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Volumn 47, Issue 1, 2003, Pages 188-195

Exploring the structure and function of the mycobacterial KatG protein using trans-dominant mutants

Author keywords

[No Author keywords available]

Indexed keywords

CATALASE; ISONIAZID; KATG PROTEIN; PEROXIDASE; UNCLASSIFIED DRUG;

EID: 0037226402     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.47.1.188-195.2003     Document Type: Article
Times cited : (19)

References (39)
  • 2
    • 41049100518 scopus 로고
    • A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase
    • Beers, R. F., and I. W. Sizer. 1952. A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J. Biol. Chem. 195:133-140.
    • (1952) J. Biol. Chem. , vol.195 , pp. 133-140
    • Beers, R.F.1    Sizer, I.W.2
  • 3
    • 0016425962 scopus 로고
    • The steady-state kinetics of peroxidase with 2′,2′-azino-di-(3-ethyl-benzathiazoline-6-sulphonic acid) as chromagen
    • Childs, R. E., and W. G. Bardsley. 1975. The steady-state kinetics of peroxidase with 2′,2′-azino-di-(3-ethyl-benzathiazoline-6-sulphonic acid) as chromagen. Biochem. J. 145:93-103.
    • (1975) Biochem. J. , vol.145 , pp. 93-103
    • Childs, R.E.1    Bardsley, W.G.2
  • 4
    • 0024558335 scopus 로고
    • One-step preparation of competent Escherichia coli: Transformation and storage of bacterial cells in the same solution
    • Chung, C. T., S. L. Niemela, and R. H. Miller. 1989. One-step preparation of competent Escherichia coli: transformation and storage of bacterial cells in the same solution. Proc. Natl. Acad. Sci. USA 86:2172-2175.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 2172-2175
    • Chung, C.T.1    Niemela, S.L.2    Miller, R.H.3
  • 6
    • 0033581124 scopus 로고    scopus 로고
    • Consensus statement. Global burden of tuberculosis: Estimated incidence, prevalence, and mortality by country
    • Dye, C., S. Scheele, P. Dolin, V. Pathania, M. C. Raviglion, et al.. 1999. Consensus statement. Global burden of tuberculosis: estimated incidence, prevalence, and mortality by country. JAMA 282:677-686.
    • (1999) JAMA , vol.282 , pp. 677-686
    • Dye, C.1    Scheele, S.2    Dolin, P.3    Pathania, V.4    Raviglion, M.C.5
  • 7
    • 0002515716 scopus 로고    scopus 로고
    • Antimicrobial combinations
    • V. Lorian (ed.). Williams and Wilkins, Baltimore, Md.
    • Eliopoulos, G. M., and R. C. Moellering. 1996. Antimicrobial combinations, p. 330-396. In V. Lorian (ed.), Antibiotics in laboratory medicine. Williams and Wilkins, Baltimore, Md.
    • (1996) Antibiotics in Laboratory Medicine , pp. 330-396
    • Eliopoulos, G.M.1    Moellering, R.C.2
  • 8
    • 0021723457 scopus 로고
    • Crystal structure of yeast cytochrome C peroxidase refined at the 1.7 angstrom resolution
    • Finzel, B. C., T. L. Poulos, and J. Kraut. 1984. Crystal structure of yeast cytochrome C peroxidase refined at the 1.7 angstrom resolution. J. Biol. Chem. 259:13027-13036.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13027-13036
    • Finzel, B.C.1    Poulos, T.L.2    Kraut, J.3
  • 9
    • 0028960179 scopus 로고
    • Missense mutations in the catalase-peroxidase gene, katG, are associated with isoniazid resistance in Mycobacterium tuberculosis
    • Heym, B., P. M. Alzari, N. Honore, and S. T. Cole. 1995. Missense mutations in the catalase-peroxidase gene, katG, are associated with isoniazid resistance in Mycobacterium tuberculosis. Mol. Microbiol 15:235-245.
    • (1995) Mol. Microbiol. , vol.15 , pp. 235-245
    • Heym, B.1    Alzari, P.M.2    Honore, N.3    Cole, S.T.4
  • 10
    • 0027248433 scopus 로고
    • Characterization of the katG gene encoding a catalase-peroxidase required for the isoniazid susceptibility of Mycobacterium tuberculosis
    • Heym, B., Y. Zhang, S. Poulet, D. Young, and S. T. Cole. 1993. Characterization of the katG gene encoding a catalase-peroxidase required for the isoniazid susceptibility of Mycobacterium tuberculosis. J. Bacteriol. 175:4255-4259.
    • (1993) J. Bacteriol. , vol.175 , pp. 4255-4259
    • Heym, B.1    Zhang, Y.2    Poulet, S.3    Young, D.4    Cole, S.T.5
  • 11
    • 0029042636 scopus 로고
    • Studies on the mechanism of action of isoniazid and ethionamide in the chemotherapy of tuberculosis
    • Johnsson, K., D. S. King, and P. Schultz. 1995. Studies on the mechanism of action of isoniazid and ethionamide in the chemotherapy of tuberculosis. J. Am. Chem. Soc. 117:5009-5010.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 5009-5010
    • Johnsson, K.1    King, D.S.2    Schultz, P.3
  • 12
    • 0027993499 scopus 로고
    • Mechanistic studies of the oxidation of isoniazid by the catase-peroxidase from Mycobacterium tuberculosis
    • Johnsson, K., and P. Schultz. 1994. Mechanistic studies of the oxidation of isoniazid by the catase-peroxidase from Mycobacterium tuberculosis. J. Am. Chem. Soc. 116:7225-7226.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 7225-7226
    • Johnsson, K.1    Schultz, P.2
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 0031957229 scopus 로고    scopus 로고
    • Expression of katG in Mycobacterium tuberculosis is associated with its growth and persistence in mice and guinea pigs
    • Li, Z., C. Kelley, F. Collins, D. Rouse, and S. Morris. 1998. Expression of katG in Mycobacterium tuberculosis is associated with its growth and persistence in mice and guinea pigs. J. Infect. Dis. 177:1030-1035.
    • (1998) J. Infect. Dis. , vol.177 , pp. 1030-1035
    • Li, Z.1    Kelley, C.2    Collins, F.3    Rouse, D.4    Morris, S.5
  • 15
    • 0035127031 scopus 로고    scopus 로고
    • A domain-swapped RNase A dimer with implications for amyloid formation
    • Liu, Y., G. Gotte, M. Libonati, and D. Eisenberg. 2001. A domain-swapped RNase A dimer with implications for amyloid formation. Nat. Struct. Biol. 8:211-214.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 211-214
    • Liu, Y.1    Gotte, G.2    Libonati, M.3    Eisenberg, D.4
  • 16
    • 0024338720 scopus 로고
    • Cloning, nucleotide sequence, and expression in Escherichia coli of the Bacillus stearothermophilus peroxidase gene (perA)
    • Loprasert, S., S. Negoro, and H. Okada. 1989. Cloning, nucleotide sequence, and expression in Escherichia coli of the Bacillus stearothermophilus peroxidase gene (perA). J. Bacteriol. 171:4871-4875.
    • (1989) J. Bacteriol. , vol.171 , pp. 4871-4875
    • Loprasert, S.1    Negoro, S.2    Okada, H.3
  • 17
    • 0030900246 scopus 로고    scopus 로고
    • The role of Mn(II)peroxidase activity of mycobacterial catalase-peroxidase in activation of the antibiotic isoniazid
    • Magliozzo, R. S., and J. A. Marcinkeviciene. 1997. The role of Mn(II)peroxidase activity of mycobacterial catalase-peroxidase in activation of the antibiotic isoniazid. J. Biol. Chem. 272:8867-8870.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8867-8870
    • Magliozzo, R.S.1    Marcinkeviciene, J.A.2
  • 18
    • 0032944213 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis catalase and peroxidase activities and resistance to oxidative killing in human monocytes in vitro
    • Manca, C., S. Paul, C. E. Barry III, V. H. Freedman, and G. Kaplan. 1999. Mycobacterium tuberculosis catalase and peroxidase activities and resistance to oxidative killing in human monocytes in vitro. Infect. Immun. 67:74-79.
    • (1999) Infect. Immun. , vol.67 , pp. 74-79
    • Manca, C.1    Paul, S.2    Barry C.E. III3    Freedman, V.H.4    Kaplan, G.5
  • 20
    • 0026465558 scopus 로고
