Chaperone networks in protein disaggregation and prion propagation

• Verfasst von: Winkler, Juliane [VerfasserIn]
• Verfasst von: Tyedmers, Jens [VerfasserIn]
• Verfasst von: Bukau, Bernd [VerfasserIn]
• Verfasst von: Mogk, Axel [VerfasserIn]
• Titel: Chaperone networks in protein disaggregation and prion propagation
• Verf.angabe: Juliane Winkler, Jens Tyedmers, Bernd Bukau, Axel Mogk
• E-Jahr: 2012
• Jahr: 10 May 2012
• Umfang: 9 S.
• Fussnoten: Available online 10 May 2012 ; Gesehen am 16.07.2018
• Titel Quelle: Enthalten in: Journal of structural biology
• Ort Quelle: San Diego, Calif. : Elsevier, 1990
• Jahr Quelle: 2012
• Band/Heft Quelle: 179(2012), 2, Seite 152-160
• ISSN Quelle: 1095-8657
• DOI: doi:10.1016/j.jsb.2012.05.002
• Datenträger: Online-Ressource
• Sprache: eng
• Sach-SW: Chaperone
• Sach-SW: ClpB
• Sach-SW: Hsp104
• Sach-SW: Hsp70
• Sach-SW: Prion
• Sach-SW: Protein disaggregation
• K10plus-PPN: 157762193X

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.