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J. Biol. Chem., August 5, 2005, 280, 28775-28784 | doi: 10.1074/jbc.M505362200 Oxidative Stress-dependent Structural and Functional Switching of a Human 2-Cys Peroxiredoxin Isotype II That Enhances HeLa Cell Resistance to H2O2-induced Cell Death

Abstract

Jeong Chan Moon^‡§¶∥, Young-Sool Hah^¶,**, Woe Yeon Kim^§¶‡‡, Bae Gyo Jung^‡§¶, Ho Hee Jang^‡§∥, Jung Ro Lee^‡§, Sun Young Kim^‡§∥, Young Mee Lee^‡§∥, Min Gyu Jeon^‡§, Choong Won Kim^**, Moo Je Cho^§ and Sang Yeol Lee^‡§§§

^‡Environmental Biotechnology National Core Research Center, ^§Division of Applied Life Sciences (BK21 Program), ^**Department of Biochemistry, College of Medicine and Institute of Health Sciences, Gyeongsang National University, Jinju 660-701, Korea

^§§ To whom correspondence should be addressed.
^¶ These authors contributed equally to this work.

Abstract
Although biochemical properties of 2-Cys peroxiredoxins (Prxs) have been extensively studied, their real physiological functions in higher eukaryotic cells remain obscure and certainly warrant further study. Here we demonstrated that human (h) PrxII, a cytosolic isotype of human 2-Cys Prx, has dual functions as a peroxidase and a molecular chaperone, and that these different functions are closely associated with its adoption of distinct protein structures. Upon exposure to oxidative stress, hPrxII assumes a high molecular weight complex structure that has a highly efficient chaperone function. However, the subsequent removal of stressors induces the dissociation of this protein structure into low molecular weight proteins and triggers a chaperone-to-peroxidase functional switch. The formation of a high molecular weight hPrxII complex depends on the hyperoxidation of its N-terminal peroxidatic Cys residue as well as on its C-terminal domain, which contains a “YF motif” that is exclusively found in eukaryotic 2-Cys Prxs. A C-terminally truncated hPrxII exists as low and oligomeric protein species and does not respond to oxidative stress. Moreover, this C-terminal deletion of hPrxII converted it from an oxidation-sensitive to a hyperoxidation-resistant form of peroxidase. When functioning as a chaperone, hPrxII protects HeLa cells from H₂O₂-induced cell death, as measured by a terminal deoxynucleotidyltransferase-mediated dUTP nick-end labeling assay and fluorescence-activated cell sorting analysis.

논문정보

형식Research article
게재일2005년 08월 (BRIC 등록일 2014-06-24)
연구진국내 연구진
분야 생명과학 > 분자생물학
피인용횟수120회 이상 인용된 논문

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