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- W2588896236 abstract "The term 'Anfinsen cage' was introduced to describe anessential feature of the mechanism by which membersof the chaperonin family of molecular chaperonesincrease the yield of correctly folded polypeptide chains[1]. Anfinsen's classical experiments on the refolding ofpure denatured proteins demonstrated that polypeptidechains can self-assemble spontaneously in the test tube,in the absence of other macromolecules or energyexpenditure [2]. Recent evidence shows, however, thatprotein folding in the cell requires interactions withpre-existing proteins that act as molecular chaperones[3], some of which hydrolyse ATP. These chaperonesdo not provide steric information for folding, butinstead prevent, and possibly also reverse, the unproduct-ive side-reactions that would otherwise result in non-functional conformations - hence the aptness of theterm 'molecular chaperone'.The initial steps in protein folding, as the polypeptidechain emerges from the ribosome, are controlled by smallchaperones of the hsp70/DnaJ/GrpE type, whereas atleast some of the later folding steps occur inside 'cages'formed by the large oligomeric protein, chaperonin 60[4]. These later steps are believed to resemble those occur-ring in the test tube in an Anfinsen refolding experiment- hence the term 'Anfinsen cage' is used to describe thestructure responsible. It is not yet clear whether the finalsteps in folding to the native form occur inside or outsidethe cage: this may vary between proteins with differentintrinsic folding rates (which can vary over a one-hundred-fold range).It seems that chaperonins are required to assist proteinfolding in vivo because of two problems. Firstly, linearpolypeptide chains collapse very rapidly into flexiblecompact structures that are intermediates in the foldingprocess. These compact intermediates present hydrophobicsurfaces that can aggregate together to form insoluble com-plexes which are incapable of progressing to the final nativeconformation. The extent of this problem varies with thepolypeptide, but it is increased by both the high concentra-tion of folding chains and the temperatures found insidecells. The second problem is that some folding intermediatesdo not aggregate, but appear to be kinetically trapped in astable misfolded conformation: they cannot progress to thenative state without binding to chaperonin 60 [5]. So howdoes chaperonin 60, and the related chaperonin 10, over-come these problems, considering that strong genetic evi-dence [6] supports the biochemical data from studies in vitroin showing that the chaperonins assist the folding of manyunrelated polypeptides in living cells?Recent experiments from Hartl's laboratory [7], combinedwith earlier studies, suggest a mechanism (see Fig. 1); themodel should, at this stage, be regarded as a workinghypothesis to stimulate further experimentation.Chaperonin 60 (GroEL in Escherichia col) assembles intotwo stacked rings of seven 60kD subunits, each of whichhas ATPase activity. Each ring encloses a central cage withdimensions of about 5x7nm. Chaperonin 10 (GroES inE. colt) assembles into a single ring of seven 10kD subunits[8]. Under most experimental conditions, one molecule ofchaperonin 10 binds to one end of the chaperonin 60oligomer, in the presence of Mg" @default.
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- W2588896236 date "1994-01-01" @default.
- W2588896236 modified "2023-09-27" @default.
- W2588896236 title "Opening and closing the Anfinsen cage Dynamic interactions between chaperonins allow newly synthesized polypeptides to begin correct folding inside a transiently closed cage. Specialized chaperonins may be used to deal with recalcitrant proteins." @default.
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