HSP60 possesses a GTPase activity and mediates protein folding with HSP10

Tomoya Okamoto; Hiroshi Yamamoto; Ikuru Kudo; Kazuya Matsumoto; Masafumi Odaka; Ewa Grave; Hideaki Itoh

doi:10.1038/s41598-017-17167-7

HSP60 possesses a GTPase activity and mediates protein folding with HSP10

Tomoya Okamoto, Hiroshi Yamamoto, Ikuru Kudo, Kazuya Matsumoto, Masafumi Odaka, Ewa Grave, Hideaki Itoh

Research output: Contribution to journal › Article › peer-review

19 Citations (Scopus)

Abstract

The mammalian molecular chaperone, HSP60, plays an essential role in protein homeostasis through mediating protein folding and assembly. The structure and ATP-dependent function of HSP60 has been well established in recent studies. After ATP, GTP is the major cellular nucleotide. In this paper, we have investigated the role of GTP in the activity of HSP60. It was found that HSP60 has different properties with respect to allostery, complex formation and protein folding activity depending on the nucleoside triphosphate present. The presence of GTP slightly affected the ATPase activity of HSP60 during protein folding. These results provide clues as to the functional mechanism of the HSP60-HSP10 complex.

Original language	English
Article number	16931
Journal	Scientific reports
Volume	7
Issue number	1
DOIs	https://doi.org/10.1038/s41598-017-17167-7
Publication status	Published - Dec 1 2017
Externally published	Yes

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abstract = "The mammalian molecular chaperone, HSP60, plays an essential role in protein homeostasis through mediating protein folding and assembly. The structure and ATP-dependent function of HSP60 has been well established in recent studies. After ATP, GTP is the major cellular nucleotide. In this paper, we have investigated the role of GTP in the activity of HSP60. It was found that HSP60 has different properties with respect to allostery, complex formation and protein folding activity depending on the nucleoside triphosphate present. The presence of GTP slightly affected the ATPase activity of HSP60 during protein folding. These results provide clues as to the functional mechanism of the HSP60-HSP10 complex.",

author = "Tomoya Okamoto and Hiroshi Yamamoto and Ikuru Kudo and Kazuya Matsumoto and Masafumi Odaka and Ewa Grave and Hideaki Itoh",

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AU - Okamoto, Tomoya

AU - Yamamoto, Hiroshi

AU - Kudo, Ikuru

AU - Matsumoto, Kazuya

AU - Odaka, Masafumi

AU - Grave, Ewa

AU - Itoh, Hideaki

N1 - Funding Information: H.I. was supported by a Grant-in-Aid for Scientific Research from the Japanese Ministry of Education, Science, Sports and Culture. We special thanks to Dr. David Morris (University of Washington, USA) for helpful comments on the manuscript. Publisher Copyright: © 2017 The Author(s).

PY - 2017/12/1

Y1 - 2017/12/1

N2 - The mammalian molecular chaperone, HSP60, plays an essential role in protein homeostasis through mediating protein folding and assembly. The structure and ATP-dependent function of HSP60 has been well established in recent studies. After ATP, GTP is the major cellular nucleotide. In this paper, we have investigated the role of GTP in the activity of HSP60. It was found that HSP60 has different properties with respect to allostery, complex formation and protein folding activity depending on the nucleoside triphosphate present. The presence of GTP slightly affected the ATPase activity of HSP60 during protein folding. These results provide clues as to the functional mechanism of the HSP60-HSP10 complex.

AB - The mammalian molecular chaperone, HSP60, plays an essential role in protein homeostasis through mediating protein folding and assembly. The structure and ATP-dependent function of HSP60 has been well established in recent studies. After ATP, GTP is the major cellular nucleotide. In this paper, we have investigated the role of GTP in the activity of HSP60. It was found that HSP60 has different properties with respect to allostery, complex formation and protein folding activity depending on the nucleoside triphosphate present. The presence of GTP slightly affected the ATPase activity of HSP60 during protein folding. These results provide clues as to the functional mechanism of the HSP60-HSP10 complex.

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HSP60 possesses a GTPase activity and mediates protein folding with HSP10

Abstract

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