Skip Navigation

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (24)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Kobayashi, M.
Right arrow Articles by Ikeuchi, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kobayashi, M.
Right arrow Articles by Ikeuchi, M.
Agricola
Right arrow Articles by Kobayashi, M.
Right arrow Articles by Ikeuchi, M.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Plant and Cell Physiology, 2004, Vol. 45, No. 3 290-299
© 2004 Oxford University Press

Response to Oxidative Stress Involves a Novel Peroxiredoxin Gene in the Unicellular Cyanobacterium Synechocystis sp. PCC 6803

Mari Kobayashi1, Tomokazu Ishizuka1, Mitsunori Katayama1, Minoru Kanehisa2, Maitrayee Bhattacharyya-Pakrasi3, Himadri B. Pakrasi3 and Masahiko Ikeuchi1,4

1 Department of Life Sciences (Biology), The University of Tokyo, Komaba, Meguro, Tokyo, 153-8902 Japan
2 Institute for Chemical Research, Kyoto University, Uji, Kyoto, 611-0011 Japan
3 Department of Biology, Washington University, St. Louis, MO 63130-4899, U.S.A.

Exposure to methyl viologen in the presence of light facilitates the production of superoxide that gives severe damage on photosynthetic apparatus as well as many cellular processes in cyanobacteria and plants. The effects of methyl viologen on global gene expression of a unicellular cyanobacterium Synechocystis sp. strain PCC 6803 were determined by DNA microarray. The ORFs sll1621, slr1738, slr0074, slr0075, and slr0589 were significantly induced by treatment of methyl viologen for 15 min commonly under conditions of normal and high light. One of these genes, slr1738, which encodes a ferric uptake repressor (Fur)-type transcriptional regulator, is located divergently next to another induced gene, sll1621, in the genome. We deleted slr1738, and compared the global gene expression patterns of this mutant to that of wild type under non-stressed conditions. It was found that sll1621 was derepressed to the greatest extent, while many other genes including slr0589 but not slr0074 or slr0075 were derepressed to lesser extent in the mutant. Genetic disruption of sll1621, which encodes a putative type 2 peroxiredoxin, indicates that it is essential for aerobic phototrophic growth in both liquid and solid media in high light and on solid medium even in low light. Slr1738 was prepared as a His-tagged recombinant protein and shown to specifically bind to the intergenic region between sll1621 and slr1738. The binding was enhanced by dithiothreitol and abolished by hydrogen peroxide. We concluded that the Fur homolog, Slr1738, plays a regulatory role in the induction of a potent antioxidant gene, sll1621, in response to oxidative stress.

4 Corresponding author: Email, mikeuchi{at}bio.c.u-tokyo.ac.jp; Fax, +81-3-5454-4337.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
J. Bacteriol.Home page
M. E. Perez-Perez, A. Mata-Cabana, A. M. Sanchez-Riego, M. Lindahl, and F. J. Florencio
A Comprehensive Analysis of the Peroxiredoxin Reduction System in the Cyanobacterium Synechocystis sp. Strain PCC 6803 Reveals that All Five Peroxiredoxins Are Thioredoxin Dependent
J. Bacteriol., December 15, 2009; 191(24): 7477 - 7489.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
T. Midorikawa, K. Matsumoto, R. Narikawa, and M. Ikeuchi
An Rrf2-Type Transcriptional Regulator Is Required for Expression of psaAB Genes in the Cyanobacterium Synechocystis sp. PCC 6803
Plant Physiology, October 1, 2009; 151(2): 882 - 892.
[Abstract] [Full Text] [PDF]


Home page
J Exp BotHome page
M. Bernroitner, M. Zamocky, P. G. Furtmuller, G. A. Peschek, and C. Obinger
Occurrence, phylogeny, structure, and function of catalases and peroxidases in cyanobacteria
J. Exp. Bot., February 1, 2009; 60(2): 423 - 440.
[Abstract] [Full Text] [PDF]


Home page
Mol Biol EvolHome page
K. Vandenbroucke, S. Robbens, K. Vandepoele, D. Inze, Y. Van de Peer, and F. Van Breusegem
Hydrogen Peroxide-Induced Gene Expression across Kingdoms: A Comparative Analysis
Mol. Biol. Evol., March 1, 2008; 25(3): 507 - 516.
[Abstract] [Full Text] [PDF]


Home page
Brief Funct Genomic ProteomicHome page
B. D. l. Cerda, O. Castielli, R. V. Duran, J. A. Navarro, M. Hervas, and M. A. D. l. Rosa
A proteomic approach to iron and copper homeostasis in cyanobacteria
Brief Funct Genomic Proteomic, January 11, 2008; (2008) elm030v1.
[Abstract] [Full Text] [PDF]


Home page
Plant Cell PhysiolHome page
S. Hishiya, W. Hatakeyama, Y. Mizota, N. Hosoya-Matsuda, K. Motohashi, M. Ikeuchi, and T. Hisabori
Binary Reducing Equivalent Pathways Using NADPH-Thioredoxin Reductase and Ferredoxin-Thioredoxin Reductase in the Cyanobacterium Synechocystis sp. Strain PCC 6803
Plant Cell Physiol., January 1, 2008; 49(1): 11 - 18.
[Abstract] [Full Text] [PDF]


Home page
J Exp BotHome page
T. Stork, K.-P. Michel, E. K. Pistorius, and K.-J. Dietz
Bioinformatic analysis of the genomes of the cyanobacteria Synechocystis sp. PCC 6803 and Synechococcus elongatus PCC 7942 for the presence of peroxiredoxins and their transcript regulation under stress
J. Exp. Bot., December 1, 2005; 56(422): 3193 - 3206.
[Abstract] [Full Text] [PDF]


Home page
Plant Cell PhysiolHome page
M. Kobayashi, K. Okada, and M. Ikeuchi
A Suppressor Mutation in the {alpha}-Phycocyanin Gene in the Light/Glucose-sensitive Phenotype of the psbK-disruptant of the Cyanobacterium Synechocystis sp. PCC 6803
Plant Cell Physiol., September 1, 2005; 46(9): 1561 - 1567.
[Abstract] [Full Text] [PDF]


Home page
J BiochemHome page
K. Okajima, S. Yoshihara, Y. Fukushima, X. Geng, M. Katayama, S. Higashi, M. Watanabe, S. Sato, S. Tabata, Y. Shibata, et al.
Biochemical and Functional Characterization of BLUF-Type Flavin-Binding Proteins of Two Species of Cyanobacteria
J. Biochem., June 1, 2005; 137(6): 741 - 750.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
N. Hosoya-Matsuda, K. Motohashi, H. Yoshimura, A. Nozaki, K. Inoue, M. Ohmori, and T. Hisabori
Anti-oxidative Stress System in Cyanobacteria: SIGNIFICANCE OF TYPE II PEROXIREDOXIN AND THE ROLE OF 1-Cys PEROXIREDOXIN IN SYNECHOCYSTIS SP. STRAIN PCC 6803
J. Biol. Chem., January 7, 2005; 280(1): 840 - 846.
[Abstract] [Full Text] [PDF]



Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.