[1] | Cannio R, Fiorentino G, Morana A, Rossi M, Bartolucci S (2000) Oxygen: friend or foe? Archaeal superoxide dismutases in the protection of intra- and extracellular oxidative stress. Front Biosci 5: D768–779.
|
[2] | Storz G, Tartaglia LA, Farr SB, Ames BN (1990) Bacterial defenses against oxidative stress. Trends Genet 6: 363–368.
|
[3] | González-Flecha B, Demple B (1997) Homeostatic regulation of intracellular hydrogen peroxide concentration in aerobically growing Escherichia coli. J Bacteriol 179: 382–388.
|
[4] | Schellhorn HE (1995) Regulation of hydroperoxidase (catalase) expression in Escherichia coli. FEMS Microbiol Lett 131: 113–119.
|
[5] | Hidalgo E, Demple B (1994) An iron-sulfur center essential for transcriptional activation by the redox-sensing SoxR protein. EMBO J 13: 138–146.
|
[6] | Hidalgo E, Bollinger JM, Bradley TM, Walsh CT, Demple B (1995) Binuclear [2Fe-2S] clusters in the Escherichia coli SoxR protein and role of the metal centers in transcription. J Biol Chem 270: 20908–20914.
|
[7] | Storz G, Imlay JA (1999) Oxidative stress. Curr Opin Microbiol 2: 188–194.
|
[8] | Greenberg JT, Monach P, Chou JH, Josephy PD, Demple B (1990) Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli. Proc Natl Acad Sci U S A 87: 6181–6185.
|
[9] | Schell MA (1993) Molecular biology of the LysR family of transcriptional regulators. Annu Rev Microbiol 47: 597–626.
|
[10] | Zheng M, Aslund F, Storz G (1998) Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 279: 1718–1721.
|
[11] | Zheng M, Wang X, Templeton LJ, Smulski DR, LaRossa RA, et al. (2001) DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide. J Bacteriol 183: 4562–4570.
|
[12] | Christman MF, Morgan RW, Jacobson FS, Ames BN (1985) Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium. Cell 41: 753–762.
|
[13] | González-Flecha B, Demple B (1999) Role for the oxyS gene in regulation of intracellular hydrogen peroxide in Escherichia coli. J Bacteriol 181: 3833–3836.
|
[14] | Tseng HJ, McEwan AG, Apicella MA, Jennings MP (2003) OxyR acts as a repressor of catalase expression in Neisseria gonorrhoeae. Infect Immun 71: 550–556.
|
[15] | Seib KL, Wu HJ, Srikhanta YN, Edwards JL, Falsetta ML, et al. (2007) Characterization of the OxyR regulon of Neisseria gonorrhoeae. Mol Microbiol 63: 54–68.
|
[16] | Ieva R, Roncarati D, Metruccio MME, Seib KL, Scarlato V, et al. (2008) OxyR tightly regulates catalase expression in Neisseria meningitidis through both repression and activation mechanisms. Mol Microbiol 70: 1152–1165.
|
[17] | Holmes RK (2000) Biology and molecular epidemiology of diphtheria toxin and the tox gene. J Infect Dis 181: Suppl 1S156–167.
|
[18] | Kunkle CA, Schmitt MP (2003) Analysis of the Corynebacterium diphtheriae DtxR regulon: Identification of a putative siderophore synthesis and transport system that is similar to the Yersinia high-pathogenicity island-encoded yersiniabactin synthesis and uptake system. J Bacteriol 185: 6826–6840.
|
[19] | Lee JH, Wang T, Ault K, Liu J, Schmitt MP, et al. (1997) Identification and characterization of three new promoter/operators from Corynebacterium diphtheriae that are regulated by the diphtheria toxin repressor (DtxR) and iron. Infect Immun 65: 4273–4280.
|
[20] | Schmitt MP, Holmes RK (1991) Iron-dependent regulation of diphtheria toxin and siderophore expression by the cloned Corynebacterium diphtheriae repressor gene DtxR in C. diphtheriae C7 Strains. Infect Immun 59: 1899–1904.
|
[21] | Oram DM, Jacobson AD, Holmes RK (2006) Transcription of the contiguous sigB, dtxR, and galE genes in Corynebacterium diphtheriae: Evidence for multiple transcripts and regulation by environmental factors. J Bacteriol 188: 2959–2973.
|
[22] | Merkamm M, Guyonvarch A (2001) Cloning of the sodA gene from Corynebacterium melassecola and role of superoxide dismutase in cellular viability. J Bacteriol 183: 1284–1295.
|
[23] | EI Shafey HM, Ghanem S, Merkamm M, Guyonvarch A (2008) Corynebacterium glutamicum superoxide dismutase is a manganese-strict non-cambialistic enzyme in vitro. Microbiol Res 163: 80–86.
|
[24] | Barksdale WL, Pappenheimer AM (1954) Phage-host relationships in nontoxigenic and toxigenic diphtheria bacilli. J Bacteriol 67: 220–232.
|
[25] | Tai SP, Krafft AE, Nootheti P, Holmes RK (1990) Coordinate regulation of siderophore and diphtheria toxin production by iron in Corynebacterium diphtheriae. Microb Pathog 9: 267–273.