    • The catalase-peroxidase of Mycobacterium intracellulare: Nucleotide sequence analysis and expression in Escherichia coli
    • 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. Microbiol. 138:2363-2370.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 2363-2370
    • Morris, S.L.1    Nair, J.2    Rouse, D.A.3
  • 21
    • 0032821142 scopus 로고    scopus 로고
    • Involvement of the N- and C-terminal domains of Mycobacterium tuberculosis KatG in the protection of mutant Escherichia coli against DNA-damaging agents
    • Mulder, M. A., S. Nair, V. R. Abratt, H. Zappe, and L. M. Steyn. 1999. Involvement of the N- and C-terminal domains of Mycobacterium tuberculosis KatG in the protection of mutant Escherichia coli against DNA-damaging agents. Microbiology 145:2011-2021.
    • (1999) Microbiology , vol.145 , pp. 2011-2021
    • Mulder, M.A.1    Nair, S.2    Abratt, V.R.3    Zappe, H.4    Steyn, L.M.5
  • 22
    • 0030996001 scopus 로고    scopus 로고
    • Global mortality, disability, and the contribution of risk factors: Global burden of disease study
    • Murray, C. J., and A. D. Lopez. 1997. Global mortality, disability, and the contribution of risk factors: global burden of disease study. Lancet 349:1436-1442.
    • (1997) Lancet , vol.349 , pp. 1436-1442
    • Murray, C.J.1    Lopez, A.D.2
  • 23
    • 0031467299 scopus 로고    scopus 로고
    • Purification and characterization of recombinant catalase-peroxidase, which confers isoniazid sensitivity in Mycobacterium tuberculosis
    • Nagy, J. M., A. E. Cass, and K. A. Brown. 1997. Purification and characterization of recombinant catalase-peroxidase, which confers isoniazid sensitivity in Mycobacterium tuberculosis. J. Biol. Chem. 272:31265-31271.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31265-31271
    • Nagy, J.M.1    Cass, A.E.2    Brown, K.A.3
  • 24
    • 0033770720 scopus 로고    scopus 로고
    • Evolution of protein function by domain swapping
    • Ostermeier, M., and S. J. Benkovic. 2000. Evolution of protein function by domain swapping. Adv. Protein Chem. 55:29-77.
    • (2000) Adv. Protein Chem. , vol.55 , pp. 29-77
    • Ostermeier, M.1    Benkovic, S.J.2
  • 25
    • 0029907148 scopus 로고    scopus 로고
    • Apramycin resistance as a selective marker for gene transfer in mycobacteria
    • Paget, E., and J. Davies. 1996. Apramycin resistance as a selective marker for gene transfer in mycobacteria. J. Bacteriol. 178:6357-6360.
    • (1996) J. Bacteriol. , vol.178 , pp. 6357-6360
    • Paget, E.1    Davies, J.2
  • 26
    • 0032466234 scopus 로고    scopus 로고
    • Molecular genetic basis of antimicrobial agent resistance in Mycobacterium tuberculosis: 1998 Update
    • Ramaswamy, S., and J. M. Musser. 1998. Molecular genetic basis of antimicrobial agent resistance in Mycobacterium tuberculosis: 1998 update. Tuber. Lung Dis. 79:3-29.
    • (1998) Tuber. Lung Dis. , vol.79 , pp. 3-29
    • Ramaswamy, S.1    Musser, J.M.2
  • 27
    • 0029836553 scopus 로고    scopus 로고
    • Sitedirected mutagenesis of the katG gene of Mycobacterium tuberculosis: Effects on catalase-peroxidase activities and isoniazid resistance
    • Rouse, D. A., J. A. DeVito, Z. Li, H. Byer, and S. L. Morris. 1996. Sitedirected mutagenesis of the katG gene of Mycobacterium tuberculosis: effects on catalase-peroxidase activities and isoniazid resistance. Mol. Microbiol. 22:583-592.
    • (1996) Mol. Microbiol. , vol.22 , pp. 583-592
    • Rouse, D.A.1    DeVito, J.A.2    Li, Z.3    Byer, H.4    Morris, S.L.5
  • 28
    • 0028886398 scopus 로고
    • Characterization of the katG and inhA genes of isoniazid-resistant clinical isolates of Mycobacterium tuberculosis
