Insertional inactivation of Streptococcus pyogenes sod suggests that prtF is regulated in response to a superoxide signal

Journal of Bacteriology

Volumn 178, Issue 15, 1996, Pages 4688-4695

  Gibson, Carmela M ^a   Caparon, Michael G ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FIBRONECTIN; SUPEROXIDE; SUPEROXIDE DISMUTASE;

ARTICLE; BACTERIAL GROWTH; CONTROLLED STUDY; EXTRACELLULAR MATRIX; GENE EXPRESSION REGULATION; GENE INSERTION; GENE REPRESSION; NONHUMAN; PRIORITY JOURNAL; SIGNAL TRANSDUCTION; STREPTOCOCCUS PYOGENES;

BACTERIA (MICROORGANISMS); STREPTOCOCCUS PYOGENES;

EID: 0029785171     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.15.4688-4695.1996     Document Type: Article

References (46)

1. Beauchamp, C. D., and I. Fridovich. 1971. Superoxide dismutase: improved assays and an assay applicable to acrylamide gel. Anal. Biochem. 44:276-287.
2. 1a.Boyer, H. W., and D. Roulland-Dussoix. 1969. A complementation analysis of the restriction and modification of DNA in Escherichia coli. J. Mol. Biol. 41:459-472.
3. Britton, L., D. Malinowski, and I. Fridovich. 1978. Superoxide dismutase and oxygen metabolism in Streptococcus faecalis and comparisons with other organisms. J. Bacteriol. 134:229-236.
4. Caparon, M. G., R. T. Geist, J. Perez-Casal, and J. R. Scott. 1992. Environmental regulation of virulence in group A streptococci: transcription of the gene encoding M protein is stimulated by carbon dioxide. J. Bacteriol. 174:5693-5701.
5. Caparon, M. G., and J. R. Scott. 1987. Identification of a gene that regulates expression of M protein, the major virulence determinant of group A streptococci. Proc. Natl. Acad. Sci. USA 84:8677-8681.
6. Caparon, M. G., and J. R. Scott. 1991. Genetic manipulation of the pathogenic streptococci. Methods Enzymol. 204:556-586.
7. Chen, C., N. Bormann, and P. P. Cleary. 1993. VirR and Mry are homologous trans-acting regulators of M protein and C5a peptidase expression in group A streptococci. Mol. Gen. Genet. 241:685-693.
8. Chen, L., and J. D. Helmann. 1995. Bacillus subtilis MrgA is a Dps (PexB) homologue: evidence for metalloregulation of an oxidative-stress gene. Mol. Microbiol. 18:295-300.
9. Chen, L., L. Keramati, and J. D. Helmann. 1995. Coordinate regulation of Bacillus subtilis peroxide stress genes by hydrogen peroxide and metal ions. Proc. Natl. Acad. Sci. USA 92:8190-8194.
10. Claiborne, A., R. P. Ross, and D. Parsonage. 1992. Flavin-linked peroxide reductases: protein-sulfenic acids and the oxidative stress response. Trends Biochem. Sci. 17:183-186.
11. Cleary, P. P., and A. Larkin. 1979. Hyaluronic acid capsule: strategy for oxygen resistance in group A streptococci. J. Bacteriol. 140:1090-1097.
12. DiRita, V. J., and J. J. Mekalanos. 1989. Genetic regulation of bacterial virulence. Annu. Rev. Genet. 23:455-482.
13. Dowds, B. C. A. 1994. The oxidative stress response in Bacillus subtilis. FEMS Microbiol. Lett. 124:255-264.
14. Eaton, T., C. Shearman, and M. Gasson. 1993. Cloning and sequence anal- ysis of the dnaK gene region of Lactococcus lactis subsp. lactis. J Gen. Microbiol. 139:3253-3264.
15. Farr, S. B., and T. Kogoma. 1991. Oxidative stress responses in Escherichia coli and Salmonella typhimurium. Microbiol. Rev. 55:561-585.
16. Fogg, G. C., C. M. Gibson, and M. G. Caparon. 1994. The identification of rofA, a positive-acting regulatory component of prtF expression: use of a mγλ-based shuttle mutagenesis strategy in Streptococcus pyogenes. Mol. Microbiol. 11:671-684.
17. Hanski, E., and M. G. Caparon. 1992. Protein F. a fibronectin-binding protein, is an adhesin of the group A streptococcus Streptococcus pyogenes. Proc. Natl. Acad. Sci. USA 89:6172-6176.
18. Hanski, E., P. A. Horwitz, and M. G. Caparon. 1992. Expression of protein F, the fibronectin-binding protein of Streptococcus pyogenes, JRS4, in heterologous streptococcal and enterococcal strains promotes their adherence to respiratory epithelial cells. Infect. Immun. 60:5119-5125.
19. Kushner, S. R. 1978. An improved method for transformation of Escherichia coli with ColE1-derived plasmids, p. 17-2.3. In H. W. Boyer and S. Micosia (ed.), Genetic engineering. Elsevier/North-Holland Biomedical Press, New York.
20. Lee, J. Y., and M. G. Caparon. 1996. An oxygen-induced, but protein F-independent, fibronectin binding pathway in Streptococcus pyogenes. Infect. Immun. 64:413-421.
