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Volumn 40, Issue 5, 2006, Pages 211-220

Truncated hemoglobin GlbO from Mycobacterium leprae alleviates nitric oxide toxicity

Author keywords

GlbO; Mycobacterium leprae; Nitric oxide; Nitrosative stress; Truncated hemoglobin

Indexed keywords

BETA GALACTOSIDASE; HEMOPROTEIN; NITRATE; NITRIC OXIDE; NITRIC OXIDE DONOR; OXIDOREDUCTASE; RECOMBINANT HEMOGLOBIN;

EID: 33646240586     PISSN: 08824010     EISSN: 10961208     Source Type: Journal    
DOI: 10.1016/j.micpath.2006.01.004     Document Type: Article
Times cited : (26)

References (61)
  • 4
    • 0035058493 scopus 로고    scopus 로고
    • Immunohistochemical analysis of cellular infiltrate and gamma interferon, interleukin-12, and inducible nitric oxide synthase expression in leprosy type 1 (reversal) reactions before and during prednisolone treatment
    • Little D., Khanolkar-Young S., Coulthart A., Suneetha S., and Lockwood D.N. Immunohistochemical analysis of cellular infiltrate and gamma interferon, interleukin-12, and inducible nitric oxide synthase expression in leprosy type 1 (reversal) reactions before and during prednisolone treatment. Infect Immun 69 (2001) 3413-3417
    • (2001) Infect Immun , vol.69 , pp. 3413-3417
    • Little, D.1    Khanolkar-Young, S.2    Coulthart, A.3    Suneetha, S.4    Lockwood, D.N.5
  • 7
    • 0032899502 scopus 로고    scopus 로고
    • Increased levels of nitric oxide metabolites in urine from leprosy patients in reversal reaction
    • Schön T., Gebre N., Sundqvist T., Habetmariam H.S., Engeda T., and Britton S. Increased levels of nitric oxide metabolites in urine from leprosy patients in reversal reaction. Lepr Rev 70 (1999) 52-55
    • (1999) Lepr Rev , vol.70 , pp. 52-55
    • Schön, T.1    Gebre, N.2    Sundqvist, T.3    Habetmariam, H.S.4    Engeda, T.5    Britton, S.6
  • 8
    • 0033850077 scopus 로고    scopus 로고
    • Role of inducible nitric oxide synthase in resistance to Mycobacterium leprae in mice
    • Adams L.B., Job C.K., and Krahenbuhl J.L. Role of inducible nitric oxide synthase in resistance to Mycobacterium leprae in mice. Infect Immun 68 (2000) 5462-5546
    • (2000) Infect Immun , vol.68 , pp. 5462-5546
    • Adams, L.B.1    Job, C.K.2    Krahenbuhl, J.L.3
  • 9
    • 0035448545 scopus 로고    scopus 로고
    • The evolution of mycobacterial pathogenicity: clues from comparative genomics
    • Brosch R., Pym A.S., Gordon S.V., and Cole S.T. The evolution of mycobacterial pathogenicity: clues from comparative genomics. Trends Microbiol 9 (2001) 452-458
    • (2001) Trends Microbiol , vol.9 , pp. 452-458
    • Brosch, R.1    Pym, A.S.2    Gordon, S.V.3    Cole, S.T.4
  • 10
    • 0036200214 scopus 로고    scopus 로고
    • Reactive nitrogen and oxygen intermediates and bacterial defenses: unusual adaptation in Mycobacterium tuberculosis
    • Zahrt T.C., and Deretic V. Reactive nitrogen and oxygen intermediates and bacterial defenses: unusual adaptation in Mycobacterium tuberculosis. Antioxid Redox Signal 4 (2002) 141-149
    • (2002) Antioxid Redox Signal , vol.4 , pp. 141-149
    • Zahrt, T.C.1    Deretic, V.2
  • 13
    • 0037059826 scopus 로고    scopus 로고
    • Truncated hemoglobins: a new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants
    • Wittenberg J.B., Bolognesi M., Wittenberg B.A., and Guertin M. Truncated hemoglobins: a new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants. J Biol Chem 277 (2002) 871-874
    • (2002) J Biol Chem , vol.277 , pp. 871-874
    • Wittenberg, J.B.1    Bolognesi, M.2    Wittenberg, B.A.3    Guertin, M.4
  • 14
    • 0141783647 scopus 로고    scopus 로고
    • Bacterial hemoglobins and flavohemoglobins: versatile proteins and their impact on microbiology and biotechnology
    • Frey A.D., and Kallio P.T. Bacterial hemoglobins and flavohemoglobins: versatile proteins and their impact on microbiology and biotechnology. FEMS Microbiol Rev 27 (2003) 525-545
    • (2003) FEMS Microbiol Rev , vol.27 , pp. 525-545
    • Frey, A.D.1    Kallio, P.T.2
  • 17
    • 0036049852 scopus 로고    scopus 로고
    • Nitric oxide scavenging and detoxification by the Mycobacterium tuberculosis haemoglobin, HbN in Escherichia coli
    • Pathania R., Navani N.K., Gardner A.M., Gardner P.R., and Dikshit K.L. Nitric oxide scavenging and detoxification by the Mycobacterium tuberculosis haemoglobin, HbN in Escherichia coli. Mol Microbiol 45 (2002) 1303-1314
    • (2002) Mol Microbiol , vol.45 , pp. 1303-1314
    • Pathania, R.1    Navani, N.K.2    Gardner, A.M.3    Gardner, P.R.4    Dikshit, K.L.5
  • 19
    • 0041827138 scopus 로고    scopus 로고
    • The effects of reactive nitrogen intermediates on gene expression in Mycobacterium tuberculosis
    • Ohno H., Zhu G., Mohan V.P., Chu D., Kohno S., Jacobs Jr. W.R., et al. The effects of reactive nitrogen intermediates on gene expression in Mycobacterium tuberculosis. Cell Microbiol 5 (2003) 637-648
    • (2003) Cell Microbiol , vol.5 , pp. 637-648
    • Ohno, H.1    Zhu, G.2    Mohan, V.P.3    Chu, D.4    Kohno, S.5    Jacobs Jr., W.R.6
  • 20
    • 0043142536 scopus 로고    scopus 로고
    • Transcriptional adaptation of Mycobacterium tuberculosis within macrophages: insights into the phagosomal environment
    • Schnappinger D., Ehrt S., Voskuil M.I., Liu Y., Mangan J.A., Monahan I.M., et al. Transcriptional adaptation of Mycobacterium tuberculosis within macrophages: insights into the phagosomal environment. J Exp Med 198 (2003) 693-704
    • (2003) J Exp Med , vol.198 , pp. 693-704
    • Schnappinger, D.1    Ehrt, S.2    Voskuil, M.I.3    Liu, Y.4    Mangan, J.A.5    Monahan, I.M.6
  • 21
    • 1642327485 scopus 로고    scopus 로고
    • Truncated hemoglobin O of Mycobacteium tuberculosis: the oligomeric state change and the interaction with membrane components
    • Liu C., He Y., and Chang Z. Truncated hemoglobin O of Mycobacteium tuberculosis: the oligomeric state change and the interaction with membrane components. Biochem Biophys Res Commun 316 (2004) 1163-1172
    • (2004) Biochem Biophys Res Commun , vol.316 , pp. 1163-1172
    • Liu, C.1    He, Y.2    Chang, Z.3
  • 22
    • 0037013274 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis haemoglobin HbO associates with membranes and stimulates cellular respiration of recombinant Escherichia coli
    • Pathania R., Navani N.K., Rajamohan G., and Dikshit K.L. Mycobacterium tuberculosis haemoglobin HbO associates with membranes and stimulates cellular respiration of recombinant Escherichia coli. J Biol Chem 277 (2002) 15293-15302
    • (2002) J Biol Chem , vol.277 , pp. 15293-15302
    • Pathania, R.1    Navani, N.K.2    Rajamohan, G.3    Dikshit, K.L.4
  • 23
    • 0038629128 scopus 로고    scopus 로고
    • Reactions of Mycobacterium tuberculosis truncated hemoglobin O with ligands reveal a novel ligand-inclusive hydrogen bond network
    • Ouellet H., Juszczak L., Dantsker D., Samuni U., Ouellet Y.H., Savard P.Y., et al. Reactions of Mycobacterium tuberculosis truncated hemoglobin O with ligands reveal a novel ligand-inclusive hydrogen bond network. Biochemistry 42 (2003) 5764-5774
    • (2003) Biochemistry , vol.42 , pp. 5764-5774
    • Ouellet, H.1    Juszczak, L.2    Dantsker, D.3    Samuni, U.4    Ouellet, Y.H.5    Savard, P.Y.6
  • 24
    • 0037177162 scopus 로고    scopus 로고
    • Unique ligand-protein interactions in a new truncated hemoglobin from Mycobacterium tuberculosis
    • Mukai M., Savard P.Y., Ouellet H., Guertin M., and Yeh S.R. Unique ligand-protein interactions in a new truncated hemoglobin from Mycobacterium tuberculosis. Biochemistry 41 (2002) 3897-3905
    • (2002) Biochemistry , vol.41 , pp. 3897-3905
    • Mukai, M.1    Savard, P.Y.2    Ouellet, H.3    Guertin, M.4    Yeh, S.R.5
  • 25
    • 0038624089 scopus 로고    scopus 로고
    • A TyrCD1/TrpG8 hydrogen bond network and a TyrB10TyrCD1 covalent link shape the heme distal site of Mycobacterium tuberculosis hemoglobin O
    • Milani M., Savard P.Y., Ouellet H., Ascenzi P., Guertin M., and Bolognesi M. A TyrCD1/TrpG8 hydrogen bond network and a TyrB10TyrCD1 covalent link shape the heme distal site of Mycobacterium tuberculosis hemoglobin O. Proc Natl Acad Sci USA 10 (2003) 5766-5771
    • (2003) Proc Natl Acad Sci USA , vol.10 , pp. 5766-5771
    • Milani, M.1    Savard, P.Y.2    Ouellet, H.3    Ascenzi, P.4    Guertin, M.5    Bolognesi, M.6
  • 27
    • 0037040980 scopus 로고    scopus 로고
    • Flavohemoglobin detoxifies nitric oxide in aerobic, but not anaerobic, Escherichia coli. Evidence for a novel inducible anaerobic nitric oxide-scavenging activity
    • Gardner A.M., and Gardner P.R. Flavohemoglobin detoxifies nitric oxide in aerobic, but not anaerobic, Escherichia coli. Evidence for a novel inducible anaerobic nitric oxide-scavenging activity. J Biol Chem 277 (2002) 8166-8171
    • (2002) J Biol Chem , vol.277 , pp. 8166-8171
    • Gardner, A.M.1    Gardner, P.R.2
  • 30
    • 0032564409 scopus 로고    scopus 로고
    • Nitrosative stress: metabolic pathway involving the flavohemoglobin
    • Hausladen A., Gow A.J., and Stamler J.S. Nitrosative stress: metabolic pathway involving the flavohemoglobin. Proc Natl Acad Sci USA 95 (1998) 14100-14105
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 14100-14105
    • Hausladen, A.1    Gow, A.J.2    Stamler, J.S.3
  • 31
    • 0039626289 scopus 로고    scopus 로고
    • The flavohemoglobin of Escherichia coli confers resistance to a nitrosating agent, a 'Nitric Oxide releaser', and paraquat and is essential for transcriptional response to oxidative stress
    • Membrillo-Hernadez J., Coopamah M.D., Anjum M.F., Stevanin T.M., Kelly A., Hughes M.N., et al. The flavohemoglobin of Escherichia coli confers resistance to a nitrosating agent, a 'Nitric Oxide releaser', and paraquat and is essential for transcriptional response to oxidative stress. J Biol Chem 274 (1999) 748-754