    • Rouse, D. A., Z. Li, G. H. Bai, and S. L. Morris. 1995. Characterization of the katG and inhA genes of isoniazid-resistant clinical isolates of Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 39:2472-2477.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 2472-2477
    • Rouse, D.A.1    Li, Z.2    Bai, G.H.3    Morris, S.L.4
  • 29
    • 0028930320 scopus 로고
    • Molecular mechanisms of isoniazid resistance in Mycobacterium tuberculosis and Mycobacterium bovis
    • Rouse, D. A., and S. L. Morris. 1995. Molecular mechanisms of isoniazid resistance in Mycobacterium tuberculosis and Mycobacterium bovis. Infect. Immun. 63:1427-1433.
    • (1995) Infect. Immun. , vol.63 , pp. 1427-1433
    • Rouse, D.A.1    Morris, S.L.2
  • 30
    • 0033559410 scopus 로고    scopus 로고
    • Use of site-directed mutagenesis to probe the structure, function and isoniazid activation of the catalase/peroxidase, KatG, from Mycobacterium tuberculosis
    • Saint-Joanis, B., H. Souchon, M. Wilming, K. Johnsson, P. M. Alzari, and S. T. Cole. 1999. Use of site-directed mutagenesis to probe the structure, function and isoniazid activation of the catalase/peroxidase, KatG, from Mycobacterium tuberculosis. Biochem. J. 338:753-760.
    • (1999) Biochem. J. , vol.338 , pp. 753-760
    • Saint-Joanis, B.1    Souchon, H.2    Wilming, M.3    Johnsson, K.4    Alzari, P.M.5    Cole, S.T.6
  • 31
    • 0034719151 scopus 로고    scopus 로고
    • Characterization of high-order diphtheria toxin oligomers
    • Steere, B., and D. Eisenberg. 2000. Characterization of high-order diphtheria toxin oligomers. Biochemistry 39:15901-15909.
    • (2000) Biochemistry , vol.39 , pp. 15901-15909
    • Steere, B.1    Eisenberg, D.2
  • 33
    • 0023050076 scopus 로고
    • A double staining method for differentiating between two classes of mycobacterial catalase in polyacrylamide electrophoresis gels
    • Wayne, L. G., and G. A. Diaz. 1986. A double staining method for differentiating between two classes of mycobacterial catalase in polyacrylamide electrophoresis gels. Anal. Biochem. 157:89-92.
    • (1986) Anal. Biochem. , vol.157 , pp. 89-92
    • Wayne, L.G.1    Diaz, G.A.2
  • 34
    • 0025995263 scopus 로고
    • Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamily
    • Welinder, K. G. 1991. Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamily. Biochim. Biophys. Acta 1080: 215-220.
    • (1991) Biochim. Biophys. Acta , vol.1080 , pp. 215-220
    • Welinder, K.G.1
  • 36
    • 0032506053 scopus 로고    scopus 로고
    • Evidence for differential binding of isoniazid by Mycobacterium tuberculosis KatG and the isoniazid-resistant mutant KatG(S315T)
    • Wengenack, N. L., S. Todorovic, L. Yu, and F. Rusnak. 1998. Evidence for differential binding of isoniazid by Mycobacterium tuberculosis KatG and the isoniazid-resistant mutant KatG(S315T). Biochemistry 37:15825-15834.
    • (1998) Biochemistry , vol.37 , pp. 15825-15834
    • Wengenack, N.L.1    Todorovic, S.2    Yu, L.3    Rusnak, F.4
  • 38
    • 0035824845 scopus 로고    scopus 로고
    • Inter- and intramolecular domain interactions of the catalase-peroxidase KatG from M. tuberculosis
    • Wilming, M., and K. Johnsson. 2001. Inter- and intramolecular domain interactions of the catalase-peroxidase KatG from M. tuberculosis. FEBS Lett. 509:272-276.
    • (2001) FEBS Lett. , vol.509 , pp. 272-276
    • Wilming, M.1    Johnsson, K.2
  • 39
    • 0026705772 scopus 로고
    • The catalase-peroxidase gene and isoniazid resistance of Mycobacterium tuberculosis
    • Zhang, Y., B. Heym, B. Allen, D. Young, and S. Cole. 1992. The catalase-peroxidase gene and isoniazid resistance of Mycobacterium tuberculosis. Nature 358:591-593.
    • (1992) Nature , vol.358 , pp. 591-593
    • Zhang, Y.1    Heym, B.2    Allen, B.3    Young, D.4    Cole, S.5


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