Chaperonin 10 | definition of Chaperonin 10 by Medical dictionary
chaperonin (redirected from Chaperonin 10)
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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]
n.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
Any of a family of large chaperone proteins that function chiefly to assist in the folding of newly synthesized proteins.
References in periodicals archive
Chaperonin 10 (Spot 10), found to be up-regulated in leaves of plants subjected to cool roots and hypoxia, is a calmodulin-binding protein (Yang and Poovaiah, 2000) and so may be involved in cold-signaling, as importance of calcium in cold sensing and signaling is well known (Lee et al.
Arabidopsis chloroplast chaperonin 10 is a calmodulin-binding protein.