Glutathione peroxidase 3 of Saccharomyces cerevisiae suppresses non-enzymatic proteolysis of glutamine synthetase in an activity-independent manner

Phil Young Lee; Chang Won Kho; Do Hee Lee; Sunghyun Kang; Seongman Kang; Sang Chul Lee; Byoung Chul Park; Sayeon Cho; Kwang Hee Bae; Sung Goo Park

doi:10.1016/j.bbrc.2007.08.035

Glutathione peroxidase 3 of Saccharomyces cerevisiae suppresses non-enzymatic proteolysis of glutamine synthetase in an activity-independent manner

Phil Young Lee, Chang Won Kho, Do Hee Lee, Sunghyun Kang, Seongman Kang, Sang Chul Lee, Byoung Chul Park, Sayeon Cho, Kwang Hee Bae, Sung Goo Park

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

7 Citations (Scopus)

Abstract

Glutathione peroxidase 3 (Gpx3) is ubiquitously expressed and is important antioxidant enzyme in yeast. It modulates the activities of redox-sensitive thiol proteins, particularly those involved in signal transduction pathway and protein translocation. Through immunoprecipitation/two-dimensional gel electrophoresis (IP-2DE), MALDI-TOF mass spectrometry, and a pull down assay, we found glutamine synthetase (GS; EC 6.3.1.2) as a candidate interacting protein with Gpx3. GS is a key enzyme in nitrogen metabolism and ammonium assimilation. It has been known that GS is non-enzymatically cleaved by ROS generated by MFO (thiol/ Fe³⁺/O₂ mixed-function oxidase) system. In this study, it is demonstrated that GS interacts with Gpx3 through its catalytic domain both in vivo and in vitro regardless of redox state. In addition, Gpx3 helps to protect GS from inactivation and degradation via oxidative stress in an activity-independent manner. Based on the results, it is suggested that Gpx3 protects GS from non-enzymatic proteolysis, thereby contributing to cell homeostasis when cell is exposed to oxidative stress.

Original language	English
Pages (from-to)	405-409
Number of pages	5
Journal	Biochemical and biophysical research communications
Volume	362
Issue number	2
DOIs	https://doi.org/10.1016/j.bbrc.2007.08.035
Publication status	Published - 2007 Oct 19

Bibliographical note

Funding Information:
We thank Ms. Lisa Wawrynchuk for carefully reading our manuscript. This work was supported by grants from the Basic Research Program of the Korea Science & Engineering Foundation (2007-01827) and the Korea Health 21 R&D Project, Ministry of Health & Welfare, Republic of Korea (01-PJ10-PG6-01GN16-0005).

Keywords

Glutamine synthetase
Glutathione peroxidase 3
MFO system
Oxidative stress
ROS

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2007.08.035

Cite this

Lee, P. Y., Kho, C. W., Lee, D. H., Kang, S., Kang, S., Lee, S. C., Park, B. C., Cho, S., Bae, K. H., & Park, S. G. (2007). Glutathione peroxidase 3 of Saccharomyces cerevisiae suppresses non-enzymatic proteolysis of glutamine synthetase in an activity-independent manner. Biochemical and biophysical research communications, 362(2), 405-409. https://doi.org/10.1016/j.bbrc.2007.08.035

Lee, PY, Kho, CW, Lee, DH, Kang, S, Kang, S, Lee, SC, Park, BC, Cho, S, Bae, KH & Park, SG 2007, 'Glutathione peroxidase 3 of Saccharomyces cerevisiae suppresses non-enzymatic proteolysis of glutamine synthetase in an activity-independent manner', Biochemical and biophysical research communications, vol. 362, no. 2, pp. 405-409. https://doi.org/10.1016/j.bbrc.2007.08.035