|
[26] | Sambrook J, Russell DW (2001) Molecular Cloning: A Laboratory Manual, 3rd Ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
|
[27] | Schafer A, Kalinowski J, Puhler A (1994) Increased fertility of Corynebacterium glutamicum recipients in intergeneric matings with Escherichia coli after stress exposure. Appl Environ Microbiol 60: 756–759.
|
[28] | Simon R, Priefer U, Puhler A (1983) A broad host mobilization system for in vivo genetic engineering: transposon mutagenesis in gram negative bacteria. Bio/Technology 1: 37–45.
|
[29] | Ton-That H, Schneewind O (2003) Assembly of pili on the surface of Corynebacterium diphtheriae. Mol Microbiol 50: 1429–1438.
|
[30] | Oram DM, Oram M, Woolston JE, Jacobson AD, Holmes RK (2007) Bacteriophage-based vectors for site-specific insertion of DNA in the chromosome of Corynebacteria. Gene 391: 53–62.
|
[31] | Oram DM, Avdalovic A, Holmes RK (2002) Construction and characterization of transposon insertion mutations in Corynebactetium diphtheriae that affect expression of the diphtheria toxin repressor (DtxR). J Bacteriol 184: 5723–5732.
|
[32] | Prentki P, Krisch HM (1984) In vitro insertional mutagenesis with a selectable DNA fragment. Gene 29: 303–313.
|
[33] | Tai TN, Havelka WA, Kaplan S (1988) A broad-host-range vector system for cloning and translational lacZ fusion analysis. Plasmid 19: 175–188.
|
[34] | Nelson DP, Kiesow LA (1972) Enthalpy of decomposition of hydrogen-peroxide by catalase at 25 degrees C (with molar extinction coefficients of H2O2 solutions in UV). Anal Biochem 49: 474–478.
|
[35] | Wayne LG, Diaz GA (1986) A double staining method for differentiating between two classes of mycobacterial catalase in polyacrylamide electrophoresis gels. Anal Biochem 157: 89–92.
|
[36] | Kim JS, Jang JH, Lee JW, Kang SO, Kim KS, et al. (2000) Identification of cis site involved in nickel-responsive transcriptional repression of sodF gene coding for Fe- and Zn-containing superoxide dismutase of Streptomyces griseus. Biochim Biophys Acta 1493: 200–207.
|
[37] | Zeller T, Mraheil MA, Moskvin OV, Li KY, Gomelsky M, et al. (2007) Regulation of hydrogen peroxide-dependent gene expression in Rhodobacter sphaeroides: regulatory functions of OxyR. J Bacteriol 189: 3784–3792.
|
[38] | Pomposiello PJ, Demple B (2001) Redox-operated genetic switches: the SoxR and OxyR transcription factors. Trends Biotechnol 19: 109–114.
|
[39] | Cerdeňo-Tarraga AM, Efstratiou A, Dover LG, Holden MT, Pallen M, et al. (2003) The complete genome sequence and analysis of Corynebacterium diphtheriae NCTC13129. Nucleic Acids Res 31: 6516–6523.
|
[40] | Tartaglia LA, Storz G, Ames BN (1989) Identification and molecular analysis of oxyR regulated promoters important for the bacterial adaptation to oxidative stress. J Mol Biol 210: 709–719.
|
[41] | Lee JH, Yeo WS, Roe JH (2004) Induction of the sufA operon encoding Fe-S assembly proteins by superoxide generators and hydrogen peroxide: involvement of OxyR, IHF and an unidentified oxidant-responsive factor. Mol Microbiol 51: 1745–1755.
|
[42] | Keen NT, Tamaki S, Kobayashi D, Trollinger D (1988) Improved broad-host-range plasmids for DNA cloning in gram-negative bacteria. Gene 70: 191–197.
|
[43] | Kalinowski J, Bathe B, Bartels D, Bischoff N, Bott M, et al. (2007) The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins. J Biotechnol 104: 5–25.
|
[44] | Sak BD, Eisenstark A, Touati D (1989) Exonuclease III and the catalase hydroperoxidase II in Escherichia coli are both regulated by the katF gene product. Proc Natl Acad Sci U S A 86: 3271–3275.
|
[45] | Pátek M, Ne?vera J (2011) Sigma factors and promoters in Corynebacterium glutamicum. J Biotechnol 154: 101–113.
|
[46] | Parsek MR, Ye RW, Pun P, Chakrabarty AM (1994) Critical nucleotides in the interaction of a LysR-type regulator with its target promoter region. J Biol Chem 269: 11279–11284.
|
[47] | Goethals K, Van Montagu M, Holsters M (1992) Conserved motifs in a divergent nod box of Azorhizobium caulinodans ORS571 reveal a common structure in promoters regulated by LysR-type proteins. Proc Natl Acad Sci U S A 89: 1646–1650.
|
[48] | Zaim J, Kierzek AM (2003) The structure of full-length LysR-type transcriptional regulators. Modeling of the full-length OxyR transcription factor dimer. Nucleic Acids Res 31: 1444–1454.
|
[49] | Sainsbury S, Lane LA, Ren J, Gilbert RJ, Saunders NJ, et al. (2009) The structure of CrgA from Neisseria meningitidis reveals a new octameric assembly state for LysR transcriptional regulators. Nucleic Acids Res 37: 4545–4558.
|
[50] | Hanahan D (1983) Studies on tansformation of Escherichia coli with plasmids. J Mol Biol 166: 557–580.
|