Year: 1998
Type: review
Abstract: An essential cellular machinery that has been identified and studied only relatively recently is a collective of specialized proteins, molecular chaperones, that bind nonnative states of other proteins and assist them to reach a functional conformation, in most cases through the expenditure of ATP. Originally identified by their increased abundance following heat shock, chaperone proteins in general recognize exposed hydrophobic surfaces of nonnative species, surfaces that will ultimately be buried in the native state, and form noncovalent interactions with them, stabilizing them against irreversible multimeric aggregation. Release of polypeptide then follows, in many cases driven by an ATP-directed conformational change of the chaperone, permitting subsequent steps of polypeptide folding or biogenesis to occur. When such steps fail to proceed productively, recognition and rebinding by the same or another chaperone can occur, allowing another opportunity for a productive conformation to be reached.
Source: Cell
Authors: Bernd Bukau, Arthur L Horwich
Language: English
Topic: Heat shock proteins research
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $11,400
OpenAlex ID: W1963770237