Editing GroEL (section)

=== Mitochondrial protein transport ===
HSP60 possesses two main responsibilities with respect to mitochondrial protein transport. It functions to [[catalyze]] the folding of proteins destined for the matrix and maintains protein in an unfolded state for transport across the inner membrane of the mitochondria.<ref name=eight>{{cite journal  |vauthors=Koll H, etal |title=Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space |journal=Cell |volume=68 |issue=6 |pages=1163–75 |date=March 1992 |pmid=1347713 |url=https://epub.ub.uni-muenchen.de/7621/1/Neupert_Walter_7621.pdf|doi=10.1016/0092-8674(92)90086-R|s2cid=7430067 }}</ref> Many proteins are targeted for processing in the matrix of the mitochondria but then are quickly exported to other parts of the cell. The hydrophobic portion HSP60 is responsible for maintaining the unfolded conformation of the protein for transmembrane transport.<ref name=eight/> Studies have shown how HSP60 binds to incoming proteins and induces conformational and structural changes. Subsequent changes in ATP concentrations hydrolyze the bonds between the protein and HSP60 which signals the protein to exit the mitochondria.<ref name=eight/> HSP60 is also capable of distinguishing between proteins designated for export and proteins destined to remain in the mitochondrial matrix by looking for an [[amphiphilic]] alpha-helix of 15-20 residues.<ref name=eight/> The existence of this sequence signals that the protein is to be exported while the absence signals that the protein is to remain in the mitochondria. The precise mechanism is not yet entirely understood.