonin.
However, high-resolution haplotyping in 16 kindred and mutational analysis of 37 positional candidates (266) revealed 3 genes: a neurofilament homologue (AK000210, part of FLJ20203) with potential involvement in regulation of kidney morphogenesis (266,267); SCAMP3, a gene encoding endocytosis/membrane trafficking protein downstream of epidermal growth factor receptor (268); and CCT3, a gene encoding chaperonin, for which interactions with tubulin (269) and inversin (NPHP2) (270) have been described.
Topics addressed in the 14 included presentations are the history of the understanding of cell stress; systems biology of molecular chaperone networks; unusual cellular disposition of the mitochondrial chaperones Hsp60, Hsp70, and Hsp10; cell surface molecular chaperones as endogenous modulators of innate immune response; cell stress proteins in extracellular fluids; Hsp60 and the immune system; novel immunotherapies from cell stress proteins; cell stress proteins as modulators of bacteria-host interactions; chaperonin 60 and microphage activation; extracellular functions of thioredoxin; Hsp27 as an anti-inflammatory and immunomodulatory stress protein acting to dampen immune function; and binding immunoglobulin protein as a potential new therapy for the treatment of rheumatoid arthritis.
XToll, a recombinant chaperonin 10 as an anti-inflammatory immunomodulator.
The lower hydrolysis of ATP by the stress protein GroEL is a major factor responsible for the diminished chaperonin activity at low temperature.
Members of the chaperonin family have been shown to increase in response to heat shock and oxidative stresses and aid in protein folding (Nishimura, 1998).
In an effort to examine the location and the conformational properties of a polypeptide chain substrate chaperonin complexes, SANS experiments with contrast variation were undertaken at the NCNR by CARB (Center for Advanced Research in Biotechnology) and NCNR scientists, using a 86 % deuterated nonnative.
The release of the protein into the cavity and its folding occurred even with the altered amino acid in GroEL, but the mature protein remained trapped inside the chaperonin cage.
Published by John Wiley and Sons Ltd, Protein Chaperones and Protection from Neurodegenerative Diseases addresses the chaperone and anti-chaperone properties of various proteins such as alpha-synuclein, Hsp70, Hsp104, and Hsc90, Chaperonin and TRiC; ER stress and chaperone production; as well as emerging areas such as torsin A and its possible role in neurodegeneration -and all from both research and clinical perspectives.