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Volumn 78, Issue 18, 2012, Pages 6499-6506

Comparative analysis of mycobacterial truncated hemoglobin promoters and the groel2 promoter in free-living and intracellular mycobacteria

Author keywords

[No Author keywords available]

Indexed keywords

COMPARATIVE ANALYSIS; EXPRESSION PROFILE; GREEN FLUORESCENT PROTEIN; HAZARDOUS ENVIRONMENT; HEAT SHOCK PROTEIN; HEMOPROTEINS; HOSTILE ENVIRONMENTS; IN-VIVO; M. TUBERCULOSIS; MYCOBACTERIAL; MYCOBACTERIUM TUBERCULOSIS; NITROSATIVE STRESS; PROMOTER ACTIVITIES; REACTIVE NITROGEN INTERMEDIATES; REACTIVE OXYGEN INTERMEDIATES; REAL-TIME PCR; SEVERE HYPOXIAS; STRESS CONDITION; TIME POINTS; TRANSCRIPTIONAL FUSION; TRUNCATED HEMOGLOBINS; UP-REGULATION;

EID: 84866181185     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.01984-12     Document Type: Article
Times cited : (11)

References (45)
  • 1
    • 59349100734 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis groE promoter controls the expression of the bicistronic groESL1 operon and shows differential regulation under stress conditions
    • Aravindhan V, et al. 2009. Mycobacterium tuberculosis groE promoter controls the expression of the bicistronic groESL1 operon and shows differential regulation under stress conditions. FEMS Microbiol. Lett. 292: 42-49.
    • (2009) FEMS Microbiol. Lett. , vol.292 , pp. 42-49
    • Aravindhan, V.1
  • 2
    • 28144440256 scopus 로고    scopus 로고
    • Nitric oxide scavenging by Mycobacterium leprae GlbO involves the formation of the ferric heme-bound peroxynitrite intermediate
    • Ascenzi P, et al. 2006. Nitric oxide scavenging by Mycobacterium leprae GlbO involves the formation of the ferric heme-bound peroxynitrite intermediate. Biochem. Biophys. Res. Commun. 339:450-456.
    • (2006) Biochem. Biophys. Res. Commun. , vol.339 , pp. 450-456
    • Ascenzi, P.1
  • 3
    • 34447509223 scopus 로고    scopus 로고
    • Mycobacterial truncated hemoglobins: from genes to functions
    • Ascenzi P, Bolognesi M, Milani M, Guertin M, Visca P. 2007. Mycobacterial truncated hemoglobins: from genes to functions. Gene 398:42-51.
    • (2007) Gene , vol.398 , pp. 42-51
    • Ascenzi, P.1    Bolognesi, M.2    Milani, M.3    Guertin, M.4    Visca, P.5
  • 4
    • 0035448545 scopus 로고    scopus 로고
    • The evolution of mycobacterial pathogenicity: clues from comparative genomics
    • Brosch R, Pym AS, Gordon SV, Cole ST. 2001. The evolution of mycobacterial pathogenicity: clues from comparative genomics. Trends Microbiol. 9:452-458.
    • (2001) Trends Microbiol , vol.9 , pp. 452-458
    • Brosch, R.1    Pym, A.S.2    Gordon, S.V.3    Cole, S.T.4
  • 5
    • 53849139142 scopus 로고    scopus 로고
    • Evolution of intracellular pathogens
    • Casadevall A. 2008. Evolution of intracellular pathogens. Annu. Rev. Microbiol. 62:19-33.
    • (2008) Annu. Rev. Microbiol , vol.62 , pp. 19-33
    • Casadevall, A.1
  • 6
    • 0035931926 scopus 로고    scopus 로고
    • Massive gene decay in the leprosy bacillus
    • Cole ST, et al. 2001. Massive gene decay in the leprosy bacillus. Nature 409:1007-1011.
