Abstract
We isolated the catA gene for the major vegetative catalase from Streptomyces coelicolor Müller. It encodes a polypeptide of 488 residues (55,440 Da) that is highly homologous to typical monofunctional catalases. We investigated catA expression by analyzing both catA mRNA and catalase activity. catA expression was increased by H2O2 treatment but did not increase during stationary phase. A putative catalase (CatB) cross-reactive with anti-CatA antibody appeared during stationary phase and in the aerial mycelium.
Full Text
The Full Text of this article is available as a PDF (1.1 MB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Bol D. K., Yasbin R. E. Analysis of the dual regulatory mechanisms controlling expression of the vegetative catalase gene of Bacillus subtilis. J Bacteriol. 1994 Nov;176(21):6744–6748. doi: 10.1128/jb.176.21.6744-6748.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Chen Z., Silva H., Klessig D. F. Active oxygen species in the induction of plant systemic acquired resistance by salicylic acid. Science. 1993 Dec 17;262(5141):1883–1886. doi: 10.1126/science.8266079. [DOI] [PubMed] [Google Scholar]
- Claiborne A., Fridovich I. Purification of the o-dianisidine peroxidase from Escherichia coli B. Physicochemical characterization and analysis of its dual catalatic and peroxidatic activities. J Biol Chem. 1979 May 25;254(10):4245–4252. [PubMed] [Google Scholar]
- Claiborne A., Malinowski D. P., Fridovich I. Purification and characterization of hydroperoxidase II of Escherichia coli B. J Biol Chem. 1979 Nov 25;254(22):11664–11668. [PubMed] [Google Scholar]
- Clare D. A., Duong M. N., Darr D., Archibald F., Fridovich I. Effects of molecular oxygen on detection of superoxide radical with nitroblue tetrazolium and on activity stains for catalase. Anal Biochem. 1984 Aug 1;140(2):532–537. doi: 10.1016/0003-2697(84)90204-5. [DOI] [PubMed] [Google Scholar]
- Fita I., Rossmann M. G. The active center of catalase. J Mol Biol. 1985 Sep 5;185(1):21–37. doi: 10.1016/0022-2836(85)90180-9. [DOI] [PubMed] [Google Scholar]
- González-Flecha B., Demple B. Metabolic sources of hydrogen peroxide in aerobically growing Escherichia coli. J Biol Chem. 1995 Jun 9;270(23):13681–13687. doi: 10.1074/jbc.270.23.13681. [DOI] [PubMed] [Google Scholar]
- Hansberg W., de Groot H., Sies H. Reactive oxygen species associated with cell differentiation in Neurospora crassa. Free Radic Biol Med. 1993 Mar;14(3):287–293. doi: 10.1016/0891-5849(93)90025-p. [DOI] [PubMed] [Google Scholar]
- Ivanova A., Miller C., Glinsky G., Eisenstark A. Role of rpoS (katF) in oxyR-independent regulation of hydroperoxidase I in Escherichia coli. Mol Microbiol. 1994 May;12(4):571–578. doi: 10.1111/j.1365-2958.1994.tb01043.x. [DOI] [PubMed] [Google Scholar]
- Kim H., Lee J. S., Hah Y. C., Roe J. H. Characterization of the major catalase from Streptomyces coelicolor ATCC 10147. Microbiology. 1994 Dec;140(Pt 12):3391–3397. doi: 10.1099/13500872-140-12-3391. [DOI] [PubMed] [Google Scholar]
- Loewen P. C., Switala J. Multiple catalases in Bacillus subtilis. J Bacteriol. 1987 Aug;169(8):3601–3607. doi: 10.1128/jb.169.8.3601-3607.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Navarro R. E., Stringer M. A., Hansberg W., Timberlake W. E., Aguirre J. catA, a new Aspergillus nidulans gene encoding a developmentally regulated catalase. Curr Genet. 1996 Mar;29(4):352–359. [PubMed] [Google Scholar]
- Schreck R., Rieber P., Baeuerle P. A. Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappa B transcription factor and HIV-1. EMBO J. 1991 Aug;10(8):2247–2258. doi: 10.1002/j.1460-2075.1991.tb07761.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Seah T. C., Bhatti A. R., Kaplan J. G. Novel catalatic proteins of bakers' yeast. I. An atypical catalase. Can J Biochem. 1973 Nov;51(11):1551–1555. doi: 10.1139/o73-208. [DOI] [PubMed] [Google Scholar]
- Seah T. C., Kaplan J. G. Purification and properties of the catalase of bakers' yeast. J Biol Chem. 1973 Apr 25;248(8):2889–2893. [PubMed] [Google Scholar]
- Smith C. P., Chater K. F. Structure and regulation of controlling sequences for the Streptomyces coelicolor glycerol operon. J Mol Biol. 1988 Dec 5;204(3):569–580. doi: 10.1016/0022-2836(88)90356-7. [DOI] [PubMed] [Google Scholar]
- Strohl W. R. Compilation and analysis of DNA sequences associated with apparent streptomycete promoters. Nucleic Acids Res. 1992 Mar 11;20(5):961–974. doi: 10.1093/nar/20.5.961. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Walker G. E., Dunbar B., Hunter I. S., Nimmo H. G., Coggins J. R. A catalase from Streptomyces coelicolor A3(2). Microbiology. 1995 Jun;141(Pt 6):1377–1383. doi: 10.1099/13500872-141-6-1377. [DOI] [PubMed] [Google Scholar]