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Journal of Bacteriology, June 2004, p. 3331-3345, Vol. 186, No. 11
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.11.3331-3345.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Differential Gene Expression in Response to Hydrogen Peroxide and the Putative PerR Regulon of Synechocystis sp. Strain PCC 6803{ddagger}

Hong Li ,1,{dagger},§ Abhay K. Singh,1,{dagger} Lauren M. McIntyre,2 and Louis A. Sherman1*

Department of Biological Sciences,1 Computational Genomics and Department of Agronomy, Purdue University, West Lafayette, Indiana 479072

Received 21 November 2003/ Accepted 20 February 2004

We utilized a full genome cDNA microarray to identify the genes that comprise the peroxide stimulon in the cyanobacterium Synechocystis sp. strain PCC 6803. We determined that a gene (slr1738) encoding a protein similar to PerR in Bacillus subtilis was induced by peroxide. We constructed a PerR knockout strain and used it to help identify components of the PerR regulon, and we found that the regulatory properties were consistent with the hypothesis that PerR functions as a repressor. This effort was guided by finding putative PerR boxes in positions upstream of specific genes and by careful statistical analysis. PerR and sll1621 (ahpC), which codes for a peroxiredoxin, share a divergent promoter that is regulated by PerR. We found that isiA, encoding a Chl protein that is induced under low-iron conditions, was strongly induced by a short-term peroxide stress. Other genes that were strongly induced by peroxide included sigD, sigB, and genes encoding peroxiredoxins and Dsb-like proteins that have not been studied yet in this strain. A gene (slr1894) that encoded a protein similar to MrgA in B. subtilis was upregulated by peroxide, and a strain containing an mrgA knockout mutation was highly sensitive to peroxide. A number of genes were downregulated, including key genes in the chlorophyll biosynthesis pathway and numerous regulatory genes, including those encoding histidine kinases. We used PerR mutants and a thioredoxin mutant (TrxA1) to study differential expression in response to peroxide and determined that neither PerR nor TrxA1 is essential for the peroxide protective response.

* Corresponding author. Mailing address: Department of Biological Sciences, Purdue University, West Lafayette, IN 47907. Phone: (765) 494-8106. Fax: (765) 496-1496. E-mail: lsherman{at}bilbo.bio.purdue.edu.

{ddagger} Supplemental material for this article may be found at http://jb.asm.org/.

{dagger} H.L. and A.K.S. participated equally in the performance of this project.

§ Present address: Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, MO 63110.

Journal of Bacteriology, June 2004, p. 3331-3345, Vol. 186, No. 11
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.11.3331-3345.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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