    • (2001) Nature , vol.409 , pp. 1007-1011
    • Cole, S.T.1
  • 7
    • 0035016754 scopus 로고    scopus 로고
    • The many faces of host responses to tuberculosis
    • Collins HL, Kaufmann SH. 2001. The many faces of host responses to tuberculosis. Immunology 103:1-9.
    • (2001) Immunology , vol.103 , pp. 1-9
    • Collins, H.L.1    Kaufmann, S.H.2
  • 8
    • 0033613114 scopus 로고    scopus 로고
    • A cooperative oxygen-binding hemoglobin from Mycobacterium tuberculosis
    • Couture M, et al. 1999. A cooperative oxygen-binding hemoglobin from Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. U. S. A. 96:11223-11228.
    • (1999) Proc. Natl. Acad. Sci. U. S. A , vol.96 , pp. 11223-11228
    • Couture, M.1
  • 9
    • 0035925053 scopus 로고    scopus 로고
    • Monitoring promoter activity and protein localization in Mycobacterium spp. using green fluorescent protein
    • Cowley SC, Av-Gay Y. 2001. Monitoring promoter activity and protein localization in Mycobacterium spp. using green fluorescent protein. Gene 264:225-231.
    • (2001) Gene , vol.264 , pp. 225-231
    • Cowley, S.C.1    Av-Gay, Y.2
  • 10
    • 0028881976 scopus 로고
    • Green fluorescent protein as a marker for gene expression and cell biology of mycobacterial interactions with macrophages
    • Dhandayuthapani S, et al. 1995. Green fluorescent protein as a marker for gene expression and cell biology of mycobacterial interactions with macrophages. Mol. Microbiol. 17:901-912.
    • (1995) Mol. Microbiol , vol.17 , pp. 901-912
    • Dhandayuthapani, S.1
  • 11
    • 0032500551 scopus 로고    scopus 로고
    • Constitutive and adaptive detoxification of nitric oxide in Escherichia coli. Role of nitric-oxide dioxygenase in the protection of aconitase
    • Gardner PR, Costantino G, Salzman AL. 1998. Constitutive and adaptive detoxification of nitric oxide in Escherichia coli. Role of nitric-oxide dioxygenase in the protection of aconitase. J. Biol. Chem. 273:26528-26533.
    • (1998) J. Biol. Chem , vol.273 , pp. 26528-26533
    • Gardner, P.R.1    Costantino, G.2    Salzman, A.L.3
  • 12
    • 0031684625 scopus 로고    scopus 로고
    • Induction of nitric oxide in human monocytes and monocyte cell lines by Mycobacterium tuberculosis
    • Jagannath C, Actor JK, Hunter RL, Jr. 1998. Induction of nitric oxide in human monocytes and monocyte cell lines by Mycobacterium tuberculosis. Nitric Oxide 2:174-186.
    • (1998) Nitric Oxide , vol.2 , pp. 174-186
    • Jagannath, C.1    Actor, J.K.2    Hunter Jr., R.L.3
  • 13
    • 67649831231 scopus 로고    scopus 로고
    • Role of pre-A motif in nitric oxide scavenging by truncated hemoglobin, HbN, of Mycobacterium tuberculosis
    • Lama A, et al. 2009. Role of pre-A motif in nitric oxide scavenging by truncated hemoglobin, HbN, of Mycobacterium tuberculosis. J. Biol. Chem. 284:14457-14468.
    • (2009) J. Biol. Chem , vol.284 , pp. 14457-14468
    • Lama, A.1
  • 14
    • 33745812343 scopus 로고    scopus 로고
    • Oxygen binding and NO scavenging properties of truncated hemoglobin, HbN, of Mycobacterium smegmatis
    • Lama A, Pawaria S, Dikshit KL. 2006. Oxygen binding and NO scavenging properties of truncated hemoglobin, HbN, of Mycobacterium smegmatis. FEBS Lett. 580:4031-4041.
