상세 정보

underline
Metadata Downloads : dc(xml) or Excel
Cited 0 time in scopus ci

Title 

Glutathione peroxidase 3 of Saccharomyces cerevisiae regulates the activity of methionine sulfoxide reductase in a redox state-dependent way

Authors 

Chang Won KhoPhil Young LeeKwang-Hee BaeS ChoZ W LeeByoung Chul ParkS KangDo Hee LeeSung Goo Park

Publisher 

Elsevier

Issue Date 

2006

Citation 

Biochemical and Biophysical Research Communications, vol. 348, no. 1, pp. 25-35

Keywords 

disulfide bondGpx3Mxr1oxidative stressROSglutathione peroxidaseglutathione peroxidase 3methioninemethionine sulfoxide reductaseunclassified drug

Abstract 

Glutathione peroxidase (Gpx) is one of the most important anti-oxidant enzymes in yeast. Gpx3 is a ubiquitously expressed isoform that modulates the activities of redox-sensitive thiol proteins, particularly those involved in signal transduction pathways and protein translocation. In order to search for the interaction partners of Gpx3, we carried out immunoprecipitation/2-dimensional gel electrophoresis (IP-2DE), MALDI-TOF mass spectrometry, and a pull down assay. We found that Mxr1, a peptide methionine sulfoxide reductase, interacts with Gpx3. By reducing methionine sulfoxide to methionine, Mxr1 reverses the inactivation of proteins caused by the oxidation of critical methionine residues. Gpx3 can interact with Mxr1 through the formation of an intermolecular disulfide bond. When oxidative stress is induced by H2O2, this interaction is compromised and the free Mxr1 then repairs the oxidized proteins. Our findings imply that this interaction links redox sensing machinery of Gpx3 to protein repair activity of Mxr1. Based on these results, we propose that Gpx3 functions as a redox-dependent exquisite regulator of the protein repair activity of Mxr1.

ISSN 

0006-291X

Link 

http://dx.doi.org/10.1016/j.bbrc.2006.06.067

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


There are no files associated with this item.
qrcode

FusionCharts.
DSpace Software Coptright(c) 2010 MIT and Hewleft-Packard  /  KRIBB-REPOSITORY ( Email:jakim@kribb.re.kr)