Dual functions of Arabidopsis sulfiredoxin: Acting as a redox-dependent sulfinic acid reductase and as a redox-independent nuclease enzyme

被引:16
作者
Chi, Yong Hun
Kim, Sun Young
Jung, In Jung
Shin, Mi Rim
Jung, Young Jun
Park, Jin Ho
Lee, Eun Seon
Maibam, Punyakishore
Kim, Kang-San
Park, Joung Hun
Kim, Min Ji
Hwang, Gwang Yong
Lee, Sang Yeol [1 ]
机构
[1] Gyeongsang Natl Univ, Div Appl Life Sci, Program BK21, Jinju 660701, South Korea
关键词
Sulfiredoxin; DNA binding; Ca2+-dependent nuclease activity; OXIDATIVE STRESS; PARB PROTEIN; 2-CYS PEROXIREDOXIN; PLANT SULFIREDOXIN; REACTIVE OXYGEN; DNA DAMAGE; CYSTEINE; SEGREGATION; GLUTATHIONYLATION; PEROXIDASE;
D O I
10.1016/j.febslet.2012.08.002
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
070307 [化学生物学]; 071010 [生物化学与分子生物学];
摘要
Based on the fact that the amino acid sequence of sulfiredoxin (Srx), already known as a redox-dependent sulfinic acid reductase, showed a high sequence homology with that of ParB, a nuclease enzyme, we examined the nucleic acid binding and hydrolyzing activity of the recombinant Srx in Arabidopsis (AtSrx). We found that AtSrx functions as a nuclease enzyme that can use single-stranded and double-stranded DNAs as substrates. The nuclease activity was enhanced by divalent cations. Particularly, by point-mutating the active site of sulfinate reductase, Cys (72) to Ser (AtS-rx-C72S), we demonstrate that the active site of the reductase function of AtSrx is not involved in its nuclease function. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:3493 / 3499
页数:7
相关论文
共 38 条
[1]
Reactive oxygen intermediates mediate a systemic signal network in the establishment of plant immunity [J].
Alvarez, ME ;
Pennell, RI ;
Meijer, PJ ;
Ishikawa, A ;
Dixon, RA ;
Lamb, C .
CELL, 1998, 92 (06) :773-784
[2]
Evolution of eukaryotic cysteine sulfinic acid reductase, sulfiredoxin (Srx), from bacterial chromosome partitioning protein ParB [J].
Basu, MK ;
Koonin, EV .
CELL CYCLE, 2005, 4 (07) :947-952
[3]
ATP-dependent reduction of cysteine-sulphinic acid by S-cerevisiae sulphiredoxin [J].
Biteau, B ;
Labarre, J ;
Toledano, MB .
NATURE, 2003, 425 (6961) :980-984
[4]
Redox regulation: A broadening horizon [J].
Buchanan, BB ;
Balmer, Y .
ANNUAL REVIEW OF PLANT BIOLOGY, 2005, 56 :187-220
[5]
Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD [J].
Budanov, AV ;
Sablina, AA ;
Feinstein, E ;
Koonin, EV ;
Chumakov, PM .
SCIENCE, 2004, 304 (5670) :596-600
[6]
Protein S-glutathionylation: a regulatory device from bacteria to humans [J].
Dalle-Donne, Isabella ;
Rossi, Ranieri ;
Colombo, Graziano ;
Giustarini, Daniela ;
Milzani, Aldo .
TRENDS IN BIOCHEMICAL SCIENCES, 2009, 34 (02) :85-96
[7]
Plasmid segregation mechanisms [J].
Ebersbach, G ;
Gerdes, K .
ANNUAL REVIEW OF GENETICS, 2005, 39 :453-479
[8]
A novel role for human sulfiredoxin in the reversal of glutathionylation [J].
Findlay, Victoria J. ;
Townsend, Danyelle M. ;
Morris, Taylor E. ;
Fraser, Jacob P. ;
He, Lin ;
Tew, Kenneth D. .
CANCER RESEARCH, 2006, 66 (13) :6800-6806
[9]
Oxidants, oxidative stress and the biology of ageing [J].
Finkel, T ;
Holbrook, NJ .
NATURE, 2000, 408 (6809) :239-247
[10]
The ParB protein encoded by the RP4 par region is a Ca2+-dependent nuclease linearizing circular DNA substrates [J].
Grohmann, E ;
Stanzer, T ;
Schwab, H .
MICROBIOLOGY-UK, 1997, 143 :3889-3898