NR AMLW
AU Wickner,S.; Maurizi,M.R.; Gottesman,S.
TI Posttranslational quality control: folding, refolding, and degrading proteins.
QU Science 1999 Dec 3; 286(5446): 1888-93
PT journal article; review; review, tutorial
AB Polypeptides emerging from the ribosome must fold into stable three-dimensional structures and maintain that structure throughout their functional lifetimes. Maintaining quality control over protein structure and function depends on molecular chaperones and proteases, both of which can recognize hydrophobic regions exposed on unfolded polypeptides. Molecular chaperones promote proper protein folding and prevent aggregation, and energy-dependent proteases eliminate irreversibly damaged proteins. The kinetics of partitioning between chaperones and proteases determines whether a protein will be destroyed before it folds properly. When both quality control options fail, damaged proteins accumulate as aggregates, a process associated with amyloid diseases.
ZR 62
MH Adenosinetriphosphatase/metabolism; Amyloid/metabolism; Animal; Endopeptidases/*metabolism; Eukaryotic Cells/metabolism; Human; Models, Biological; Molecular Chaperones/*metabolism; Prions/metabolism; Prokaryotic Cells/metabolism; *Protein Folding; Proteins/*chemistry/*metabolism; Translation, Genetic; Ubiquitins/metabolism
AD Laboratory of Molecular Biology, National Cancer Institute, Bethesda, MD 20892-4255, USA
SP englisch
PO USA