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J. Biol. Chem., Vol. 278, Issue 37, 34952-34958, September 12, 2003

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The Protein Interaction of Saccharomyces cerevisiae Cytoplasmic Thiol Peroxidase II with SFH2p and Its in Vivo Function^*

Mee-Kyung Cha  , Seung-Keun Hong , Young-Mee Oh and Il-Han Kim ¶

From the Department of Biochemistry, Paichai University, 439-6 Doma-2-Dong Seo-Gu, Taejon 302-735, Republic of Korea

Previously, we reported that the yeast cytoplasmic thiol peroxidase type II isoform (cTPx II), a member of the TSA/AhpC family, showed a very low peroxidase activity when compared with other cytoplasmic yeast isoforms, and that cTPx II mutant (cTPx II) showed a severe growth retardation compared with that of the wild-type cells. To reveal the physiological function of cTPx II in yeast cell growth, we searched for proteins which react with cTPx II. In this study, we identified a novel interaction between cTPx II and CSR1p using the yeast two-hybrid system. CSR1p (SFH2p) has been known to be one member of Sec14 homologous (SFH2) proteins. SFH2p exhibits phosphatidylinositol transfer protein activity. Interestingly, we found that cTPx II selectively bound to SFH2p among the five types of SFH proteins and Sec14p. The interaction required the dimerization of cTPx II. In addition, SFH2p also specifically bound to cTPx II among the yeast thiol peroxidase isoforms. The selective interaction of the dimer form of cTPx II (the oxidized form) with SFH2p was also confirmed by glutathione S-transferase pull-down and immunoprecipitation assays. The growth retardation, clearly reflected by the length of the lag phase, of cTPx II was rescued by deleting SFH2p in the cTPx II strain. The SFH2 strain did not show any growth retardation. In addition, the double mutant showed a higher susceptibility to oxidative stress. This finding provides the first in vivo demonstration of the specific interaction of cTPx II with SFH2p in an oxidative stress-sensitive manner and a novel physiological function of the complex of cTPx II and SFH2p.

Received for publication, February 20, 2003 , and in revised form, June 18, 2003.

^* This work was supported by Korea Research Foundation Grant KRF-2001-015-DP0343. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

These authors made equal contribution to this work and should both be considered as first author.

Present address: Laboratory of Biochemistry, NHLBI, National Institutes of Health, Bethesda, MD 20892.

^¶ To whom correspondence should be addressed. Tel.: 82-42-520-5379; E-mail: ihkim{at}mail.paichai.ac.kr.

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