Nucleotide sequence of the Mycobacterium leprae katG region

Journal of Bacteriology

Volumn 179, Issue 9, 1997, Pages 3053-3057

  Nakata, Noboru ^a   Matsuoka, Masanori ^a   Kashiwabara, Yoshiko ^a   Okada, Nobuhiko ^b   Sasakawa, Chihiro ^b  

^a NATIONAL INSTITUTE OF INFECTIOUS DISEASES   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL DNA; CATALASE; PEROXIDASE;

ARTICLE; DNA PROBE; GENE DELETION; MYCOBACTERIUM LEPRAE; NONHUMAN; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; SOUTHERN BLOTTING;

EID: 0030903166     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.9.3053-3057.1997     Document Type: Article

References (27)

1. Barry, V. C., M. L. Conalty, J. M. Denneny, and F. Winder. 1956. Peroxide formation in bacteriological media. Nature (London) 178:596-597.
2. Beaman, L., and B. L. Beaman. 1984. The role of oxygen and its derivatives in microbial pathogenesis and host defense. Annu. Rev. Microhiol. 38:127-148.
3. Dhandayuthapani, S., M. J. Banu, and Y. Kashiwabara. 1994. Cloning and sequence determination of the gene coding for the elongation factor Tu of Mycobacterium leprae. J. Biochem. (Tokyo) 115:664-669.
4. Fickett, J. W. 1982. Recognition of protein coding regions in DNA sequences. Nucleic Acids Res. 10:5303-5318.
5. Heym, B., Y. Zhang, S. Poulet, D. Young, and S. T. Cole. 1993. Characterization of the kutG gene encoding a catalase-peroxidase required for the isoniazid susceptibility of Mycobacterium tuberculosis. J. Bacteriol. 175:4255-4259.
6. Levy, L. 1976. Studies of the mouse footpad technique for cultivation of Mycobacterium leprae. III. Doubling time during logarithmic multiplication. Lepr. Rev. 47:103-116.
7. Loewen, P. C., J. Switara, and B. L. Triggs-Raine. 1985. Catalasc HPI and HPII in Escherichia coli are induced independently. Arch. Biochem. Biophys. 243:144-149.
8. Lygren, S. T., O. Cross, H. Bercouvier, and L. G. Wayne. 1986. Catalases, peroxidases,. and Superoxide dismutases in Mycobacterium leprae and other mycobacteria studied by crossed immunoelectrophoresis and polyacrylamide gel electrophoresis. Infect. Immun. 54:666-672.
9. Mayer, B. K., and J. O. Falkinham III. 1986. Catalase activity and its heat inactivation for differentiation of Mycobacterium avium, Mycobacterium iniracellulare, and Mycobacterium scrofulaceum. Int. J. Syst. Bacteriol. 36:207-212.
10. Middlebrook, G. 1954. Isoniazid-resislance and catalase activity of tuberele bacilli. Am. Rev. Tuberc. 69:471-4172.
11. Milano, A., E. De Rossi, L. Gusberti, B. Heym, P. Marone, and G. Riccardi. 1996. The katE gene, which encodes the catalase HPII of Mycobacterium avium. Mol. Microhiol. 19:113-123.
12. Morris, S. L., J. Nair, and D. A. Rouse. 1992. The catalase-peroxidase of Mycobacterium intracellulare: nucleotide sequence analysis and expression in Escherichia coli. J. Gen. Microhiol. 138:2363-2370.
13. Morse, W. C., O. L. Weiser, D. M. Kuhns, M. Fusillo. M. C. Dail, and J. R. Evance. 1954. Study of the virulence of isoniazid-resistant tubercle bacilli in guinea pigs and mice. Am. Rev. Tuberc. 69:464-468.
14. O'Brien, S., P. S. Jackett, D. B. Lowrie, and P. W. Andrew. 1991. Guinea pig alveolar macrophages kill Mycobacterium tuberculosis in vitro, but killing is independent of susceptibility to hydrogen peroxide or triggering of the respiratory burst. Microb. Pathog. 10:199-207.
15. Prabhakaran, K. 1967. Metabolism of Mycobacterium leprae separated from human leprosy nodules. Int. J. Lepr. 35:34-41.
16. Triggs-Raine, B. L., B. W. Doble, M. R. Mulvey, P. A. Sorby, and P. C. Loewen. 1988. Nucleotide sequence of katG. encoding catalase HPI of Escherichia coli. J. Bacteriol. 170:4415-4419.
17. von Ossowski, J., M. R. Mulvey, P. A. Leco, A. Borys, and P. C. Loewen. 1991. Nucleotide sequence of Escherichia coli katE, which encodes catalase HPII. J. Bacteriol. 173:514-520.
18. Walker, L., and D. B. Lowrie. 1981. Killing of Mycobacterium microti by immunolngically activated macrophages. Nature (London) 293:69-70.
19. Wayne, L. G., and G. A. Diaz. 1976. Immunoprecipitation studies of mycobacterial catalase. Int. J. Syst. Bacteriol. 26:38-44.
20. Wayne, L. G., and G. A. Diaz. 1982. Serological, taxonomic, and kinetic studies of the T and M classes of mycobacterial catalase. Int. J. Syst. Bacteriol. 32:296-304.
21. Wayne, L. G., and G. A. Diaz. 1986. Differentiation between T-catalases derived from Mycobacterium avium and Mycobacterium intracellulare by a solid-phase immunosorbent assay. Int. J. Syst. Bacteriol. 36:363-367.
22. Welinder, K. G. 1991. Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamily. Biochim. Biophys. Acta 1080: 215-220.
23. Wheeler, P. R., and D. Gregory. 1980. Superoxide dismutase, peroxidatic activity and catalase in Mycobacterium leprae purified from armadillo liver. J. Gen. Microbiol. 121:457-464.
24. Williams, D. L., T. P. Gillis, and F. Portaels. 1990. Geographically distinct isolates of Mycobacterium leprae exhibit no genotypic diversity by restriction fragment-length polymorphism analysis. Mol. Microbiol. 4:1653-1659.
25. Woods, S. A., and S. T. Cole. 1990. A family of dispersed repeats in Mycobacterium leprae. Mol. Microbiol. 4:1745-1751.
26. Zhang, Y., T. Garbe, and D. Young. 1993. Transformation with katG restores isoniazid-sensitivity in Mycobacterium tuberculosis isolates resistant to a range of drug concentrations. Mol. Microbiol. 8:521-524.
27. Zhang, Y., B. Heym, B. Allen, D. Young, and S. Cole. 1992. The catalaseperoxidase gene and isoniazid resistance of Mycobacterium tuberculosis. Nature (London) 358:591-593.