ausblenden:
Schlagwörter:
Actins/*metabolism
Cytoskeletal Proteins/genetics/metabolism
Cytoskeleton/*metabolism
Heat-Shock Proteins/genetics/*metabolism
Microtubule-Associated Proteins/genetics/metabolism
Molecular Chaperones/genetics/*metabolism
Oxidation-Reduction
Protein Carbonylation
Recombinant Fusion Proteins/genetics/metabolism
Saccharomyces cerevisiae/cytology/genetics/*metabolism
Saccharomyces cerevisiae Proteins/genetics/*metabolism
Zusammenfassung:
The yeast AAA(+) chaperone Hsp104 is essential for the development of thermotolerance and for the inheritance of prions. Recently, Hsp104, together with the actin cytoskeleton, has been implicated in the asymmetric distribution of carbonylated proteins. Here, we investigated the interplay between Hsp104 and actin by using a dominant-negative variant of Hsp104 (HAP/ClpP) that degrades substrate proteins instead of remodeling them. Coexpression of HAP/ClpP causes defects in morphology and the actin cytoskeleton. Taking a candidate approach, we identified Spa2, a member of the polarisome complex, as an Hsp104 substrate. Furthermore, we provided genetic evidence that links Spa2 and Hsp104 to Hof1, a member of the cytokinesis machinery. Spa2 and Hof1 knockout cells are affected in the asymmetric distribution of damaged proteins, suggesting that Hsp104, Spa2, and Hof1 are members of a network controlling the inheritance of carbonylated proteins.