    • (1999) J Biol Chem , vol.274 , pp. 748-754
    • Membrillo-Hernadez, J.1    Coopamah, M.D.2    Anjum, M.F.3    Stevanin, T.M.4    Kelly, A.5    Hughes, M.N.6
  • 32
    • 0022402203 scopus 로고
    • Role of glnB and glnD gene products in regulation of the glnALG operon of Escherichia coli
    • Bueno R., Pahel G., and Magasanik B. Role of glnB and glnD gene products in regulation of the glnALG operon of Escherichia coli. J Bacteriol 164 (1985) 816-822
    • (1985) J Bacteriol , vol.164 , pp. 816-822
    • Bueno, R.1    Pahel, G.2    Magasanik, B.3
  • 33
    • 0020070412 scopus 로고
    • Characterization of a gene, glnL, the product of which is involved in the regulation of nitrogen utilization in Escherichia coli chromosome
    • Chen Y.M., Backman K., and Magasanik B. Characterization of a gene, glnL, the product of which is involved in the regulation of nitrogen utilization in Escherichia coli chromosome. J Bacteriol 150 (1982) 214-220
    • (1982) J Bacteriol , vol.150 , pp. 214-220
    • Chen, Y.M.1    Backman, K.2    Magasanik, B.3
  • 34
    • 0025295438 scopus 로고
    • Decay of nitroprusside. I. In vitro
    • Vesey C.J., Stringer M., and Cole P.V. Decay of nitroprusside. I. In vitro. Br J Anaesth 64 (1990) 696-703
    • (1990) Br J Anaesth , vol.64 , pp. 696-703
    • Vesey, C.J.1    Stringer, M.2    Cole, P.V.3
  • 35
    • 0030910666 scopus 로고    scopus 로고
    • Interactions of OxyR with the promoter region of the oxyR and ahpC genes from Mycobacterium leprae and Mycobacterium tuberculosis
    • Dhandayuthapani S., Mudd M., and Deretic V. Interactions of OxyR with the promoter region of the oxyR and ahpC genes from Mycobacterium leprae and Mycobacterium tuberculosis. J Bacteriol 179 (1997) 2401-2409
    • (1997) J Bacteriol , vol.179 , pp. 2401-2409
    • Dhandayuthapani, S.1    Mudd, M.2    Deretic, V.3
  • 36
    • 0029098674 scopus 로고
    • Characterization of the gene encoding the immunodominant 35 kDa protein of Mycobacterium leprae
    • Winter N., Triccas J.A., Rivoire B., Pessolani M.C., Eiglmeier K., Lim E.M., et al. Characterization of the gene encoding the immunodominant 35 kDa protein of Mycobacterium leprae. Mol Microbiol 16 (1995) 865-876
    • (1995) Mol Microbiol , vol.16 , pp. 865-876
    • Winter, N.1    Triccas, J.A.2    Rivoire, B.3    Pessolani, M.C.4    Eiglmeier, K.5    Lim, E.M.6
  • 37
    • 0028079877 scopus 로고
    • Escherichia coli-mycobacteria shuttle vectors for operon and gene fusions to lacZ: the pJEM series
    • Timm J., Limr E.M., and Gicquel B. Escherichia coli-mycobacteria shuttle vectors for operon and gene fusions to lacZ: the pJEM series. J Bacteriol 176 (1994) 6749-6753
    • (1994) J Bacteriol , vol.176 , pp. 6749-6753
    • Timm, J.1    Limr, E.M.2    Gicquel, B.3
  • 38
    • 0017129243 scopus 로고
    • Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu
    • Casadaban M.J. Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu. J Mol Biol 104 (1976) 541-555
    • (1976) J Mol Biol , vol.104 , pp. 541-555
    • Casadaban, M.J.1
  • 40
    • 0035699030 scopus 로고    scopus 로고
    • The microbial physiologist's guide to the leprosy genome
    • Wheeler P.R. The microbial physiologist's guide to the leprosy genome. Lepr Rev 72 (2001) 399-407
    • (2001) Lepr Rev , vol.72 , pp. 399-407
    • Wheeler, P.R.1
  • 41
    • 0034724887 scopus 로고    scopus 로고
    • Steady-state and transient kinetics of Escherichia coli nitric-oxide dioxygenase (flavohemoglobin). The B10 tyrosine hydroxyl is essential for dioxygen binding and catalysis
    • Gardner A.M., Martin L.A., Gardner P.R., Dou Y., and Olson J.S. Steady-state and transient kinetics of Escherichia coli nitric-oxide dioxygenase (flavohemoglobin). The B10 tyrosine hydroxyl is essential for dioxygen binding and catalysis. J Biol Chem 275 (2000) 12581-12589
    • (2000) J Biol Chem , vol.275 , pp. 12581-12589
    • Gardner, A.M.1    Martin, L.A.2    Gardner, P.R.3    Dou, Y.4    Olson, J.S.5
  • 42
    • 0344417899 scopus 로고    scopus 로고
    • Regulation of hmp gene transcription in Mycobacterium tuberculosis: effects of oxygen limitation and nitrosative and oxidative stress
    • Hu Y., Butcher P.D., Mangan J.A., Rajandream M.A., and Coates A.R.M. Regulation of hmp gene transcription in Mycobacterium tuberculosis: effects of oxygen limitation and nitrosative and oxidative stress. J Bacteriol 181 (1999) 3486-3493
    • (1999) J Bacteriol , vol.181 , pp. 3486-3493
    • Hu, Y.1    Butcher, P.D.2    Mangan, J.A.3    Rajandream, M.A.4    Coates, A.R.M.5
  • 43
    • 0036794855 scopus 로고    scopus 로고
    • Bacterial hemoglobins and flavohemoglobins for alleviation of nitrosative stress in Escherichia coli
    • Frey A.D., Farres J., Bollinger C.J., and Kallio P.T. Bacterial hemoglobins and flavohemoglobins for alleviation of nitrosative stress in Escherichia coli. Appl Environ Microbiol 68 (2002) 4835-4840
    • (2002) Appl Environ Microbiol , vol.68 , pp. 4835-4840
    • Frey, A.D.1    Farres, J.2    Bollinger, C.J.3    Kallio, P.T.4
  • 44
    • 10644291828 scopus 로고    scopus 로고
    • Nitric oxide dioxygenase function and mechanism of flavohemoglobin, hemoglobin, myoglobin and their associated reductases
    • Gardner P.R. Nitric oxide dioxygenase function and mechanism of flavohemoglobin, hemoglobin, myoglobin and their associated reductases. J Inorg Biochem 99 (2005) 247-266
    • (2005) J Inorg Biochem , vol.99 , pp. 247-266
    • Gardner, P.R.1
  • 46
    • 0029159816 scopus 로고
    • Activity of mycobacterial promoters during intracellular and extracellular growth
    • Dellagostin O.A., Esposito G., Eales L.J., Dale J.W., and McFadden J. Activity of mycobacterial promoters during intracellular and extracellular growth. Microbiology 141 (1995) 1785-1792
    • (1995) Microbiology , vol.141 , pp. 1785-1792
    • Dellagostin, O.A.1    Esposito, G.2    Eales, L.J.3    Dale, J.W.4    McFadden, J.5
  • 47
    • 0029747225 scopus 로고    scopus 로고
    • A study of mycobacterial transcriptional apparatus: identification of novel features in promoter elements
    • Bashyam M.D., Kaushal D., Dasgupta S.K., and Tyagi A.K. A study of mycobacterial transcriptional apparatus: identification of novel features in promoter elements. J Bacteriol 178 (1996) 4847-4853
    • (1996) J Bacteriol , vol.178 , pp. 4847-4853
    • Bashyam, M.D.1    Kaushal, D.2    Dasgupta, S.K.3    Tyagi, A.K.4
  • 48
    • 0036468504 scopus 로고    scopus 로고
