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- Title
Molecular chaperones in the cytosol: from nascent chain to folded protein.
- Authors
Hartl, F Ulrich; Hayer-Hartl, Manajit
- Abstract
Efficient folding of many newly synthesized proteins depends on assistance from molecular chaperones, which serve to prevent protein misfolding and aggregation in the crowded environment of the cell. Nascent chain--binding chaperones, including trigger factor, Hsp70, and prefoldin, stabilize elongating chains on ribosomes in a nonaggregated state. Folding in the cytosol is achieved either on controlled chain release from these factors or after transfer of newly synthesized proteins to downstream chaperones, such as the chaperonins. These are large, cylindrical complexes that provide a central compartment for a single protein chain to fold unimpaired by aggregation. Understanding how the thousands of different proteins synthesized in a cell use this chaperone machinery has profound implications for biotechnology and medicine.
- Publication
Science (New York, N.Y.), 2002, Vol 295, Issue 5561, p1852
- ISSN
1095-9203
- Publication type
Journal Article
- DOI
10.1126/science.1068408