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Int. J. Mol. Sci. 2018, 19(2), 489;

Physicochemical Properties of the Mammalian Molecular Chaperone HSP60

Department of Life Science, Graduate School and Faculty of Engineering Science, Akita University, Akita 010-8502, Japan
Department of Molecular Biosciences, Faculty of Life Sciences, Kyoto Sangyo University, Kamigamo, Kita-ku, Kyoto 803-8555, Japan
Department of Physics, Faculty of Science, Shizuoka University, 836 Ohya, Suruga, Shizuoka 422-8529, Japan
Laboratory of Molecular Cell Dynamics, Faculty of Advanced Life Science, Hokkaido University, N21W11, Kita-ku, Sapporo 001-0021, Japan
Department of Gastroenterology, Juntendo University School of Medicine, Bunkyo-Ku, Tokyo 113-8421, Japan
Author to whom correspondence should be addressed.
Received: 3 October 2017 / Revised: 23 January 2018 / Accepted: 25 January 2018 / Published: 6 February 2018
(This article belongs to the Special Issue Molecular Chaperones)
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The E. coli GroEL/GroES chaperonin complex acts as a folding cage by producing a bullet-like asymmetric complex, and GroEL exists as double rings regardless of the presence of adenosine triphosphate (ATP). Its mammalian chaperonin homolog, heat shock protein, HSP60, and co-chaperonin, HSP10, play an essential role in protein folding by capturing unfolded proteins in the HSP60/HSP10 complex. However, the structural transition in ATPase-dependent reaction cycle has remained unclear. We found nucleotide-dependent association and dissociation of the HSP60/HSP10 complex using various analytical techniques under near physiological conditions. Our results showed that HSP60 exist as a significant number of double-ring complexes (football- and bullet-type complexes) and a small number of single-ring complexes in the presence of ATP and HSP10. HSP10 binds to HSP60 in the presence of ATP, which increased the HSP60 double-ring formation. After ATP is hydrolyzed to Adenosine diphosphate (ADP), HSP60 released the HSP10 and the dissociation of the double-ring to single-rings occurred. These results indicated that HSP60/HSP10 undergoes an ATP-dependent transition between the single- and double-rings in their system that is highly distinctive from the GroEL/GroES system particularly in the manner of complex formation and the roles of ATP binding and hydrolysis in the reaction cycle. View Full-Text
Keywords: molecular chaperone; chaperonin; HSP60; GroEL molecular chaperone; chaperonin; HSP60; GroEL

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Ishida, R.; Okamoto, T.; Motojima, F.; Kubota, H.; Takahashi, H.; Tanabe, M.; Oka, T.; Kitamura, A.; Kinjo, M.; Yoshida, M.; Otaka, M.; Grave, E.; Itoh, H. Physicochemical Properties of the Mammalian Molecular Chaperone HSP60. Int. J. Mol. Sci. 2018, 19, 489.

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