Critical beginnings: tuning of solubility and structural accuracy of newly-synthesized proteins by the Hsp70 chaperone system

Abstract

The early stages of protein folding in the cell, in the presence of the ribosome and molecular chaperones, are not well understood. Upon release from the ribosome, proteins are kinetically channeled toward either the native or aggregated states. Once formed, the above species are often kinetically trapped from each other and cannot interconvert. Therefore, co- and immediately post-translational folding events are important prerequisites for long-term protein solubility and cell function. Chaperones grant solubility to aggregation-prone proteins during the earliest stages of protein life and can prevent harm from deleterious mutations.