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

Faculty of Pharmaceutical Sciences

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

30 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	1858-1864
Number of pages	7
Journal	Bioscience, Biotechnology and Biochemistry
Volume	62
Issue number	10
DOIs	https://doi.org/10.1271/bbb.62.1858
Publication status	Published - Jan 1 1998

Keywords

Glutathione
Inhibition
Kinetic analysis
Saccharomyces cerevisiae
Transport

ASJC Scopus subject areas

Biotechnology
Analytical Chemistry
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology
Organic Chemistry

Access to Document

10.1271/bbb.62.1858

Fingerprint Dive into the research topics of 'Glutathione transport systems of the budding yeast saccharomyces cerevisiae'. Together they form a unique fingerprint.

Cite this

@article{732e979c7acf4e6a8ca876589cce24d6,

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}",

year = "1998",

month = jan,

day = "1",

doi = "10.1271/bbb.62.1858",

language = "English",

volume = "62",

pages = "1858--1864",

journal = "Bioscience, Biotechnology and Biochemistry",

issn = "0916-8451",

publisher = "Japan Society for Bioscience Biotechnology and Agrochemistry",

number = "10",

}

TY - JOUR

T1 - Glutathione transport systems of the budding yeast saccharomyces cerevisiae

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

UR - http://www.scopus.com/inward/record.url?scp=0032174632&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032174632&partnerID=8YFLogxK

U2 - 10.1271/bbb.62.1858

DO - 10.1271/bbb.62.1858

M3 - Article

C2 - 9836420

AN - SCOPUS:0032174632

VL - 62

SP - 1858

EP - 1864

JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

SN - 0916-8451

IS - 10

ER -

Glutathione transport systems of the budding yeast saccharomyces cerevisiae

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Cite this