Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance

Article Abstract:

The capacity of RNA viruses for rapid adaptation is exploited with an aim to explore the evolutionary constraints of chaperone-mediated protein folding. Chaperone Hsp90 is identified as an essential factor for folding and maturation of picornavirus capsid proteins. Results reveal tight evolutionary constraints on chaperone-mediated protein folding, which may be exploited for vital inhibition in vivo.

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Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells

Article Abstract:

Molecular chaperones assist the folding of newly translated and stress-denatured proteins and that eukaryotes evolved distinct chaperone networks to carry out these functions. The emergence of a translation-linked chaperone network likely underlies the elaborate cotranslational folding process necessary for the evolution of larger multidomain proteins characteristic of eukaryotic cells.

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Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways

Article Abstract:

An analysis of the chaperone requirement for degradation of misfolded variants of a cytosolic protein the von Hippel-Lindau (VHL) tumor suppressor reveals that distinct chaperone pathways mediate its folding and quality control. The finding suggests that a hierarchy of chaperone interactions can control the alternate fates of a cytosolic protein.

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