Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins

Article Abstract:

Hsp104 is a stress tolerance factor that promotes reactivation of heat-damaged proteins in the yeast Saccharomyces cerevisiae through a direct process. Together with Hsp40 and Hsp70, Hsp104 can reactivate proteins that have been denatured and allowed to aggregate. It cooperates with the chaperones present in reticulocyte lysates. This suggests that Hsp104 has a protein remodeling activity that acts on trapped, aggregated proteins and requires specific interactions with conventional chaperones to promote refolding of the intermediates it produces.

Yeast, Yeast (Food product), Protein denaturation

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Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae

Article Abstract:

The role of the Hsp104 proteins in inducing the conformational change of Sup35 was analyzed to characterize the mechanisms that mediate the maintenance of the [PSI+] state in Saccharomyces cerevisiae. Dye-binding and and secondary-structure analysis of Sup35-derived fiber from Saccharomyces cerevisiae indicated the role of the protein in acting as the determinant of the unconventional [PSI+] genetic element. Furthermore, the Sup35 protein derivatives exhibited an intrinsic capacity to form highly-ordered fibrous structures.

Nucleoproteins, Prions, Saccharomyces, Prions (Proteins)

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Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains

Article Abstract:

A study was conducted to show that DnaK, the major Escherichia coli heat shock 70 protein, transiently associates with a broad range of nascent and newly synthesized polypeptides. The cells were grown to midlog phase in M63 medium before being converted to spheroplasts and pulse-chase labeled. Results indicated partially overlapping functions of DnaK and trigger factor in de novo protein folding.

Analysis, Escherichia coli, Polypeptides

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