메뉴 건너뛰기




Volumn 224, Issue 1, 2003, Pages 127-132

Vitreoscilla hemoglobin promoter is not responsive to nitrosative and oxidative stress in Escherichia coli

Author keywords

Gene regulation; Nitrosative stress; Oxidative stress; Vitreoscilla hemoglobin

Indexed keywords

BACTERIAL ENZYME; BACTERIAL PROTEIN; CHLORAMPHENICOL ACETYLTRANSFERASE; FLAVOPROTEIN; HEMOGLOBIN;

EID: 0037632516     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(03)00434-8     Document Type: Article
Times cited : (12)

References (34)
  • 1
    • 0014027821 scopus 로고
    • The purification and properties of cytochrome o from Vitreoscilla
    • Webster D.A., Hackett D.P. The purification and properties of cytochrome o from Vitreoscilla. J. Biol. Chem. 241:1966;3308-3315.
    • (1966) J. Biol. Chem. , vol.241 , pp. 3308-3315
    • Webster, D.A.1    Hackett, D.P.2
  • 2
    • 0024428050 scopus 로고
    • Characterization of the oxygen-dependent promoter of the Vitreoscilla hemoglobin gene in Escherichia coli
    • Khosla C., Bailey J.E. Characterization of the oxygen-dependent promoter of the Vitreoscilla hemoglobin gene in Escherichia coli. J. Bacteriol. 171:1989;5990-6004.
    • (1989) J. Bacteriol. , vol.171 , pp. 5990-6004
    • Khosla, C.1    Bailey, J.E.2
  • 3
    • 0025353062 scopus 로고
    • Study of Vitreoscilla globin (vgb) gene expression and promoter activity in E. coli through transcriptional fusion
    • Dikshit K.L., Dikshit R.P., Webster D.A. Study of Vitreoscilla globin (vgb) gene expression and promoter activity in E. coli through transcriptional fusion. Nucleic Acids Res. 18:1990;4149-4155.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 4149-4155
    • Dikshit, K.L.1    Dikshit, R.P.2    Webster, D.A.3
  • 4
    • 14744278506 scopus 로고
    • Actinorhodin production by Streptomyces coelicolor and growth of Streptomyces lividans are improved by the expression of a bacterial hemoglobin
    • Magnolo S.K., Leenutaphong D.L., Demodena J.A., Curtis J.E., Bailey J.E., Galazzo J.L., Hughes D.E. Actinorhodin production by Streptomyces coelicolor and growth of Streptomyces lividans are improved by the expression of a bacterial hemoglobin. Bio/Technology. 9:1991;473-476.
    • (1991) Bio/Technology , vol.9 , pp. 473-476
    • Magnolo, S.K.1    Leenutaphong, D.L.2    Demodena, J.A.3    Curtis, J.E.4    Bailey, J.E.5    Galazzo, J.L.6    Hughes, D.E.7
  • 5
    • 0032487128 scopus 로고    scopus 로고
    • Metabolic engineering of Serratia marcescens with the bacterial hemoglobin gene: Alterations in fermentation pathways
    • Wei M.L., Webster D.A., Stark B.C. Metabolic engineering of Serratia marcescens with the bacterial hemoglobin gene: Alterations in fermentation pathways. Biotechnol. Bioeng. 59:1998;640-646.
    • (1998) Biotechnol. Bioeng. , vol.59 , pp. 640-646
    • Wei, M.L.1    Webster, D.A.2    Stark, B.C.3
  • 6
    • 0344117846 scopus 로고    scopus 로고
    • Rhizobium etli genetically engineered for the heterologous expression of Vitreoscilla sp. hemoglobin: Effect on free-living and symbiosis
    • Ramírez M., Valderrama B., Arrendondo-Peter R., Sobéron M., Mora J., Hernández G. Rhizobium etli genetically engineered for the heterologous expression of Vitreoscilla sp. hemoglobin: Effect on free-living and symbiosis. Mol. Plant-Microbe Interact. 12:1999;1008-1015.
    • (1999) Mol. Plant-Microbe Interact. , vol.12 , pp. 1008-1015
    • Ramírez, M.1    Valderrama, B.2    Arrendondo-Peter, R.3    Sobéron, M.4    Mora, J.5    Hernández, G.6
  • 7
    • 0033951878 scopus 로고    scopus 로고
    • Cloning and expression of Vitreoscilla hemoglobin gene in Burkholderia sp. strain DNT for enhancement of 2,4-dinitrotoluene degradation
    • Patel S.M., Stark B.C., Hwang K.W., Dikshit K.L., Webster D.A. Cloning and expression of Vitreoscilla hemoglobin gene in Burkholderia sp. strain DNT for enhancement of 2,4-dinitrotoluene degradation. Biotechnol. Prog. 16:2000;26-30.
