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

(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
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References in periodicals archive ?
The chaperonin 60 encoding gene has been previously used for the identification of various Gram positive bacteria and a chaperonin sequence database containing a large collections of sequences including gene cpn60 of T.
Citarrella et al., "Elevated blood Hsp60, its structural similarities and cross-reactivity with thyroid molecules, and its presence on the plasma membrane of oncocytes point to the chaperonin as an immunopathogenic factor in Hashimoto's thyroiditis," Cell Stress and Chaperones, vol.
Bahar, "Coupling between global dynamics and signal transduction pathways: a mechanism of allostery for chaperonin GroEL," Molecular BioSystems, vol.
The same concept was further proven by using whole-cell MALDI-TOF MS spectra which identified three specific biomarkers, namely the histone-like protein HU form B, the 10 kDa chaperonin Cpn10, and the 50S ribosomal protein L24 that were found to be relatively conserved amongst the Francisella genus but enabling the distinction of subspecies owing to slight differences in their sequences [23].
Based on molecular weight, the protein band with decreased intensity is most probably the heat shock protein-60 (HSP-60) or known as chaperonin 60.
[sup][10],[11],[12] PDCD5 can also interact with other molecules such as nuclear factor-?B p65 to regulate apoptosis via small heterodimer partner protein [sup][13] and another protein, cytosolic chaperonin containing tailless complex polypeptide one, partly by inhibiting [sz]-tubulin folding.
The five genes include contactin 3 (CNTN3); Chaperonin Containing TCP1, Subunit 5 (CCT5); valyl-tRNA synthetase 2, mitochondrial (VARS2) and inositol polyphosphate-5-phosphatase J (INPP5J), Protein Phosphatase 4, Regulatory Subunit 2 (PPP4R2).
Subunits of the chaperonin CCT interact with F-actin and influence cell shape and cytoskeletal assembly.
They identified three genetic pathways that appear to be involved: the TCP-1 ring complex chaperonin, which helps proteins fold; mitochondrial electron transport chain complexes (mETC); and a suite of genes responsible for the body's circadian rhythm.
Abstract | View Record in Scopus | Cited By in Scopus (1; sequencing of the DNA (8); it is also a tool for monitoring in vivo protein folding and chaperonin activity [9].
HSP are highly conserved and ubiquitously expressed proteins and function as an intracellular chaperonin for other proteins.
(a) Cytoskeleton and Chaperonin, stress, Metabolic enzymes related proteins and folding proteins 17.1% 26.5% 24.8% Proteins associated Proteins involved in Proteins associated with detoxification cell cycle with translation and 6.8% regulation 6.8% transduction 5.1% Proteins associated Proteins associated Extracellular with membrane with biodegradative proteins 3.5% activity 5.1% metabolism 4.3% (b) Secreted 1.3% Endoplasmic Golgi 1.3% reticulum and secreted 1.3% Cytoplasmic vesicles Mitochondrial and Nuclear and 1.3% plasma membrane 4.0% cytoplasmatic 9.4% Endoplasmic Mitochondrial 16.3% Cytoplasmatic 50.2% reticulum lumen 14.9%