title: Normal protein folding machinery.
abstract: A highly conserved protein folding machine has been maintained in the cytosol of both prokaryotic and eukaryotic organisms and in eukaryotic mitochondria. Homologous components of this machinery have also been identified in other organelles such as the endoplasmic reticulum in which HSP70 and DnaJ-like homologs reside. The high degree of conservation presumably reflects the proficiency with which these molecules have evolved to mediate the folding of proteins to their native functional states.
authors.affiliation: Department of Biochemistry and Molecular Biology, University of Melbourne, Parkville, Victoria, Australia.
authors.forename: D
authors.initials: D
authors.lastname: Hartman
authors.forename: M J
authors.initials: MJ
authors.lastname: Gething
mesh_terms: D004721:Endoplasmic Reticulum / Q000737:chemistry; D005057:Eukaryotic Cells / Q000378:metabolism; D050956:HSP40 Heat-Shock Proteins; D006360:Heat-Shock Proteins / Q000378:metabolism; D008928:Mitochondria / Q000737:chemistry; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D050956:HSP40 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones