Oxidative stress induced by the photosensitizers neutral red (type I) or rose bengal (type II) in the light causes different molecular responses in Chlamydomonas reinhardtii

被引:41
作者
Fischer, BB [1 ]
Krieger-Liszkay, A [1 ]
Eggen, RIL [1 ]
机构
[1] Swiss Fed Inst Environm Sci & Technol, Dept Environm Technol, CH-8600 Dubendorf, Switzerland
关键词
Chlamydomonas reinhardtii; photooxidative stress; neutral red; rose bengal; singlet oxygen; DNA-microarray;
D O I
10.1016/j.plantsci.2004.10.008
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
The molecular defense mechanisms against photooxidative stress in photosynthetic organisms are essential to protect cells from damaging effects of high light illumination and photoinhibition but also to protect against effects by endogenous and exogenous photosensitizers. Here, we analyzed the genetic response of Chlaniydomonas reinhardtii to the model type I photosensitizer neutral red (NR) and the type II photosensitizer rose bengal (RB) using DNA-microarrays. Many oxidative and general stress response genes, which were also induced by other oxidative stress conditions, were strongly induced by NR. Only one gene was upregulated by RB, the glutathione (GSH) peroxidase homologous gene Gpxh, which was also induced by NR. In addition NR exposure resulted in the reduced expression of most nuclear photosynthetic genes and subunits of the light harvesting complex (LHC) indicating an effect on the photosynthetic activity. This is supported by a stimulation of singlet oxygen generation in NR-treated thylakoids. Thus, in C reinhardtii the Gpxh expression is most probably induced by the formation of singlet oxygen in both the NR and RB-treated cells via the activation of a very sensitive and specific sensor, whereas general oxidative stress response mechanisms seem to be involved in the response of most other genes to the type I photooxidative stress. (C) 2004 Elsevier Ireland Ltd. All rights reserved.
引用
收藏
页码:747 / 759
页数:13
相关论文
共 74 条
[21]   Induction of protein catabolism and the ubiquitin-proteasome pathway by mild oxidative stress [J].
Gomes-Marcondes, MCC ;
Tisdale, MJ .
CANCER LETTERS, 2002, 180 (01) :69-74
[22]   Isolation and characterization of a thioredoxin-dependent peroxidase from Chlamydomonas reinhardtii [J].
Goyer, A ;
Haslekås, C ;
Miginiac-Maslow, M ;
Klein, U ;
Le Marechal, P ;
Jacquot, JP ;
Decottignies, P .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2002, 269 (01) :272-282
[23]   Biologic and pharmacologic regulation of mammalian glutathione synthesis [J].
Griffith, OW .
FREE RADICAL BIOLOGY AND MEDICINE, 1999, 27 (9-10) :922-935
[25]   Selective degradation of oxidatively modified protein substrates by the proteasome [J].
Grune, T ;
Merker, K ;
Sandig, G ;
Davies, KJA .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2003, 305 (03) :709-718
[26]   Balance of power: a view of the mechanism of photosynthetic state transitions [J].
Haldrup, A ;
Jensen, PE ;
Lunde, C ;
Scheller, HV .
TRENDS IN PLANT SCIENCE, 2001, 6 (07) :301-305
[27]  
Harris E.H., 1989, CHLAMYDOMONAS SOURCE
[28]   A chloroplast DegP2 protease performs the primary cleavage of the photodamaged D1 protein in plant photosystem II [J].
Kirsten Haußühl ;
Bertil Andersson ;
Iwona Adamska .
The EMBO Journal, 2001, 20 (4) :713-722
[29]   The small, methionine-rich chloroplast heat-shock protein protects photosystem II electron transport during heat stress [J].
Heckathorn, SA ;
Downs, CA ;
Sharkey, TD ;
Coleman, JS .
PLANT PHYSIOLOGY, 1998, 116 (01) :439-444
[30]   Do oxidative stress conditions impairing photosynthesis in the light manifest as photoinhibition? [J].
Hideg, É ;
Kálai, T ;
Hideg, K ;
Vass, I .
PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES, 2000, 355 (1402) :1511-1516