    • (2006) FEBS Lett , vol.580 , pp. 4031-4041
    • Lama, A.1    Pawaria, S.2    Dikshit, K.L.3
  • 15
    • 0029091479 scopus 로고
    • Identification of macrophage and stress-induced proteins of Mycobacterium tuberculosis
    • Lee BY, Horwitz MA. 1995. Identification of macrophage and stress-induced proteins of Mycobacterium tuberculosis. J. Clin. Invest. 96:245-249.
    • (1995) J. Clin. Invest , vol.96 , pp. 245-249
    • Lee, B.Y.1    Horwitz, M.A.2
  • 16
    • 1642327485 scopus 로고    scopus 로고
    • Truncated hemoglobin o of Mycobacterium tuberculosis: the oligomeric state change and the interaction with membrane components
    • Liu C, He Y, Chang Z. 2004. Truncated hemoglobin o of Mycobacterium tuberculosis: the oligomeric state change and the interaction with membrane components. Biochem. Biophys. Res. Commun. 316:1163-1172.
    • (2004) Biochem. Biophys. Res. Commun , vol.316 , pp. 1163-1172
    • Liu, C.1    He, Y.2    Chang, Z.3
  • 17
    • 0028999596 scopus 로고
    • Altered responses to bacterial infection and endotoxic shock in mice lacking inducible nitric oxide synthase
    • MacMicking JD, et al. 1995. Altered responses to bacterial infection and endotoxic shock in mice lacking inducible nitric oxide synthase. Cell 81: 641-650.
    • (1995) Cell , vol.81 , pp. 641-650
    • MacMicking, J.D.1
  • 18
    • 0031010661 scopus 로고    scopus 로고
    • Identification of nitric oxide synthase as a protective locus against tuberculosis
    • MacMicking JD, et al. 1997. Identification of nitric oxide synthase as a protective locus against tuberculosis. Proc. Natl. Acad. Sci. U. S. A. 94: 5243-5248.
    • (1997) Proc. Natl. Acad. Sci. U. S. A , vol.94 , pp. 5243-5248
    • MacMicking, J.D.1
  • 19
    • 0026511987 scopus 로고
    • Environmental signals controlling expression of virulence determinants in bacteria
    • Mekalanos JJ. 1992. Environmental signals controlling expression of virulence determinants in bacteria. J. Bacteriol. 174:1-7.
    • (1992) J. Bacteriol , vol.174 , pp. 1-7
    • Mekalanos, J.J.1
  • 20
    • 0037177162 scopus 로고    scopus 로고
    • Unique ligand-protein interactions in a new truncated hemoglobin from Mycobacterium tuberculosis
    • Mukai M, Savard PY, Ouellet H, Guertin M, Yeh SR. 2002. Unique ligand-protein interactions in a new truncated hemoglobin from Mycobacterium tuberculosis. Biochemistry 41:3897-3905.
    • (2002) Biochemistry , vol.41 , pp. 3897-3905
    • Mukai, M.1    Savard, P.Y.2    Ouellet, H.3    Guertin, M.4    Yeh, S.R.5
  • 21
    • 0026629902 scopus 로고
    • Nitric oxide as a secretory product of mammalian cells
    • Nathan C. 1992. Nitric oxide as a secretory product of mammalian cells. FASEB J. 6:3051-3064.
    • (1992) FASEB J , vol.6 , pp. 3051-3064
    • Nathan, C.1
  • 22
    • 0034255209 scopus 로고    scopus 로고
    • Reactive oxygen and nitrogen intermediates in the relationship between mammalian hosts and microbial pathogens
    • Nathan C, Shiloh MU. 2000. Reactive oxygen and nitrogen intermediates in the relationship between mammalian hosts and microbial pathogens. Proc. Natl. Acad. Sci. U. S. A. 97:8841-8848.
