Molecular Chaperones and Mitochondrial Protein Folding

摘要: Precursor proteins destined for the mitochondrial matrix traverse inner and outer organelle membranes in an extended conformation. Translocation events are therefore integrally coupled to processes of protein unfolding cytosol refolding matrix. To successfully import from cytoplasm into mitochondria, cells have recruited a variety molecular chaperone systems folding catalysts. Within organelles, Hsp70 (mt-Hsp70) is major player this process exerts multiple functions. First, mt-Hsp70 binds together with cohort incoming polypeptide chains, thus conferring unidirectionality on translocation process, then assists their refolding. A subset imported requires additional assistance by chaperonins Hsp60/Hsp10 family. Protein occurs within cavity these cylindrical complexes. productive interaction precursor chaperones not only crucial correct assembly, but also processing presequences, intramitochondrial sorting, degradation proteins. This review focuses role discusses recent findings mechanism action.