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Article

Fusion protein analysis reveals the precise regulation between Hsp70 and Hsp100 during protein disaggregation.

Scientific reports - 17 Aug 2017

Hayashi Sayaka, Nakazaki Yosuke, Kagii Kei, Imamura Hiromi, Watanabe Yo-Hei

Abstract excerpt

ClpB, a bacterial Hsp100, is a ring-shaped AAA+ chaperone that can reactivate aggregated proteins in cooperation with DnaK, a bacterial Hsp70, and its co-factors. ClpB subunits comprise two AAA+ modules with an interstitial rod-shaped M-domain. The M-domain regulates ClpB ATPase activity and interacts directly with the DnaK nucleotide-binding domain (NBD). Here, to clarify how these functions contribute to the...

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Identifiers

PMID: 28819163
DOI: 10.1038/s41598-017-08917-8
PMCID: PMC5561102

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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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Fusion protein analysis reveals the precise regulation between Hsp70 and Hsp100 during protein disaggregation.PMID 28819163Read ↗

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