• [1]
    Dye, C., Scheele, S., Dolin, P., Pathania, V., Raviglione, M.C. (1999) Consensus statement. Global burden of tuberculosis estimated incidence, prevalence, and mortality by country. WHO global suveillance and monitoring project. J. Am. Med. Assoc. 282, 677686.
  • [2]
    Laochumroonvorapong, P., Paul, S., Manca, C., Freedman, V.H., Kaplan, C.F. (1997) Mycobacterial growth and sensitivity to H2O2 killing in human monocytes in vitro. Infect. Immun. 65, 48504857.
  • [3]
    Dolphin, D., Poulson, R. and Avramovic, O. (1989) Glutathione: Chemical, Biochemical, and Medical Aspects – Parts A and B. Coenzymes and Cofactors. John Wiley and Sons, New York.
  • [4]
    Newton, G.L., Arnold, K., Price, M.S., Sherill, C., DelCardayré, S.B., Aharonowitz, Y., Cohen, G. (1996) Distribution of thiols in microorganisms: Mycothiol is a major thiol in most actinomycetes. J. Bacteriol. 178, 19901995.
  • [5]
    Newton, G.L., Unson, M., Anderberg, S., Aguilera, J.A., Oh, N.N., DelCardayré, S., Av-Gay, Y., Fahey, R.C. (1999) Characterization of Mycobacterium smegmatis mutants defective in 1-D-myo-inosityl-2-amino-2-deoxy-a-D-glucopyranoside and mycothiol biosynthesis. Biochem. Biophys. Res. Commun. 255, 239244.
  • [6]
    Rawat, M., Newton, G.L., Ko, M., Martinez, J.G., Fahey, R.C., Av-Gay, Y. (2002) Mycothiol deficient mutants in Mycobacterium smegmatis are hypersensitive to alkylating agents, free radicals and antibiotics. Antimicrob. Agents Chemother. 46, 33483355.
  • [7]
    Kosower, N.S., Kosower, E.M. (1995) Diamide: An oxidant probe for thiols. Methods Enzymol. 251, 123133.
  • [8]
    Apontoweil, P., Berends, W. (1975) Isolation and initial characterization of glutathione-deficient mutants of Escerichia coli K 12. Biochim. Biophys. Acta 399, 1012.
  • [9]
    Carmel-Harel, O., Storz, G. (2000) Roles of glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress. Annu. Rev. Microbiol. 54, 439461.
  • [10]
    Paget, M.S.B., Kang, J., Roe, J., Buttner, M.J. (1998) σR and RNA polymerase sigma factor that modulates expression of the thioredoxin system in response to oxidative stress in Streptomyces coelicolor A3. EMBO J. 19 (2), 57765782.
  • [11]
    Wemmie, J.A., Steggerda, S.M., Moye-Rowley, W.S. (1997) The Saccharomyces cerevisiae AP-1 protein discriminates between oxidative stress elicited by the oxidants H2O2 and diamide. J. Biol. Chem. 272, 79087914.
  • [12]
    Raman, S., Song, T., Puyang, X., Bardarov, S., W.R. Jacobs Jr., Husson, R.N. (2001) The alternative sigma factor SigH regulates major components of oxidative and heat stress responses in Mycobacterium tuberculosis. J. Bacteriol. 183, 61196125.
  • [13]
    Larsen, M.H. (2000) Some common methods in mycobacterial genetics. In: Molecular Genetics of Mycobacteria (Hatfull, G.F. and Jacobs, W.R. Jr.), pp. 313–321. ASM Press, Washington, DC.
  • [14]
    Sambrook, J., Fritsch, E.F. and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual, 2nd edn. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
  • [15]
    Snapper, S.B., Lugosi, L., Jekkel, A., Melton, R.E., Kieser, T., Bloom, B.R., Jacobs, W.R.Jr. (1988) Lysogeny and transformation in mycobacteria: stable expression of foreign genes. Proc. Natl. Acad. Sci. USA 85, 69876991.
  • [16]
    Altschul, S.F., Madden, T.L., Schaeffer, A.A., Zhang, J., Zhang, Z., Miller, W., Lipman, D.J. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25, 33893402.
  • [17]
    De Smet, K.A., Kempsell, K.E., Gallagher, A., Duncan, K., Young, D.B. (1999) Alteration of a single amino acid residue reverses fosfomycin resistance of recombinant MurA from Mycobacterium tuberculosis. Microbiology 145, 31773184.
  • [18]
    Gerlt, J.A., Babbitt, P.C. (2001) Divergent evolution of enzymatic function: Mechanistically diverse superfamilies and functionally distinct suprafamilies. Annu. Rev. Biochem. 70, 209246.
  • [19]
    Bernat, B.A., Laughlin, L.T., Armstrong, R.N. (1997) Fosfomycin resistance protein (FosA) is a manganese metalloglutathione transferase related to glyoxalase I and the extradiol dioxygenases. Biochemistry 36, 30503055.
  • [20]
    Bergdoll, M., Eltis, L.D., Cameron, A.D., Dumas, P., Bolin, J.T. (1998) All in the family: Structural and evolutionary relationships among three modular proteins with diverse functions and variable assembly. Protein Sci. 7, 16611670.
  • [21]
    Kosower, N.S., Kosower, E.M. (1987) Formation of disulfides with diamide. Methods Enzymol. 143, 264270.
  • [22]
    Kosower, E.M., Correa, W., Kinon, B.J., Kosower, N.S. (1972) Glutathione. VII. Differentiation among substrates by the thiol-oxidizing agent, glutathione. Biochim. Biophys. Acta 264, 3944.
  • [23]
    Hibberd, K.A., Berget, P.B., Warner, H.R., Fuchs, J.A. (1978) Role of glutathione in reversing the deleterious effects of a thiol-oxidizing agent in Escherichia coli. J. Bacteriol. 133, 11501155.
  • [24]
    Wax, R., Rosenberg, E., Kosower, N.S., Kosower, E.M. (1970) Effect of the thiol-oxidizing agent diamide on the growth of Escherichia coli. J. Bacteriol. 101, 10921093.