NDLI: Association of deoxyhypusine hydroxylase with peroxiredoxin I was modulated in the yeast Saccharomyces cerevisiae under oxidative stress

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Association of deoxyhypusine hydroxylase with peroxiredoxin I was modulated in the yeast Saccharomyces cerevisiae under oxidative stress

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Journal of the Korean Society for Applied Biological Chemistry : Volume 54, Issue 3, June 2011

Journal of the Korean Society for Applied Biological Chemistry : Volume 54, Issue 2, April 2011

Journal of the Korean Society for Applied Biological Chemistry : Volume 54, Issue 1, February 2011

Journal of the Korean Society for Applied Biological Chemistry : Volume 53

Journal of the Korean Society for Applied Biological Chemistry : Volume 52

Association of deoxyhypusine hydroxylase with peroxiredoxin I was modulated in the yeast Saccharomyces cerevisiae under oxidative stress

Content Provider	Springer Nature Link
Author	Choi, Yeon Jin Kang, Kee Ryeon Kim, Min Gab Kang, Ju Hwan Shim, Doobo Lee, Ji Young Park, Eun Sil Jung, Eun Jung Yoo, Hyun Joo Lee, Young Mee Kang, Dawon Sim, Gyujin Lee, Sang Yeol
Copyright Year	2011
Abstract	Eukaryotic translation initiation factor 5A (eIF5A) is the only hypusine-containing protein, which is formed by deoxyhypusine synthase (DHS) and deoxyhypusine hydroxylase (DOHH). DOHH is a novel metalloenzyme with HEAT [named for human huntingtin (H), elongation factor 3 (E), a subunit of protein phosphatase 2A (A), and the target of rapamycin (T)]-repeat motifs. Inspite of much progress in determining the roles of iron-containing DOHH holoenzyme as an eIF5A hydroxylase, little is known about iron-free apoenzyme of DOHH under certain stress conditions. For this purpose, we compared cell growth in two yeast strains subjected to oxidative damage. Thus, the existence of more viable cells in the Saccharomyces cerevisiae BY4743 (parental yeast) strain than in the DOHH-null strain after H$_{2}$O$_{2}$ treatment indicates the importance of DOHH in protecting yeast cells against oxidative stress. To identify endogenous target proteins influenced by DOHH under oxidative damage, proteomic analysis was applied to the two yeast strains. Of these proteins, the oxidized form of peroxiredoxin I (PrxI) was concomitantly up-regulated in both strains under H$_{2}$O$_{2}$ treatment. Two-dimensional electrophoresis (DE) followed by immunoblot analysis shows that the recovery of the oxidized PrxI to the reduced enzyme under H$_{2}$O$_{2}$ treatment was found to be much slower in the DOHH-null strain than in the parental strain. Based on the results, we discovered a possible interaction between DOHH and PrxI by immunoprecipitation/ immunoblotting in yeast under oxidative stress. Taken together, these results suggest that DOHH might be a candidate protein for protection of yeast cells against oxidative stress in conjunction with PrxI.
Starting Page	515
Ending Page	523
Page Count	9
File Format	PDF
ISSN	17382203
Journal	Journal of the Korean Society for Applied Biological Chemistry
Volume Number	54
Issue Number	4
e-ISSN	2234344X
Language	English
Publisher	Springer-Verlag
Publisher Date	2012-07-26
Publisher Place	New York
Access Restriction	Subscribed
Subject Keyword	peroxiredoxin I proteomics deoxyhypusine hydroxylase Applied Microbiology Biological Techniques redox state oxidative stress Bioorganic Chemistry
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Biochemistry, Genetics and Molecular Biology

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