    • (2000) Proc. Natl. Acad. Sci. U. S. A , vol.97 , pp. 8841-8848
    • Nathan, C.1    Shiloh, M.U.2
  • 23
    • 0034650427 scopus 로고    scopus 로고
    • Cutting edge: heat shock protein 60 is a putative endogenous ligand of the Toll-like receptor-4 complex
    • Ohashi K, Burkart V, Flohe S, Kolb H. 2000. Cutting edge: heat shock protein 60 is a putative endogenous ligand of the Toll-like receptor-4 complex. J. Immunol. 164:558-561.
    • (2000) J. Immunol , vol.164 , pp. 558-561
    • Ohashi, K.1    Burkart, V.2    Flohe, S.3    Kolb, H.4
  • 24
    • 0037197913 scopus 로고    scopus 로고
    • Truncated hemoglobin HbN protects Mycobacterium bovis from nitric oxide
    • Ouellet H, et al. 2002. Truncated hemoglobin HbN protects Mycobacterium bovis from nitric oxide. Proc. Natl. Acad. Sci. U. S. A. 99:5902-5907.
    • (2002) Proc. Natl. Acad. Sci. U. S. A , vol.99 , pp. 5902-5907
    • Ouellet, H.1
  • 25
    • 0036049852 scopus 로고    scopus 로고
    • Nitric oxide scavenging and detoxification by the Mycobacterium tuberculosis haemoglobin, HbN in Escherichia coli
    • Pathania R, Navani NK, Gardner AM, Gardner PR, Dikshit KL. 2002. Nitric oxide scavenging and detoxification by the Mycobacterium tuberculosis haemoglobin, HbN in Escherichia coli. Mol. Microbiol. 45:1303-1314.
    • (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
  • 26
    • 0037013274 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis hemoglobin HbO associates with membranes and stimulates cellular respiration of recombinant Escherichia coli
    • Pathania R, Navani NK, Rajamohan G, Dikshit KL. 2002. Mycobacterium tuberculosis hemoglobin HbO associates with membranes and stimulates cellular respiration of recombinant Escherichia coli. J. Biol. Chem. 277:15293-15302.
    • (2002) J. Biol. Chem , vol.277 , pp. 15293-15302
    • Pathania, R.1    Navani, N.K.2    Rajamohan, G.3    Dikshit, K.L.4
  • 27
    • 44949234852 scopus 로고    scopus 로고
    • Responses of Mycobacterium tuberculosis hemoglobin promoters to in vitro and in vivo growth conditions
    • Pawaria S, Lama A, Raje M, Dikshit KL. 2008. Responses of Mycobacterium tuberculosis hemoglobin promoters to in vitro and in vivo growth conditions. Appl. Environ. Microbiol. 74:3512-3522.
    • (2008) Appl. Environ. Microbiol , vol.74 , pp. 3512-3522
    • Pawaria, S.1    Lama, A.2    Raje, M.3    Dikshit, K.L.4
  • 28
    • 34047270404 scopus 로고    scopus 로고
    • Intracellular growth and survival of Salmonella enterica serovar Typhimurium carrying truncated hemoglobins of Mycobacterium tuberculosis
    • Pawaria S, et al. 2007. Intracellular growth and survival of Salmonella enterica serovar Typhimurium carrying truncated hemoglobins of Mycobacterium tuberculosis. Microb. Pathog. 42:119-128.
    • (2007) Microb. Pathog , vol.42 , pp. 119-128
    • Pawaria, S.1
  • 29
    • 34547943491 scopus 로고    scopus 로고
    • Protein structure in the truncated (2/2) hemoglobin family
    • Pesce A, Nardini M, Milani M, Bolognesi M. 2007. Protein structure in the truncated (2/2) hemoglobin family. IUBMB Life 59:535-541.
    • (2007) IUBMB Life , vol.59 , pp. 535-541
    • Pesce, A.1    Nardini, M.2    Milani, M.3    Bolognesi, M.4
  • 30
    • 0042235547 scopus 로고    scopus 로고
    • Heat shock proteins as regulators of the immune response
    • Pockley AG. 2003. Heat shock proteins as regulators of the immune response. Lancet 362:469-476.