    • (2000) Biotechnol. Prog. , vol.16 , pp. 26-30
    • Patel, S.M.1    Stark, B.C.2    Hwang, K.W.3    Dikshit, K.L.4    Webster, D.A.5
  • 8
    • 0029294091 scopus 로고
    • Fnr, a global transcriptional regulator of Escherichia coli, activates the Vitreoscilla hemoglobin (vhb) promoter and intracellular VHb expression increases cytochrome d promoter activity
    • Tsai P.S., Kallio P.T., Bailey J.E. Fnr, a global transcriptional regulator of Escherichia coli, activates the Vitreoscilla hemoglobin (vhb) promoter and intracellular VHb expression increases cytochrome d promoter activity. Biotechnol. Prog. 11:1995;288-293.
    • (1995) Biotechnol. Prog. , vol.11 , pp. 288-293
    • Tsai, P.S.1    Kallio, P.T.2    Bailey, J.E.3
  • 9
    • 0025116097 scopus 로고
    • Expression of recombinant proteins in Escherichia coli using an oxygen-responsive promoter
    • Khosla C., Curtis J.E., Bydalek P., Swartz J.R., Bailey J.E. Expression of recombinant proteins in Escherichia coli using an oxygen-responsive promoter. Bio/Technology. 8:1990;554-558.
    • (1990) Bio/Technology , vol.8 , pp. 554-558
    • Khosla, C.1    Curtis, J.E.2    Bydalek, P.3    Swartz, J.R.4    Bailey, J.E.5
  • 10
    • 85031156176 scopus 로고    scopus 로고
    • Kallio, P.T., Frey, A.D. and Bailey, J.E. (2001) From Vitreoscilla hemoglobin (VHb) to a novel class of growth stimulating hemoglobin proteins. In: Recombinant Protein Production with Prokaryotic and Eukaryotic Cells. A Comparative View on Host Physiology (Merten, O.-W., Mattanovich, D., Larsson, G., Neubauer, P., Lang, C., Porro, D., Teixeira de Mattos, J., Postma, P. and Cole, J., Eds.), pp. 75-87. Kluwer Academic, Dordrecht.
    • Kallio, P.T., Frey, A.D. and Bailey, J.E. (2001) From Vitreoscilla hemoglobin (VHb) to a novel class of growth stimulating hemoglobin proteins. In: Recombinant Protein Production with Prokaryotic and Eukaryotic Cells. A Comparative View on Host Physiology (Merten, O.-W., Mattanovich, D., Larsson, G., Neubauer, P., Lang, C., Porro, D., Teixeira de Mattos, J., Postma, P. and Cole, J., Eds.), pp. 75-87. Kluwer Academic, Dordrecht.
  • 11
    • 0036794855 scopus 로고    scopus 로고
    • Bacterial hemoglobins and flavohemoglobins for alleviation of nitrosative stress in Escherichia coli
    • Frey A.D., Farrés J., Bollinger C.J.T., 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    Farrés, J.2    Bollinger, C.J.T.3    Kallio, P.T.4
  • 12
    • 0036135136 scopus 로고    scopus 로고
    • Chimeric Vitreoscilla hemoglobin (VHb) carrying a flavoreductase domain relieves nitrosative stress in Escherichia coli: New insight into the functional role of VHb
    • Kaur R., Pathania R., Sharma V., Mande S.C., Dikshit K.L. Chimeric Vitreoscilla hemoglobin (VHb) carrying a flavoreductase domain relieves nitrosative stress in Escherichia coli: New insight into the functional role of VHb. Appl. Environ. Microbiol. 68:2002;152-160.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 152-160
    • Kaur, R.1    Pathania, R.2    Sharma, V.3    Mande, S.C.4    Dikshit, K.L.5
  • 13
    • 0029967350 scopus 로고    scopus 로고
    • Oxygen-controlled regulation of the flavohemoglobin gene in Bacillus subtilis
    • LaCelle M., Kumano M., Kurita K., Yamane K., Zuber P., Nakano M.M. Oxygen-controlled regulation of the flavohemoglobin gene in Bacillus subtilis. J. Bacteriol. 178:1996;3803-3808.
    • (1996) J. Bacteriol. , vol.178 , pp. 3803-3808
    • LaCelle, M.1    Kumano, M.2    Kurita, K.3    Yamane, K.4    Zuber, P.5    Nakano, M.M.6
  • 14
    • 0344417899 scopus 로고    scopus 로고
    • Regulation of hmp gene transcription in Mycobacterium tuberculosis: Effects of oxygen limitation and nitrosative and oxidative stress
