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A Nonconventional Role of Molecular Chaperones: Involvement in the Cytoarchitecture

Peter Csermely

P. Csermely is in the Department of Medical Chemistry, Semmelweis University, H-1444 Budapest, and the Biorex Corporation, H-8200 Veszprém, Hungary.
A hallmark of chaperone action is assistance in protein folding. Indeed, folding of nascent prokaryotic proteins proceeds mostly as a chaperone-assisted, posttranslational event. On the contrary, in nonstressed eukaryotic cells folding-related tasks of eukaryotic chaperones are restricted to a subset of proteins, and "jobless" chaperones may form an extension of the cytoarchitecture, facilitating intracellular traffic of proteins and other macromolecules.

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