AI Article Synopsis
- The chaperones ClpB (E. coli) and Hsp104 (yeast), along with Hsp70/Hsp40, work together to reactivate aggregated proteins in their respective organisms.
- Hsp104 and Hsp70/Hsp40 are essential for managing prion aggregates in yeast cells, enabling the maintenance and transmission of these aggregates.
- Recent studies highlight both common mechanisms and unique sensitivities in how Hsp104 and Hsp70/Hsp40 collaborate to reshape amorphous aggregates and prion fibrils.
Article Abstract
The oligomeric AAA+ chaperones Escherichia coli ClpB and Saccharomyces cerevisiae Hsp104 cooperate with cognate Hsp70/Hsp40 chaperone machineries in the reactivation of aggregated proteins in E. coli and S. cerevisiae. In addition, Hsp104 and Hsp70/Hsp40 are crucial for the maintenance of prion aggregates in yeast cells. While the bichaperone system efficiently solubilizes stress-generated amorphous aggregates, structurally highly ordered prion fibrils are only partially processed, resulting in the generation of fragmented prion seeds that can be transmitted to daughter cells for stable inheritance. Here, we describe and discuss the most recent mechanistic findings on yeast Hsp104 and Hsp70/Hsp40 cooperation in the remodeling of both types of aggregates, emphasizing similarities in the mechanism but also differences in the sensitivities towards chaperone activities.
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| http://dx.doi.org/10.1016/j.jsb.2012.05.002 | DOI Listing |
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