    • Hu Y.M., Butcher P.D., Mangan J.A., Rajandream M.A., 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.M.1    Butcher, P.D.2    Mangan, J.A.3    Rajandream, M.A.4    Coates, A.R.M.5
  • 15
    • 0034072208 scopus 로고    scopus 로고
    • New functions for the ancient globin family: Bacterial responses to nitric oxide and nitrosative stress
    • Poole R.K., Hughes M.N. New functions for the ancient globin family: Bacterial responses to nitric oxide and nitrosative stress. Mol. Microbiol. 36:2000;775-783.
    • (2000) Mol. Microbiol. , vol.36 , pp. 775-783
    • Poole, R.K.1    Hughes, M.N.2
  • 16
    • 0024080671 scopus 로고
    • The Vitreoscilla hemoglobin gene: Molecular cloning, nucleotide sequence and genetic expression in Escherichia coli
    • Khosla C., Bailey J.E. The Vitreoscilla hemoglobin gene: Molecular cloning, nucleotide sequence and genetic expression in Escherichia coli. Mol. Gen. Genet. 214:1988;158-161.
    • (1988) Mol. Gen. Genet. , vol.214 , pp. 158-161
    • Khosla, C.1    Bailey, J.E.2
  • 17
    • 0024470362 scopus 로고
    • A new oxygen-regulated promoter for the expression of proteins in Escherichia coli
    • Hughes D.E., Curtis J.E., Khosla C., Bailey J.E. A new oxygen-regulated promoter for the expression of proteins in Escherichia coli. BioTechniques. 7:1989;1026-1028.
    • (1989) BioTechniques , vol.7 , pp. 1026-1028
    • Hughes, D.E.1    Curtis, J.E.2    Khosla, C.3    Bailey, J.E.4
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage-T4
    • Laemmli U.K. Cleavage of structural proteins during assembly of the head of bacteriophage-T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0036010276 scopus 로고    scopus 로고
    • Improved cell growth in tobacco suspension cultures expressing Vitreoscilla hemoglobin
    • Farrés J., Kallio P.T. Improved cell growth in tobacco suspension cultures expressing Vitreoscilla hemoglobin. Biotechnol. Prog. 18:2002;229-233.
    • (2002) Biotechnol. Prog. , vol.18 , pp. 229-233
    • Farrés, J.1    Kallio, P.T.2
  • 20
    • 0034450181 scopus 로고    scopus 로고
    • Streptomycetes in micro-cultures: Growth, production of secondary metabolites, and storage and retrieval in the 96-well format
    • Minas W., Bailey J.E., Duetz W. Streptomycetes in micro-cultures: Growth, production of secondary metabolites, and storage and retrieval in the 96-well format. Antonie Van Leeuwenhoek. 78:2000;297-305.
    • (2000) Antonie Van Leeuwenhoek , vol.78 , pp. 297-305
    • Minas, W.1    Bailey, J.E.2    Duetz, W.3
  • 21
    • 0343673773 scopus 로고    scopus 로고
    • Methods for intense aeration, growth, storage, and replication of bacterial strains in microtiter plates
    • Duetz W.A., Ruedi L., Hermann R., O'Connor K., Buchs J., Witholt B. Methods for intense aeration, growth, storage, and replication of bacterial strains in microtiter plates. Appl. Environ. Microbiol. 66:2000;2641-2646.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 2641-2646
    • Duetz, W.A.1    Ruedi, L.2    Hermann, R.3    O'Connor, K.4    Buchs, J.5    Witholt, B.6
  • 22
    • 0029831326 scopus 로고    scopus 로고
    • Nitric oxide, nitrite, and Fnr regulation of hmp (flavohemoglobin) gene expression in Escherichia coli K-12
    • Poole R.K., Anjum M.F., Membrillo-Hernández J., Kim S.O., Hughes M.N., Stewart V. Nitric oxide, nitrite, and Fnr regulation of hmp (flavohemoglobin) gene expression in Escherichia coli K-12. J. Bacteriol. 178:1996;5487-5492.
    • (1996) J. Bacteriol. , vol.178 , pp. 5487-5492
    • Poole, R.K.1    Anjum, M.F.2    Membrillo-Hernández, J.3    Kim, S.O.4    Hughes, M.N.5    Stewart, V.6
  • 24
    • 0032545367 scopus 로고    scopus 로고
    • Regulation of the Salmonella typhimurium flavohemoglobin gene. A new pathway for bacterial gene expression in response to nitric oxide
