The Hsp104 N-Terminal Domain Enables Disaggregase Plasticity and Potentiation

The structural basis by which Hsp104 dissolves disordered aggregates and prions is unknown. A single subunit within the Hsp104 hexamer can solubilize disordered aggregates, whereas prion dissolution requires collaboration by multiple Hsp104 subunits. Here, we establish that the poorly understood Hsp...

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Veröffentlicht in:	Molecular cell 2015-03, Vol.57 (5), p.836-849
Hauptverfasser:	Sweeny, Elizabeth A., Jackrel, Meredith E., Go, Michelle S., Sochor, Matthew A., Razzo, Beatrice M., DeSantis, Morgan E., Gupta, Kushol, Shorter, James
Format:	Artikel
Sprache:	eng
Schlagworte:	adenosine diphosphate adenosine monophosphate adenosine triphosphate Adenosine Triphosphate - analogs & derivatives Adenosine Triphosphate - chemistry Adenosine Triphosphate - metabolism Adenylyl Imidodiphosphate - chemistry Adenylyl Imidodiphosphate - metabolism Heat-Shock Proteins - chemistry Heat-Shock Proteins - genetics Heat-Shock Proteins - metabolism hydrolysis Microscopy, Electron Microscopy, Fluorescence Models, Molecular Mutation Peptide Termination Factors - chemistry Peptide Termination Factors - metabolism prions Protein Binding Protein Multimerization Protein Structure, Tertiary Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Scattering, Small Angle solubilization X-radiation X-Ray Diffraction
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