Work

Mechanisms of Cellular Proteostasis: Insights from Single-Molecule Approaches

Year: 2014

Type: review

Abstract: Cells employ a variety of strategies to maintain proteome homeostasis. Beginning during protein biogenesis, the translation machinery and a number of molecular chaperones promote correct de novo folding of nascent proteins even before synthesis is complete. Another set of molecular chaperones helps to maintain proteins in their functional, native state. Polypeptides that are no longer needed or pose a threat to the cell, such as misfolded proteins and aggregates, are removed in an efficient and timely fashion by ATP-dependent proteases. In this review, we describe how applications of single-molecule manipulation methods, in particular optical tweezers, are shedding new light on the molecular mechanisms of quality control during the life cycles of proteins.

Source: Annual Review of Biophysics

DOI: 10.1146/annurev-biophys-051013-022811

Authors: Carlos J. Bustamante, Christian M. Kaiser, Rodrigo A. Maillard, Daniel H. Goldman, Christian A.M. Wilson

Institutions: QB3, Johns Hopkins University, Georgetown University, University of California, Berkeley

Language: English

Topic: Heat shock proteins research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green