Oxidative stress in Synechococcus sp strain PCC 7942:: Various mechanisms for H2O2 detoxification with different physiological roles

被引:55
作者
Perelman, A [1 ]
Uzan, A [1 ]
Hacohen, D [1 ]
Schwarz, R [1 ]
机构
[1] Bar Ilan Univ, Fac Life Sci, IL-52900 Ramat Gan, Israel
关键词
D O I
10.1128/JB.185.12.3654-3660.2003
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
This study focuses on the mechanisms for hydrogen peroxide detoxification in Synechococcus sp. strain PCC 7942. To gain better understanding of the role of different routes of hydrogen peroxide detoxification, we inactivated tpl4 (thioredoxin-peroxidase-like), which we recently identified. In addition, we inactivated the gene encoding catalase-peroxidase and examined the ability to detoxify H2O2 and to survive oxidative stress in both of the single mutants and in the double mutant. Surprisingly, we observed that the double mutant survived H2O2 concentrations that the single catalase-peroxidase mutant could not tolerate. This phenotype correlated with an increased ability of the double mutant to detoxify externally added H2O2 compared to the catalase-peroxidase mutant. Therefore, our studies suggested the existence of a hydrogen peroxide detoxification activity in addition to catalase-peroxidase and thioredoxin-peroxidase. The rate of detoxification of externally added H2O2 was similar in the wild-type and the TplA mutant cells, suggesting that, under these conditions, catalase-peroxidase activity was essential for this process and TplA was dispensable. However, during excessive radiation, conditions under which the cell might experience oxidative stress, TplA appears to be essential for growth, and cells lacking it cannot compete with the wild-type strain. Overall, these studies suggested different physiological roles for various cellular hydrogen peroxide detoxification mechanisms in Synechococcus sp. strain PCC 7942.
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页码:3654 / 3660
页数:7
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共 38 条
[1]  
[Anonymous], 1983, COLD SPRING HARBOR L
[2]   The water-water cycle in chloroplasts: Scavenging of active oxygens and dissipation of excess photons [J].
Asada, K .
ANNUAL REVIEW OF PLANT PHYSIOLOGY AND PLANT MOLECULAR BIOLOGY, 1999, 50 :601-639
[3]   Primary structure and expression of plant homologues of animal and fungal thioredoxin-dependent peroxide reductases and bacterial alkyl hydroperoxide reductases [J].
Baier, M ;
Dietz, KJ .
PLANT MOLECULAR BIOLOGY, 1996, 31 (03) :553-564
[4]   Protective function of chloroplast 2-cysteine peroxiredoxin in photosynthesis. Evidence from transgenic Arabidopsis [J].
Baier, M ;
Dietz, KJ .
PLANT PHYSIOLOGY, 1999, 119 (04) :1407-1414
[5]   The complete genome sequence of Escherichia coli K-12 [J].
Blattner, FR ;
Plunkett, G ;
Bloch, CA ;
Perna, NT ;
Burland, V ;
Riley, M ;
ColladoVides, J ;
Glasner, JD ;
Rode, CK ;
Mayhew, GF ;
Gregor, J ;
Davis, NW ;
Kirkpatrick, HA ;
Goeden, MA ;
Rose, DJ ;
Mau, B ;
Shao, Y .
SCIENCE, 1997, 277 (5331) :1453-+
[7]  
CHAE HZ, 1994, J BIOL CHEM, V269, P27670
[8]   A SMALL POLYPEPTIDE TRIGGERS COMPLETE DEGRADATION OF LIGHT-HARVESTING PHYCOBILIPROTEINS IN NUTRIENT-DEPRIVED CYANOBACTERIA [J].
COLLIER, JL ;
GROSSMAN, AR .
EMBO JOURNAL, 1994, 13 (05) :1039-1047
[9]   CHLOROSIS INDUCED BY NUTRIENT DEPRIVATION IN SYNECHOCOCCUS SP STRAIN PCC-7942 - NOT ALL BLEACHING IS THE SAME [J].
COLLIER, JL ;
GROSSMAN, AR .
JOURNAL OF BACTERIOLOGY, 1992, 174 (14) :4718-4726
[10]   Catalase-deficient tobacco plants:: tools for in planta studies on the role of hydrogen peroxide [J].
Dat, JF ;
Inzé, D ;
Van Breusegem, F .
REDOX REPORT, 2001, 6 (01) :37-42