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 ?
Analysis of the interaction between the eukaryotic chaperonin CCT and its substrates actin and tubulin.
Chaperonins not only protect proteins against stress conditions that cause denaturation but also bind to unfolded proteins to help them fold into their active conformations.
One class of chaperone molecules, called chaperonins, performs the important task of shepherding newly made proteins away from each other and helping them fold into the correct shape.
Streptococcus suis serotypes characterized by analysis of chaperonin 60 gene sequences.
Characterization and over-expression of chaperonin t-complex proteins in colorectal cancer.
The chaperonin containing TCP-1 is a heterooligomeric particle needed to fold the cytoskeletal proteins tubulin and actin (Sternlicht et al.
Streptoccus iniae, a human and anima pathogen: specific identification by the chaperonin 60 gene identification method.
13 NATURE, he and his colleagues describe the structure of a bacterial chaperonin, GroEL.
Cell stress proteins as modulators of bacteria-host interactions 141 Chaperonin 60 and macrophage activation
by direct sequencing of PCR-amplified cpn60 sequences and comparison to cpnDB, a chaperonin reference sequence database.
Recent findings suggest that all PDC family members act as cochaperones with the cytosolic chaperonin complex to assist in the folding of a variety of proteins, including actins, tubulins, and regulators of the cell cycle (Stirling et al.