    • (2003) Lancet , vol.362 , pp. 469-476
    • Pockley, A.G.1
  • 32
    • 0031400122 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis (MTB)-stimulated production of nitric oxide by human alveolar macrophages and relationship of nitric oxide production to growth inhibition of MTB
    • Rich EA, et al. 1997. Mycobacterium tuberculosis (MTB)-stimulated production of nitric oxide by human alveolar macrophages and relationship of nitric oxide production to growth inhibition of MTB. Tuber. Lung Dis. 78:247-255.
    • (1997) Tuber. Lung Dis , vol.78 , pp. 247-255
    • Rich, E.A.1
  • 33
    • 27644485468 scopus 로고    scopus 로고
    • Identification of moaA3 gene in patient isolates of Mycobacterium tuberculosis in Kerala, which is absent in M. tuberculosis H37Rv and H37Ra
    • Sarojini S, Soman S, Radhakrishnan I, Mundayoor S. 2005. Identification of moaA3 gene in patient isolates of Mycobacterium tuberculosis in Kerala, which is absent in M. tuberculosis H37Rv and H37Ra. BMCInfect. Dis. 5:81.
    • (2005) BMCInfect. Dis , vol.5 , pp. 81
    • Sarojini, S.1    Soman, S.2    Radhakrishnan, I.3    Mundayoor, S.4
  • 34
    • 0034826633 scopus 로고    scopus 로고
    • Silencing of oxidative stress response in Mycobacterium tuberculosis: expression patterns of ahpC in virulent and avirulent strains and effect of ahpC inactivation
    • Springer B, et al. 2001. Silencing of oxidative stress response in Mycobacterium tuberculosis: expression patterns of ahpC in virulent and avirulent strains and effect of ahpC inactivation. Infect. Immun. 69:5967-5973.
    • (2001) Infect. Immun , vol.69 , pp. 5967-5973
    • Springer, B.1
  • 35
    • 0025922291 scopus 로고
    • New use of BCG for recombinant vaccines
    • Stover CK, et al. 1991. New use of BCG for recombinant vaccines. Nature 351:456-460.
    • (1991) Nature , vol.351 , pp. 456-460
    • Stover, C.K.1
  • 36
    • 0037177833 scopus 로고    scopus 로고
    • HSP70 as endogenous stimulus of the Toll/interleukin-1 receptor signal pathway
    • Vabulas RM, et al. 2002. HSP70 as endogenous stimulus of the Toll/interleukin-1 receptor signal pathway. J. Biol. Chem. 277:15107-15112.
    • (2002) J. Biol. Chem , vol.277 , pp. 15107-15112
    • Vabulas, R.M.1
  • 37
    • 84859645414 scopus 로고    scopus 로고
    • The response of Mycobacterium tuberculosis to reactive oxygen and nitrogen species
    • Voskuil MI, Bartek IL, Visconti K, Schoolnik GK. 2011. The response of Mycobacterium tuberculosis to reactive oxygen and nitrogen species. Front. Microbiol. 2:105.
    • (2011) Front. Microbiol , vol.2 , pp. 105
    • Voskuil, M.I.1    Bartek, I.L.2    Visconti, K.3    Schoolnik, G.K.4
  • 38
    • 33646341657 scopus 로고    scopus 로고
    • A phylogenetic and structural analysis of truncated hemoglobins
    • Vuletich DA, Lecomte JT. 2006. A phylogenetic and structural analysis of truncated hemoglobins. J. Mol. Evol. 62:196-210.
