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Title 

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

 

효모 Gpx3의 글루타민 합성효소의 비효소적 분해의 억제

Authors 

Phil Young LeeC W KhoDo Hee LeeSunghyun KangS KangSang Chul LeeByoung Chul ParkS ChoKwang-Hee BaeSung Goo Park

Publisher 

Elsevier

Issue Date 

2007

Citation 

Biochemical and Biophysical Research Communications, vol. 362, no. 2, pp. 405-409

Keywords 

glutamine synthetaseglutathione peroxidase 3MFO systemoxidative stressROSglutathione peroxidasenonhumansaccharomyces cerevisiaesaccharomyces cerevisiae proteins

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.

ISSN 

0006-291X

Link 

http://dx.doi.org/10.1016/j.bbrc.2007.08.035

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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