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abstract = "Glutathione peroxidase 3 (Gpx3) is ubiquitously expressed and is important antioxidant enzyme in yeast. It modulates the activities of redox-sensitive thiol proteins, particularly those involved in signal transduction pathway and protein translocation. Through immunoprecipitation/two-dimensional gel electrophoresis (IP-2DE), MALDI-TOF mass spectrometry, and a pull down assay, we found glutamine synthetase (GS; EC 6.3.1.2) as a candidate interacting protein with Gpx3. GS is a key enzyme in nitrogen metabolism and ammonium assimilation. It has been known that GS is non-enzymatically cleaved by ROS generated by MFO (thiol/ Fe3+/O2 mixed-function oxidase) system. In this study, it is demonstrated that GS interacts with Gpx3 through its catalytic domain both in vivo and in vitro regardless of redox state. In addition, Gpx3 helps to protect GS from inactivation and degradation via oxidative stress in an activity-independent manner. Based on the results, it is suggested that Gpx3 protects GS from non-enzymatic proteolysis, thereby contributing to cell homeostasis when cell is exposed to oxidative stress.",

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note = "Funding Information: We thank Ms. Lisa Wawrynchuk for carefully reading our manuscript. This work was supported by grants from the Basic Research Program of the Korea Science & Engineering Foundation (2007-01827) and the Korea Health 21 R&D Project, Ministry of Health & Welfare, Republic of Korea (01-PJ10-PG6-01GN16-0005).",

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AU - Kho, Chang Won

AU - Lee, Do Hee

AU - Kang, Sunghyun

AU - Kang, Seongman

AU - Lee, Sang Chul

AU - Park, Byoung Chul

AU - Cho, Sayeon

AU - Bae, Kwang Hee

AU - Park, Sung Goo

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PY - 2007/10/19

Y1 - 2007/10/19

N2 - Glutathione peroxidase 3 (Gpx3) is ubiquitously expressed and is important antioxidant enzyme in yeast. It modulates the activities of redox-sensitive thiol proteins, particularly those involved in signal transduction pathway and protein translocation. Through immunoprecipitation/two-dimensional gel electrophoresis (IP-2DE), MALDI-TOF mass spectrometry, and a pull down assay, we found glutamine synthetase (GS; EC 6.3.1.2) as a candidate interacting protein with Gpx3. GS is a key enzyme in nitrogen metabolism and ammonium assimilation. It has been known that GS is non-enzymatically cleaved by ROS generated by MFO (thiol/ Fe3+/O2 mixed-function oxidase) system. In this study, it is demonstrated that GS interacts with Gpx3 through its catalytic domain both in vivo and in vitro regardless of redox state. In addition, Gpx3 helps to protect GS from inactivation and degradation via oxidative stress in an activity-independent manner. Based on the results, it is suggested that Gpx3 protects GS from non-enzymatic proteolysis, thereby contributing to cell homeostasis when cell is exposed to oxidative stress.

AB - Glutathione peroxidase 3 (Gpx3) is ubiquitously expressed and is important antioxidant enzyme in yeast. It modulates the activities of redox-sensitive thiol proteins, particularly those involved in signal transduction pathway and protein translocation. Through immunoprecipitation/two-dimensional gel electrophoresis (IP-2DE), MALDI-TOF mass spectrometry, and a pull down assay, we found glutamine synthetase (GS; EC 6.3.1.2) as a candidate interacting protein with Gpx3. GS is a key enzyme in nitrogen metabolism and ammonium assimilation. It has been known that GS is non-enzymatically cleaved by ROS generated by MFO (thiol/ Fe3+/O2 mixed-function oxidase) system. In this study, it is demonstrated that GS interacts with Gpx3 through its catalytic domain both in vivo and in vitro regardless of redox state. In addition, Gpx3 helps to protect GS from inactivation and degradation via oxidative stress in an activity-independent manner. Based on the results, it is suggested that Gpx3 protects GS from non-enzymatic proteolysis, thereby contributing to cell homeostasis when cell is exposed to oxidative stress.

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Glutathione peroxidase 3 of Saccharomyces cerevisiae suppresses non-enzymatic proteolysis of glutamine synthetase in an activity-independent manner

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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