title: [CCT chaperonins and their cochaperons].
abstract: Chaperonins are large oligomers consisting of two superimposed rings, each enclosing a cavity used for the folding of other proteins. They have been divided into two groups. Chaperonins of type I were identified in mitochondria and chloroplasts (Hsp60) or bacterial cytosol (GroEL) as well. Chaperonins type II were found in Archea and the eukaryotic cell cytosol (CCT). Protein folding occurs in the chaperonin after its conformational changes induced upon ATP binding. Mechanism of the protein folding, although still poorly defined, clearly differs from the one established for GroEL. Although CCT with prefoldin seems to be mainly involved in the folding of actin and tubulin, other substrates engaged in various cellular processes are beginning to be characterized, including proteins possessing WD40-repeats. Moreover, several lines of evidence suggest that beside prefoldin, CCT may work in concert with phosducin-like proteins (PhLPs).
authors.affiliation: Zakład Biologii Komórki, Instytut Biologii Doświadczalnej im. Marcelego Nenckiego PAN, Warszawa.
authors.forename: Cezary
authors.initials: C
authors.lastname: Bregier
authors.forename: Barbara
authors.initials: B
authors.lastname: Kupikowska
authors.forename: Hanna
authors.initials: H
authors.lastname: Fabczak
authors.forename: Stanisław
authors.initials: S
authors.lastname: Fabczak
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D056404:Chaperonin Containing TCP-1; D018833:Chaperonins / Q000737:chemistry / Q000145:classification* / Q000378:metabolism; D017510:Protein Folding
chemical_list: D000255:Adenosine Triphosphate; D056404:Chaperonin Containing TCP-1; D018833:Chaperonins