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Article

The Hsp104 N-terminal domain enables disaggregase plasticity and potentiation.

Molecular cell - 5 Mar 2015

Sweeny Elizabeth A, Jackrel Meredith E, Go Michelle S, Sochor Matthew A, Razzo Beatrice M, DeSantis Morgan E, Gupta Kushol, Shorter James

Abstract excerpt

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 Hsp104 N-terminal domain (NTD) enables this operational plasticity. Hsp104 lacking the NTD (Hsp104(ΔN)) dissolves...

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Identifiers

PMID: 25620563
DOI: 10.1016/j.molcel.2014.12.021
PMCID: PMC4623595

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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