    • Mycobacterium smegmatis and tuberculosis
    • Tyagi J.S., and Sharma D. Mycobacterium smegmatis and tuberculosis. Trends Microbiol 10 (2002) 68-69
    • (2002) Trends Microbiol , vol.10 , pp. 68-69
    • Tyagi, J.S.1    Sharma, D.2
  • 50
  • 51
    • 0035146934 scopus 로고    scopus 로고
    • Nitric oxide, cytochrome-c oxidase and myoglobin
    • Brunori M. Nitric oxide, cytochrome-c oxidase and myoglobin. Trends Biochem Sci 26 (2001) 21-23
    • (2001) Trends Biochem Sci , vol.26 , pp. 21-23
    • Brunori, M.1
  • 52
    • 0038629108 scopus 로고    scopus 로고
    • Interaction with membrane lipids and heme ligand binding properties of Escherichia coli flavohemoglobin
    • Bonamore A., Farina A., Gattoni M., Schininà M.E., Bellelli A., and Boffi A. Interaction with membrane lipids and heme ligand binding properties of Escherichia coli flavohemoglobin. Biochemistry 42 (2003) 5792-5801
    • (2003) Biochemistry , vol.42 , pp. 5792-5801
    • Bonamore, A.1    Farina, A.2    Gattoni, M.3    Schininà, M.E.4    Bellelli, A.5    Boffi, A.6
  • 55
    • 0035709008 scopus 로고    scopus 로고
    • A rapid, simple spectrophotometric method for simultaneous detection of nitrate and nitrite
    • Miranda K.M., Espey M.G., and Wink D.A. A rapid, simple spectrophotometric method for simultaneous detection of nitrate and nitrite. Nitric Oxide 5 (2001) 62-71
    • (2001) Nitric Oxide , vol.5 , pp. 62-71
    • Miranda, K.M.1    Espey, M.G.2    Wink, D.A.3
  • 56
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 57
    • 0027434569 scopus 로고
    • Use of an ordered cosmid library to deduce the genomic organization of Mycobacterium leprae
    • Eiglmeier K., Honore N., Woods S.A., Caudron B., and Cole S.T. Use of an ordered cosmid library to deduce the genomic organization of Mycobacterium leprae. Mol Microbiol 7 (1993) 197-206
    • (1993) Mol Microbiol , vol.7 , pp. 197-206
    • Eiglmeier, K.1    Honore, N.2    Woods, S.A.3    Caudron, B.4    Cole, S.T.5
  • 58
    • 0025295967 scopus 로고
    • Differential plasmid rescue from transgenic mouse DNAs into Escherichia coli methylation-restriction mutants
    • Grant S.G., Jessee J., Bloom F.R., and Hanahan D. Differential plasmid rescue from transgenic mouse DNAs into Escherichia coli methylation-restriction mutants. Proc Natl Acad Sci 87 (1990) 4645-4649
    • (1990) Proc Natl Acad Sci , vol.87 , pp. 4645-4649
    • Grant, S.G.1    Jessee, J.2    Bloom, F.R.3    Hanahan, D.4
  • 60
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Miller J.H. Experiments in molecular genetics (1972), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • (1972) Experiments in molecular genetics
    • Miller, J.H.1
  • 61
    • 0025081151 scopus 로고
    • Isolation and characterization of efficient plasmid transformation mutants of Mycobacterium smegmatis
    • Snapper S.B., Melton R.E., Mustafa S., Kieser T., and Jacobs Jr. W.R. Isolation and characterization of efficient plasmid transformation mutants of Mycobacterium smegmatis. Mol Microbiol 11 (1990) 1911-1919
    • (1990) Mol Microbiol , vol.11 , pp. 1911-1919
    • Snapper, S.B.1    Melton, R.E.2    Mustafa, S.3    Kieser, T.4    Jacobs Jr., W.R.5


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