Special Reviews

Posttranslational Quality Control: Folding, Refolding, and Degrading Proteins

See allHide authors and affiliations

Science  03 Dec 1999:
Vol. 286, Issue 5446, pp. 1888-1893
DOI: 10.1126/science.286.5446.1888

You are currently viewing the abstract.

View Full Text


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.

  • * To whom correspondence should be addressed: E-mail: susang{at}helix.nih.gov

View Full Text