chaperonin

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.