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:Mol Cell
Hauptverfasser: Sweeny, Elizabeth A., Jackrel, Meredith E., Go, Michelle S., Sochor, Matthew A., Razzo, Beatrice M., DeSantis, Morgan E., Gupta, Kushol, Shorter, James
Format: Artigo
Sprache:Inglês
Veröffentlicht: 2015
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Article
Online Zugang:https://ncbi.nlm.nih.gov/pmc/articles/PMC4623595/
https://ncbi.nlm.nih.gov/pubmed/25620563
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.molcel.2014.12.021
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