Glutathione transport systems of the budding yeast saccharomyces cerevisiae

Tsuyoshi Miyake; Toshiya Hazu; Sayaka Yoshida; Munetoshi Kanayama; Ken Ichi Tomochika; Sumio Shinoda; Bun Ichiro Ono

doi:10.1271/bbb.62.1858

Glutathione transport systems of the budding yeast saccharomyces cerevisiae

Tsuyoshi Miyake, Toshiya Hazu, Sayaka Yoshida, Munetoshi Kanayama, Ken Ichi Tomochika, Sumio Shinoda, Bun Ichiro Ono

薬学部

研究成果 › 査読

31 被引用数 (Scopus)

抄録

The budding yeast Saccharomyces cerevisiae was shown to have two kinetically distinguishable glutathione transport systems. While one with high affinity (GSH-P1; K_T=0.045 mM) was regulated, the other with low affinity (GSH-P2; K_T>2 mM) was not. GSH-P1 was highly specific to glutathione, and its activity was quickly lost by suspending the cells in buffer solutions. This activity loss was not observed if glucose-containing buffer was used. In addition, ρ ⁻ isolates had only about one half of the glutathione transport activity of the original (ρ ⁺) strain. Therefore, it is concluded that GSH-P1 is an ATP-driven transport system. Strong and moderate inhibition of GSH-P1 by protonophores and ionophores, respectively, are attributed to competition for ATP between GSH-P1 and proton- and cation-pumps, re.

本文言語	English
ページ（範囲）	1858-1864
ページ数	7
ジャーナル	Bioscience, Biotechnology and Biochemistry
巻	62
号	10
DOI	https://doi.org/10.1271/bbb.62.1858
出版ステータス	Published - 1月 1 1998

ASJC Scopus subject areas

バイオテクノロジー
分析化学
生化学
応用微生物学とバイオテクノロジー
分子生物学
有機化学

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10.1271/bbb.62.1858

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title = "Glutathione transport systems of the budding yeast saccharomyces cerevisiae",

abstract = "The budding yeast Saccharomyces cerevisiae was shown to have two kinetically distinguishable glutathione transport systems. While one with high affinity (GSH-P1; KT=0.045 mM) was regulated, the other with low affinity (GSH-P2; KT>2 mM) was not. GSH-P1 was highly specific to glutathione, and its activity was quickly lost by suspending the cells in buffer solutions. This activity loss was not observed if glucose-containing buffer was used. In addition, ρ − isolates had only about one half of the glutathione transport activity of the original (ρ +) strain. Therefore, it is concluded that GSH-P1 is an ATP-driven transport system. Strong and moderate inhibition of GSH-P1 by protonophores and ionophores, respectively, are attributed to competition for ATP between GSH-P1 and proton- and cation-pumps, re.",

keywords = "Glutathione, Inhibition, Kinetic analysis, Saccharomyces cerevisiae, Transport",

author = "Tsuyoshi Miyake and Toshiya Hazu and Sayaka Yoshida and Munetoshi Kanayama and Tomochika, {Ken Ichi} and Sumio Shinoda and Ono, {Bun Ichiro}",

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AU - Miyake, Tsuyoshi

AU - Hazu, Toshiya

AU - Yoshida, Sayaka

AU - Kanayama, Munetoshi

AU - Tomochika, Ken Ichi

AU - Shinoda, Sumio

AU - Ono, Bun Ichiro

PY - 1998/1/1

Y1 - 1998/1/1

N2 - The budding yeast Saccharomyces cerevisiae was shown to have two kinetically distinguishable glutathione transport systems. While one with high affinity (GSH-P1; KT=0.045 mM) was regulated, the other with low affinity (GSH-P2; KT>2 mM) was not. GSH-P1 was highly specific to glutathione, and its activity was quickly lost by suspending the cells in buffer solutions. This activity loss was not observed if glucose-containing buffer was used. In addition, ρ − isolates had only about one half of the glutathione transport activity of the original (ρ +) strain. Therefore, it is concluded that GSH-P1 is an ATP-driven transport system. Strong and moderate inhibition of GSH-P1 by protonophores and ionophores, respectively, are attributed to competition for ATP between GSH-P1 and proton- and cation-pumps, re.

AB - The budding yeast Saccharomyces cerevisiae was shown to have two kinetically distinguishable glutathione transport systems. While one with high affinity (GSH-P1; KT=0.045 mM) was regulated, the other with low affinity (GSH-P2; KT>2 mM) was not. GSH-P1 was highly specific to glutathione, and its activity was quickly lost by suspending the cells in buffer solutions. This activity loss was not observed if glucose-containing buffer was used. In addition, ρ − isolates had only about one half of the glutathione transport activity of the original (ρ +) strain. Therefore, it is concluded that GSH-P1 is an ATP-driven transport system. Strong and moderate inhibition of GSH-P1 by protonophores and ionophores, respectively, are attributed to competition for ATP between GSH-P1 and proton- and cation-pumps, re.

KW - Glutathione

KW - Inhibition

KW - Kinetic analysis

KW - Saccharomyces cerevisiae

KW - Transport

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JO - Bioscience, Biotechnology and Biochemistry

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Glutathione transport systems of the budding yeast saccharomyces cerevisiae

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