5 results match your criteria: "Japan ywatanab@center.konan-u.ac.jp.[Affiliation]"
Publisher Correction: Dynamic structural states of ClpB involved in its disaggregation function.
Nat Commun
July 2019
Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, 920-1192, Japan.
An amendment to this paper has been published and can be accessed via a link at the top of the paper.
View Article and Find Full Text PDFDynamic structural states of ClpB involved in its disaggregation function.
Nat Commun
June 2018
Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, 920-1192, Japan.
The ATP-dependent bacterial protein disaggregation machine, ClpB belonging to the AAA+ superfamily, refolds toxic protein aggregates into the native state in cooperation with the cognate Hsp70 partner. The ring-shaped hexamers of ClpB unfold and thread its protein substrate through the central pore. However, their function-related structural dynamics has remained elusive.
View Article and Find Full Text PDFFusion protein analysis reveals the precise regulation between Hsp70 and Hsp100 during protein disaggregation.
Sci Rep
August 2017
Department of Biology, Faculty of Science and Engineering, Konan University, Kobe, Japan.
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).
View Article and Find Full Text PDFAnalysis of the cooperative ATPase cycle of the AAA+ chaperone ClpB from Thermus thermophilus by using ordered heterohexamers with an alternating subunit arrangement.
J Biol Chem
April 2015
From the Department of Biology, Faculty of Science and Engineering and the Institute for Integrative Neurobiology, Konan University, Okamoto 8-9-1, Kobe 658-8501, Japan
Article Synopsis
- * The chaperone utilizes ATP binding and hydrolysis to generate mechanical force necessary for disaggregating proteins, although the details of its ATPase cycle remain complex and poorly understood across different species.
- * Research on ordered structures of ClpB from Thermus thermophilus revealed that ATP binding is random initially, but once enough ATP binds to one ring, it activates the other ring for cooperative ATP hydrolysis, which is essential for the protein disaggregation function of ClpB.
Stability of the two wings of the coiled-coil domain of ClpB chaperone is critical for its disaggregation activity.
Biochem J
June 2009
Department of Biology, Faculty of Science and Engineering, Konan University, Okamoto 8-9-1, Kobe 658-8501, Japan.
The ClpB chaperone forms a hexamer ring and rescues aggregated proteins in co-operation with the DnaK system. Each subunit of ClpB has two nucleotide-binding modules, AAA (ATPase associated with various cellular activities)-1 and AAA-2, and an 85-A (1 A=0.1 nm)-long coiled-coil.
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