21. Liochev, S. I., and I. Fridovich. 1992. Fumarase C. the stable fumarase of Escherichia coli, is controlled by the soxRS regulon. Proc. Natl. Acad. Sci. USA 89:5892-5896.
22. Miller, J. F., J. J. Mekalanos, and S. Falkow. 1989. Coordinate regulation of signal transduction in the control of bacterial virulence. Science 243:916-921.
23. Nakayama, K. 1992. Nucleotide sequence of Streptococcus mutans superoxide dismutase gene and isolation of insertion mutants. J. Bactcriol. 174:4928-4934.
24. Okada, N., R. T. Geist, and M. G. Caparon. 1993. Positive transcriptional control of mry regulates virulence in the group A streptococcus. Mol. Microbiol. 7:893-903.
25. Parker, M. W., and C. C. F. Blake. 1988. Iron- and manganese-containing superoxide dismutases can be distinguished by analysis of their primary structures. FEBS Lett. 229:377-382.
26. Perez-Casal, J., M. G. Caparon, and J. R. Scott. 1991. Mry, a trans-acting positive regulator of the M protein gene of Streptococcus pyogenes with similarity to the receptor proteins of two-component regulatory systems. J. Bacteriol. 173:2617-2624.
27. Podbielski, A., J. A. Peterson, and P. Clearly. 1992. Surface protein-CAT reporter fusions demonstrate differential gene expression in the vir regulon of Streptococcus pyogenes. Mol. Microbiol. 6:2253-2265.
28. Privalle, C. T., and I. Fridovich. 1992. Transcriptional and maturational effects of manganese and iron on the biosynthesis of manganese-superoxide in Escherichia coli. J. Biol. Chem. 267:9140-9145.
29. Ross, R. P., and A. Claiborne. 1991. Cloning, sequence and overexpression of NADH peroxidase from Streptococcus faecalis 10C1: structural relationship with the flavoprotein disulfide reductases. J. Mol. Biol. 221:857-871.
30. Ross, R. P., and A. Claiborne. 1992. Molecular cloning and analysis of the gene encoding the NADH oxidase from Streptococcus faecalis 10C1: comparison with NADH peroxidase and the flavoprotein disulfide reductases. J. Mol. Biol. 227:658-671.
31. Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463-5467.
32. 2. Biochim. Biophys. Acta 1216:186-190.
33. Scott, J. R. 1972. A turbid plaque-forming mutant of phage P1 that cannot lysogenize Escherichia coli. Virology 62:344-349.
34. - by transfer of a plasmid containing an M6 gene. J. Exp. Med. 164:1641-1651.
35. Shaw, W. V. 1975. Chloramphenicol acetyltransferase from chloramphenicol-resistant bacteria. Methods Enzymol. 43:737-755.
36. Simpson, W. J., D. LaPenta, C. Chen, and P. Cleary. 1990. Coregulation of type 12 M protein and streptococcal C5a peptidase genes in group A streptococci: evidence for a virulence regulon controlled by the virR locus. J. Bacteriol. 172:696-700.
37. Smith, P. K., K. I. Krohn, G. T. Hermanson, A. K. Malia, F. J. H. Gartner, M. D. Provenzano, E. K. Fujimoto, N. M. Goeke, B. J. Olsen, and D. C. Klenk. 1985. Measurement of protein using bicinchoninic acid. Anal. Biochem. 150:76-85.
38. Southern, E. M. 1975. Detection of specific sequences among DNA fragments separated by gel electrophoresis. J. Mol. Biol. 98:503-517.
39. Stevens, D. L. 1992. Invasive group A streptococcus infections. Clin. Infect. Dis. 14:2-13.
40. VanHeyningen, T., G. Fogg, D. Yates, E. Hanski, and M. Caparon. 1993. Adherence and fibronectin binding are environmentally regulated in the group A streptococci. Mol. Microbiol. 9:1213-1222.
41. Vieira, J., and J. Messing. 1982. The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene 19:259-268.
42. Völker, D., S. Englemann, B. Maul, S. Riethdorf, A. Völker, R. Schmid, H. Mach and M. Hecker. 1994. Analysis of the induction of general stress proteins of Bacillus subtilis. Microbiology 140:741-752.
43. B of Bacillus subtilis in response to environmental and metabolic stress. J. Baeteriol. 177:3771-3780.
44. Wannamaker, L. W. 1970. Differences between streptococcal infections of the throat and of the skin. N. Engl. J. Med. 282:23-30.
45. Wu, J., and B. Weiss. 1991. Two divergently transcribed genes, soxR and soxS, control a superoxide response regulon of Escherichia coli. J. Bacteriol. 173:2864-2871.
46. Zitzelberger, W., F. Gotz, and K. H. Schleifer. 1984. Distribution of superoxide dismutases, oxidases, and NADH peroxidase in various streptococci. FEMS Microbiol. Lett. 21:243-246.