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Introduction Chaperonins represent a ubiquitous and essential family of
 

Summary: Introduction
Chaperonins represent a ubiquitous and essential family of
sequence and structurally related molecular chaperones
required for assisting the folding of newly synthesized, non-
native polypeptides (Hartl and Hayer-Hartl, 2002). In bacteria,
the chaperonin GroEL is implicated in folding ~10% of all
cytoplasmic proteins. Together with endosymbiotically derived
mitochondrial Hsp60 and chloroplast cpn60, chaperonins of
bacterial origin are classified as Group I (Horwich and
Willison, 1993). Their distant relatives, termed Group II
chaperonins, are found in the cytosols of eukaryotes and
archaea (Gutsche et al., 1999). The eukaryotic cytosolic
chaperonin, known as CCT, TRiC or c-cpn, interacts with a
range of substrates comparable to that of GroEL, but has also
evolved the ability to fold proteins found only in eukaryotes,
including actins and tubulins (Leroux and Hartl, 2000;
Valpuesta et al., 2002). Both Group I and II chaperonin
monomers exhibit a bilobed structure consisting of an ATPase
equatorial domain that is joined, via a small intermediate
domain, to a substrate-binding apical domain; these in turn

  

Source: Archibald, John - Department of Biochemistry and Molecular Biology, Dalhousie University

 

Collections: Biology and Medicine