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Article

ClpB chaperone passively threads soluble denatured proteins through its central pore.

Genes to cells : devoted to molecular & cellular mechanisms - 1 Dec 2014

Nakazaki Yosuke, Watanabe Yo-Hei

Abstract excerpt

ClpB disaggregase forms a ring-shaped hexamer that threads substrate proteins through the central pore using energy from ATP. The ClpB protomer consists of an N-terminal domain, a middle domain, and two AAA+ modules. These two AAA+ modules bind and hydrolyze ATP and construct the core of the hexameric ring. Here, we investigated the roles of the two AAA+ modules in substrate threading. BAP is an engineered ClpB...

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Identifiers

PMID: 25288401
DOI: 10.1111/gtc.12188

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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