Categories of chaperonins Chaperonin

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thermosome chaperonin ii, hetero16mer, sulfolobus solfataricus.


group ii chaperonins, found in eukaryotic cytosol , in archaea, more poorly characterized.


tric (tcp-1 ring complex, called cct chaperonin containing tcp-1), eukaryotic chaperonin, composed of 2 rings of 8 different though related subunits, each thought represented once per eight-membered ring. tric thought fold cytoskeletal proteins actin , tubulin known fold dozens of substrates.


mm cpn (methanococcus maripaludis chaperonin), found in archaea methanococcus maripaludis, composed of sixteen identical subunits (eight per ring). has been shown fold mitochondrial protein rhodanese; however, no natural substrates have yet been identified.


group ii chaperonins not thought utilize groes-type cofactor fold substrates. instead contain built-in lid closes in atp-dependent manner encapsulate substrates, process required optimal protein folding activity.








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