    • (2006) J. Mol. Evol , vol.62 , pp. 196-210
    • Vuletich, D.A.1    Lecomte, J.T.2
  • 39
    • 0030589083 scopus 로고    scopus 로고
    • Electroporation at elevated temperatures substantially improves transformation efficiency of slow-growing mycobacteria
    • Wards BJ, Collins DM. 1996. Electroporation at elevated temperatures substantially improves transformation efficiency of slow-growing mycobacteria. FEMS Microbiol. Lett. 145:101-105.
    • (1996) FEMS Microbiol. Lett , vol.145 , pp. 101-105
    • Wards, B.J.1    Collins, D.M.2
  • 40
    • 0037059826 scopus 로고    scopus 로고
    • Truncated hemoglobins: a new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants
    • Wittenberg JB, Bolognesi M, Wittenberg BA, Guertin M. 2002. Truncated hemoglobins: a new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants. J. Biol. Chem. 277:871-874.
    • (2002) J. Biol. Chem , vol.277 , pp. 871-874
    • Wittenberg, J.B.1    Bolognesi, M.2    Wittenberg, B.A.3    Guertin, M.4
  • 41
    • 0031002421 scopus 로고    scopus 로고
    • Superoxide and peroxynitrite generation from inducible nitric oxide synthase in macrophages
    • Xia Y, Zweier JL. 1997. Superoxide and peroxynitrite generation from inducible nitric oxide synthase in macrophages. Proc. Natl. Acad. Sci. U. S. A. 94:6954-6958.
    • (1997) Proc. Natl. Acad. Sci. U. S. A , vol.94 , pp. 6954-6958
    • Xia, Y.1    Zweier, J.L.2
  • 42
    • 0025776531 scopus 로고
    • Heat shock proteins and antigens of Mycobacterium tuberculosis
    • Young DB, Garbe TR. 1991. Heat shock proteins and antigens of Mycobacterium tuberculosis. Infect. Immun. 59:3086-3093.
    • (1991) Infect. Immun , vol.59 , pp. 3086-3093
    • Young, D.B.1    Garbe, T.R.2
  • 43
    • 79953675701 scopus 로고    scopus 로고
    • Nicotine-induced differential modulation of autoimmune arthritis in the Lewis rat involves changes in interleukin-17 and anti-cyclic citrullinated peptide antibodies
    • Yu H, Yang YH, Rajaiah R, Moudgil KD. 2011. Nicotine-induced differential modulation of autoimmune arthritis in the Lewis rat involves changes in interleukin-17 and anti-cyclic citrullinated peptide antibodies. Arthritis Rheum. 63:981-991.
    • (2011) Arthritis Rheum , vol.63 , pp. 981-991
    • Yu, H.1    Yang, Y.H.2    Rajaiah, R.3    Moudgil, K.D.4
  • 44
    • 79851486240 scopus 로고    scopus 로고
    • Nitric oxide dioxygenation reaction in DevS and the initial response to nitric oxide in Mycobacterium tuberculosis
    • Yukl ET, et al. 2011. Nitric oxide dioxygenation reaction in DevS and the initial response to nitric oxide in Mycobacterium tuberculosis. Biochemistry 50:1023-1028.
    • (2011) Biochemistry , vol.50 , pp. 1023-1028
    • Yukl, E.T.1
  • 45
    • 0030026515 scopus 로고    scopus 로고
    • Peroxynitrite-mediated DNA strand breakage activates poly-adenosine diphosphate ribosyl synthetase and causes cellular energy depletion in macrophages stimulated with bacterial lipopolysaccharide
    • Zingarelli B, O'Connor M, Wong H, Salzman AL, Szabo C. 1996. Peroxynitrite-mediated DNA strand breakage activates poly-adenosine diphosphate ribosyl synthetase and causes cellular energy depletion in macrophages stimulated with bacterial lipopolysaccharide. J. Immunol. 156:350-358.
    • (1996) J. Immunol , vol.156 , pp. 350-358
    • Zingarelli, B.1    O'Connor, M.2    Wong, H.3    Salzman, A.L.4    Szabo, C.5


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