Protein folding in vivo: the importance of molecular chaperones.
The contribution of the two major cytosolic chaperone systems, Hsp70 and the cylindrical chaperonins, to cellular protein folding has been clarified by a number of recent papers. These studies found that, in vivo, a significant fraction of newly synthesized polypeptides transit through these chaperone systems in both prokaryotic and eukaryotic cells. The identification and characterization of the cellular substrates of chaperones will be instrumental in understanding how proteins fold in vivo.
Feldman
D E
DE
Department of Biological Sciences, Stanford University, Stanford, CA 94305-5020, USA.
Frydman
J
J
D000818:Animals; D001426:Bacterial Proteins / Q000502:physiology; D018834:Chaperonin 60 / Q000502:physiology; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins; D005544:Forecasting; D018840:HSP70 Heat-Shock Proteins / Q000502:physiology; D006801:Humans; D046911:Macromolecular Substances; D008954:Models, Biological; D018832:Molecular Chaperones / Q000145:classification / Q000502:physiology*; D010455:Peptides / Q000737:chemistry; D011387:Prokaryotic Cells / Q000378:metabolism / Q000648:ultrastructure; D014176:Protein Biosynthesis; D017510:Protein Folding
D001426:Bacterial Proteins; D018834:Chaperonin 60; D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins; D046911:Macromolecular Substances; D018832:Molecular Chaperones; D010455:Peptides; C063842:dnaK protein, E coli