Editing GroEL (section)

== Synthesis and assembly ==
HSP60 is typically found in the mitochondria and has been found in organelles of endosymbiotic origin. HSP60 monomers form two heptameric rings that bind to the surface of linear proteins and catalyze their folding in an ATP dependent process.<ref name=thirteen>{{cite journal  |vauthors=Itoh H, etal |title=Mammalian HSP60 is quickly sorted into the mitochondria under conditions of dehydration |journal=Eur. J. Biochem. |volume=269 |issue=23 |pages=5931–8 |date=December 2002 |pmid=12444982 |doi= 10.1046/j.1432-1033.2002.03317.x}}</ref> HSP60 subunits are encoded by nuclear [[genes]] and translated into the cytosol. These subunits then move into the mitochondria where they are processed by other HSP60 molecules.<ref name=four/> Several studies have shown how HSP60 proteins must be present in the mitochondria for the synthesis and assembly of additional HSP60 components.<ref name=four/> There is a direct positive correlation between the presence of HSP60 proteins in the mitochondria and the production of additional HSP60 protein complexes.
	
The [[enzyme kinetics|kinetics]] of assembly of HSP60 subunits into the 2-heptameric rings takes two minutes. The subsequent [[protease]]-resistant HSP60 is formed in a half-time of 5–10 minutes.<ref name=four/> This rapid synthesis indicates that there is an ATP-dependent interaction where the formed HSP60 complex stabilizes the intermediate of the HSP60 assembly complex, effectively serving as a catalyst.<ref name=four/> The necessity of preexisting HSP60 in order to synthesize additional HSP60 molecules supports the [[endosymbiotic theory]] of the origin of [[mitochondria]]. There must have been a rudimentary prokaryotic homologous protein that was capable of similar self-assembly.