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5 results on '"Ishida, Ryuichi"'

1. Physicochemical Properties of the Mammalian Molecular Chaperone HSP60

Author

Ishida, Ryuichi, Okamoto, Tomoya, Motojima, Fumihiro, Kubota, Hiroshi, Takahashi, Hiroki, Tanabe, Masako, Oka, Toshihiko, Kitamura, Akira, Kinjo, Masataka, Yoshida, Masasuke, Otaka, Michiro, Grave, Ewa, Itoh, Hideaki, Ishida, Ryuichi, Okamoto, Tomoya, Motojima, Fumihiro, Kubota, Hiroshi, Takahashi, Hiroki, Tanabe, Masako, Oka, Toshihiko, Kitamura, Akira, Kinjo, Masataka, Yoshida, Masasuke, Otaka, Michiro, Grave, Ewa, and Itoh, Hideaki

Abstract

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.

Published
2023

2. Bioluminescent Ratiometric Indicator for Analysis of Water Hardness in Household Water

Author

Ishida Ryuichi, Tomoki Matsuda, Mitsuru Hattori, Takeharu Nagai, and Nadim Hossain

Subjects
Energy transfer, softener, water hardness, lcsh:Chemical technology, smartphone, 01 natural sciences, Biochemistry, Article, Analytical Chemistry, 03 medical and health sciences, Hardness, Bioluminescence, Humans, lcsh:TP1-1185, Electrical and Electronic Engineering, Luciferases, Instrumentation, 030304 developmental biology, 0303 health sciences, Measurement method, Drinking Water, 010401 analytical chemistry, Calcium-Binding Proteins, Hard water, indicator ratiometry, Pulp and paper industry, bioluminescence, Atomic and Molecular Physics, and Optics, 0104 chemical sciences, Luminescent Proteins, Energy Transfer, Luminescent Measurements, Environmental science
Abstract

Water hardness (WH) is a useful parameter for testing household water, such as drinking, cooking, and washing water. Many countries around the world use pipeline water in their houses, but there is a need to monitor the WH because hard water has a negative impact on appliances. Currently, WH is often measured using chemical dye-based WH indicators, and these techniques require expensive equipment, and trained personnel. Therefore, a low-cost and simple measurement method has been desired. Here, we report LOTUS-W, which consists of a luciferase, Nanoluc, a yellow fluorescent protein Venus, and a Ca2+/Mg2+ detection domain of human centrin 3. The binding of Ca2+/Mg2+ to this indicator changes the conformation of human centrin 3, and induces bioluminescence resonance energy transfer (BRET) from Nanoluc to Venus, which changes its emission spectrum about 140%. The dissociation constants of LOTUS-W for Ca2+/Mg2+ are approximately several mM, making it suitable for measuring WH in the household water. With this indicator in combination with a smartphone, we have demonstrated that it is possible to evaluate WH easily and quickly. This novel indicator has the potential to be used for measuring not only household water but also water used in the food industry, etc.

Published
2020

3. Physicochemical Properties of the Mammalian Molecular Chaperone HSP60

Author

Ishida, Ryuichi, Okamoto, Tomoya, Motojima, Fumihiro, Kubota, Hiroshi, Takahashi, Hiroki, Tanabe, Masako, Oka, Toshihiko, Kitamura, Akira, Kinjo, Masataka, Yoshida, Masasuke, Otaka, Michiro, Grave, Ewa, Itoh, Hideaki, Ishida, Ryuichi, Okamoto, Tomoya, Motojima, Fumihiro, Kubota, Hiroshi, Takahashi, Hiroki, Tanabe, Masako, Oka, Toshihiko, Kitamura, Akira, Kinjo, Masataka, Yoshida, Masasuke, Otaka, Michiro, Grave, Ewa, and Itoh, Hideaki

Abstract

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.

Published
2018

4. Bioluminescent Ratiometric Indicator for Analysis of Water Hardness in Household Water.

Author

Hossain, Md Nadim, Ishida, Ryuichi, Hattori, Mitsuru, Matsuda, Tomoki, and Nagai, Takeharu

Subjects
*WATER hardness, *WATER analysis, *FLUORESCENCE resonance energy transfer, *COLORING matter in food, *FLUORESCENT proteins, *WATER use, *BIOLUMINESCENCE
Abstract

Water hardness (WH) is a useful parameter for testing household water, such as drinking, cooking, and washing water. Many countries around the world use pipeline water in their houses, but there is a need to monitor the WH because hard water has a negative impact on appliances. Currently, WH is often measured using chemical dye-based WH indicators, and these techniques require expensive equipment, and trained personnel. Therefore, a low-cost and simple measurement method has been desired. Here, we report LOTUS-W, which consists of a luciferase, Nanoluc, a yellow fluorescent protein Venus, and a Ca2+/Mg2+ detection domain of human centrin 3. The binding of Ca2+/Mg2+ to this indicator changes the conformation of human centrin 3, and induces bioluminescence resonance energy transfer (BRET) from Nanoluc to Venus, which changes its emission spectrum about 140%. The dissociation constants of LOTUS-W for Ca2+/Mg2+ are approximately several mM, making it suitable for measuring WH in the household water. With this indicator in combination with a smartphone, we have demonstrated that it is possible to evaluate WH easily and quickly. This novel indicator has the potential to be used for measuring not only household water but also water used in the food industry, etc. [ABSTRACT FROM AUTHOR]

Published
2020
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5. Physicochemical Properties of the Mammalian Molecular Chaperone HSP60.

Author

Ishida R, Okamoto T, Motojima F, Kubota H, Takahashi H, Tanabe M, Oka T, Kitamura A, Kinjo M, Yoshida M, Otaka M, Grave E, and Itoh H

Subjects
Adenosine Triphosphate chemistry, Adenosine Triphosphate metabolism, Animals, Chaperonin 10 chemistry, Chaperonin 10 metabolism, Humans, Molecular Chaperones chemistry, Molecular Chaperones metabolism, Molecular Structure, Multiprotein Complexes chemistry, Multiprotein Complexes metabolism, Multiprotein Complexes ultrastructure, Protein Binding, Chaperonin 60 chemistry, Chaperonin 60 metabolism, Chemical Phenomena
Abstract

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., Competing Interests: The authors declare no conflict of interest.

Published
2018
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