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Reversal of 2-Cys peroxiredoxin oligomerization by sulfiredoxin.
Biochem Biophys Res Commun. 2013 Mar 08; 432(2):291-5.BB

Abstract

Hydrogen peroxide (H(2)O(2)) regulates the structure and function of 2-Cys peroxiredoxins (Prxs). Upon oxidation by excess H(2)O(2), Prxs become overoxidized to a sulfinic acid of its peroxidatic cysteine residue, resulting in a structural change from a small oligomer with peroxidase function to a large oligomer with chaperone function. Then, sulfiredoxin (Srx) reduces the overoxidized Prxs by an ATP-dependent mechanism. Although Srx is known to repair the overoxidized forms of Prx, the role of Srx in the reversal of Prx oligomerization remains to be elucidated. Here we investigated whether Srx1 directly facilitates the dissociation of yeast Prx1 (YPrx1) from a high-molecular-weight (HMW) complex to a low-molecular-weight (LMW) complex in vitro. Srx1 reactivates the YPrx1 peroxidase activity that is inactivated by H(2)O(2), whereas it decreases the chaperone activity enhanced by H(2)O(2). We show that Srx1 dissociates the H(2)O(2)-induced HMW YPrx1 complex, and that the Srx1 Cys84 residue is critical for its dissociation. In contrast to wild-type Srx1, an inactive Srx1 mutant (Srx1-C84S) did not induce the reactivation of inactivated YPrx1 or dissociation of the HMW YPrx1 complex. We revealed that Srx1 interacts directly with YPrx1 in yeast cells using bimolecular fluorescence complementation. Taken together, these findings suggest that Srx1 regulates YPrx1 function and structure in yeast cells through a direct interaction.

Authors+Show Affiliations

Department of Molecular Medicine, Lee Gil Ya Cancer and Diabetes Institute, Gachon University, Incheon 406-799, Republic of Korea.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

23396059

Citation

Moon, Jeong Chan, et al. "Reversal of 2-Cys Peroxiredoxin Oligomerization By Sulfiredoxin." Biochemical and Biophysical Research Communications, vol. 432, no. 2, 2013, pp. 291-5.
Moon JC, Kim GM, Kim EK, et al. Reversal of 2-Cys peroxiredoxin oligomerization by sulfiredoxin. Biochem Biophys Res Commun. 2013;432(2):291-5.
Moon, J. C., Kim, G. M., Kim, E. K., Lee, H. N., Ha, B., Lee, S. Y., & Jang, H. H. (2013). Reversal of 2-Cys peroxiredoxin oligomerization by sulfiredoxin. Biochemical and Biophysical Research Communications, 432(2), 291-5. https://doi.org/10.1016/j.bbrc.2013.01.114
Moon JC, et al. Reversal of 2-Cys Peroxiredoxin Oligomerization By Sulfiredoxin. Biochem Biophys Res Commun. 2013 Mar 8;432(2):291-5. PubMed PMID: 23396059.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Reversal of 2-Cys peroxiredoxin oligomerization by sulfiredoxin. AU - Moon,Jeong Chan, AU - Kim,Gyeong Mi, AU - Kim,Eun-Kyung, AU - Lee,Hae Na, AU - Ha,Bin, AU - Lee,Sang Yeol, AU - Jang,Ho Hee, Y1 - 2013/02/08/ PY - 2013/01/28/received PY - 2013/01/30/accepted PY - 2013/2/12/entrez PY - 2013/2/12/pubmed PY - 2013/9/4/medline SP - 291 EP - 5 JF - Biochemical and biophysical research communications JO - Biochem Biophys Res Commun VL - 432 IS - 2 N2 - Hydrogen peroxide (H(2)O(2)) regulates the structure and function of 2-Cys peroxiredoxins (Prxs). Upon oxidation by excess H(2)O(2), Prxs become overoxidized to a sulfinic acid of its peroxidatic cysteine residue, resulting in a structural change from a small oligomer with peroxidase function to a large oligomer with chaperone function. Then, sulfiredoxin (Srx) reduces the overoxidized Prxs by an ATP-dependent mechanism. Although Srx is known to repair the overoxidized forms of Prx, the role of Srx in the reversal of Prx oligomerization remains to be elucidated. Here we investigated whether Srx1 directly facilitates the dissociation of yeast Prx1 (YPrx1) from a high-molecular-weight (HMW) complex to a low-molecular-weight (LMW) complex in vitro. Srx1 reactivates the YPrx1 peroxidase activity that is inactivated by H(2)O(2), whereas it decreases the chaperone activity enhanced by H(2)O(2). We show that Srx1 dissociates the H(2)O(2)-induced HMW YPrx1 complex, and that the Srx1 Cys84 residue is critical for its dissociation. In contrast to wild-type Srx1, an inactive Srx1 mutant (Srx1-C84S) did not induce the reactivation of inactivated YPrx1 or dissociation of the HMW YPrx1 complex. We revealed that Srx1 interacts directly with YPrx1 in yeast cells using bimolecular fluorescence complementation. Taken together, these findings suggest that Srx1 regulates YPrx1 function and structure in yeast cells through a direct interaction. SN - 1090-2104 UR - https://www.unboundmedicine.com/medline/citation/23396059/Reversal_of_2_Cys_peroxiredoxin_oligomerization_by_sulfiredoxin_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(13)00215-5 DB - PRIME DP - Unbound Medicine ER -