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Prion aggregate structure in yeast cells is determined by the Hsp104 Hsp110 disaggregase machinery

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Figure

Figure 1. Aggregate remodeling in chaperone knockout strains. Representative tomographic slices through recon-structions of NM-YFP dots in HM20-embedded cell sections from cells with a wild-type chaperone complement and those with Δssa1, Δssa2, and Δsse1 d
Figure 2. Chaperone deletion alters the size rental wild-type strain, devoid of the NM-YFP expression cassette, but otherwise isogenic, is included as a control
Figure 3. NM-YFP assemblies have a nonuni-fluorescence from the dot aggregates. A line form distribution of molecular chaperones
Figure 4. Immunogold labeling of NM-YFP in dot assemblies in Hsp70 and Hsp110 knockout cell sections
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