Molecular mechanism of the reduction of cysteine sulfinic acid of peroxiredoxin to cysteine by mammalian sulfiredoxin

被引:115
作者
Jeong, Woojin
Park, Sung Jun
Chang, Tong-Shin
Lee, Duck-Yeon
Rhee, Sue Goo
机构
[1] Ewha Womans Univ, Ctr Cell Signaling Res, Seoul 120750, South Korea
[2] Ewha Womans Univ, Div Mol Life Sci, Seoul 120750, South Korea
[3] NHLBI, Lab Cell Signaling, NIH, Bethesda, MD 20892 USA
关键词
D O I
10.1074/jbc.M511082200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Among many proteins with cysteine sulfinic acid (Cys-SO2H) residues, the sulfinic forms of certain peroxiredoxins (Prxs) are selectively reduced by sulfiredoxin (Srx) in the presence of ATP. All Srx enzymes contain a conserved cysteine residue. To elucidate the mechanism of the Srx-catalyzed reaction, we generated various mutants of Srx and examined their interaction with PrxI, their ATPase activity, and their ability to reduce sulfinic PrxI. Our results suggest that three surface-exposed amino acid residues, corresponding to Arg(50), Asp(57), and Asp(79) of rat Srx, are critical for substrate recognition. The presence of the sulfinic form (but not the reduced form) of PrxI induces the conserved cysteine of Srx to take the gamma-phosphate of ATP and then immediately transfers the phosphate to the sulfinic moiety of PrxI to generate a sulfinic acid phosphoryl ester (Prx-Cys-S(=O)OPO32-). This ester is reductively cleaved by a thiol molecule (RSH) such as GSH, thioredoxin, and dithiothreitol to produce a disulfide-S-monoxide (Prx-Cys-S(=O)-S-R). The disulfide-S-monoxide is further reduced through the oxidation of three thiol equivalents to complete the catalytic cycle and regenerate Prx-Cys-SH.
引用
收藏
页码:14400 / 14407
页数:8
相关论文
共 34 条
[1]   ATP-dependent reduction of cysteine-sulphinic acid by S-cerevisiae sulphiredoxin [J].
Biteau, B ;
Labarre, J ;
Toledano, MB .
NATURE, 2003, 425 (6961) :980-984
[2]   Oxidation of a eukaryotic 2-Cys peroxiredoxin is a molecular switch controlling the transcriptional response to increasing levels of hydrogen peroxide [J].
Bozonet, SM ;
Findlay, VJ ;
Day, AM ;
Cameron, J ;
Veal, EA ;
Morgan, BA .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (24) :23319-23327
[3]   The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization [J].
Canet-Avilés, RM ;
Wilson, MA ;
Miller, DW ;
Ahmad, R ;
McLendon, C ;
Bandyopadhyay, S ;
Baptista, MJ ;
Ringe, D ;
Petsko, GA ;
Cookson, MR .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (24) :9103-9108
[4]   AN IMPROVED METHOD FOR THIN-LAYER CHROMATOGRAPHY OF NUCLEOTIDE MIXTURES CONTAINING 32P-LABELED ORTHOPHOSPHATE [J].
CASHEL, M ;
LAZZARINI, RA ;
KALBACHER, B .
JOURNAL OF CHROMATOGRAPHY, 1969, 40 (01) :103-+
[5]   CLONING AND SEQUENCING OF THIOL-SPECIFIC ANTIOXIDANT FROM MAMMALIAN BRAIN - ALKYL HYDROPEROXIDE REDUCTASE AND THIOL-SPECIFIC ANTIOXIDANT DEFINE A LARGE FAMILY OF ANTIOXIDANT ENZYMES [J].
CHAE, HZ ;
ROBISON, K ;
POOLE, LB ;
CHURCH, G ;
STORZ, G ;
RHEE, SG .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1994, 91 (15) :7017-7021
[6]  
CHAE HZ, 1994, J BIOL CHEM, V269, P27670
[7]   DIMERIZATION OF THIOL-SPECIFIC ANTIOXIDANT AND THE ESSENTIAL ROLE OF CYSTEINE-47 [J].
CHAE, HZ ;
UHM, TB ;
RHEE, SG .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1994, 91 (15) :7022-7026
[8]   Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine [J].
Chang, TS ;
Jeong, W ;
Woo, HA ;
Lee, SM ;
Park, S ;
Rhee, SG .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (49) :50994-51001
[9]  
Claiborne A, 2001, ADV PROTEIN CHEM, V58, P215
[10]   Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7). A mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase. [J].
Fu, XY ;
Kassim, SY ;
Parks, WC ;
Heinecke, JW .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (44) :41279-41287