    • Crawford M.J., Goldberg D.E. Regulation of the Salmonella typhimurium flavohemoglobin gene. A new pathway for bacterial gene expression in response to nitric oxide. J. Biol. Chem. 273:1998;34028-34032.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34028-34032
    • Crawford, M.J.1    Goldberg, D.E.2
  • 25
    • 0031844664 scopus 로고    scopus 로고
    • A novel mechanism for upregulation of the Escherichia coli K-12 hmp (flavohaemoglobin) gene by the 'NO releaser', S-nitrosoglutathione: Nitrosation of homocysteine and modulation of MetR binding to the glyA-hmp intergenic region
    • Membrillo-Hernández J., Coopamah M.D., Channa A., Hughes M.N., Poole R.K. A novel mechanism for upregulation of the Escherichia coli K-12 hmp (flavohaemoglobin) gene by the 'NO releaser', S-nitrosoglutathione: Nitrosation of homocysteine and modulation of MetR binding to the glyA-hmp intergenic region. Mol. Microbiol. 29:1998;1101-1112.
    • (1998) Mol. Microbiol. , vol.29 , pp. 1101-1112
    • Membrillo-Hernández, J.1    Coopamah, M.D.2    Channa, A.3    Hughes, M.N.4    Poole, R.K.5
  • 27
    • 0033017012 scopus 로고    scopus 로고
    • Anoxic function for the Escherichia coli flavohaemoglobin (Hmp): Reversible binding of nitric oxide and reduction to nitrous oxide
    • Kim S.O., Orii Y., Lloyd D., Hughes M.N., Poole R.K. Anoxic function for the Escherichia coli flavohaemoglobin (Hmp): Reversible binding of nitric oxide and reduction to nitrous oxide. FEBS Lett. 445:1999;389-394.
    • (1999) FEBS Lett. , vol.445 , pp. 389-394
    • Kim, S.O.1    Orii, Y.2    Lloyd, D.3    Hughes, M.N.4    Poole, R.K.5
  • 28
    • 0037040921 scopus 로고    scopus 로고
    • Flavorubredoxin, an inducible catalyst for nitric oxide reduction and detoxification in Escherichia coli
    • Gardner A.M., Helmick R.A., Gardner P.R. Flavorubredoxin, an inducible catalyst for nitric oxide reduction and detoxification in Escherichia coli. J. Biol. Chem. 277:2002;8172-8177.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8172-8177
    • Gardner, A.M.1    Helmick, R.A.2    Gardner, P.R.3
  • 30
    • 0032529916 scopus 로고    scopus 로고
    • Response of the NAD(P)H-oxidising flavohaemoglobin (Hmp) to prolonged oxidative stress and implications for its physiological role in Escherichia coli
    • Anjum M.F., Ioannidis N., Poole R.K. Response of the NAD(P)H-oxidising flavohaemoglobin (Hmp) to prolonged oxidative stress and implications for its physiological role in Escherichia coli. FEMS Microbiol. Lett. 166:1998;219-223.
    • (1998) FEMS Microbiol. Lett. , vol.166 , pp. 219-223
    • Anjum, M.F.1    Ioannidis, N.2    Poole, R.K.3
  • 31
    • 0018801772 scopus 로고
    • An oxygen-binding flavohemoprotein from Alcaligenes eutrophus
    • Probst I., Wolf G., Schlegel H.G. An oxygen-binding flavohemoprotein from Alcaligenes eutrophus. Biochim. Biophys. Acta. 576:1979;471-478.
    • (1979) Biochim. Biophys. Acta , vol.576 , pp. 471-478
    • Probst, I.1    Wolf, G.2    Schlegel, H.G.3
  • 32
    • 0028242684 scopus 로고
    • Primary sequence and evidence for a physiological function of the flavohemoprotein of Alcaligenes eutrophus
    • Cramm R., Siddiqui R.A., Friedrich B. Primary sequence and evidence for a physiological function of the flavohemoprotein of Alcaligenes eutrophus. J. Biol. Chem. 269:1994;7349-7354.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7349-7354
    • Cramm, R.1    Siddiqui, R.A.2    Friedrich, B.3
  • 33
    • 0034644756 scopus 로고    scopus 로고
    • Nitric-oxide dioxygenase activity and function of flavohemoglobins. Sensitivity to nitric oxide and carbon monoxide inhibition
    • Gardner P.R., Gardner A.M., Martin L.A., Dou Y., Li T., Olson J.S., Zhu H., Riggs A.F. Nitric-oxide dioxygenase activity and function of flavohemoglobins. Sensitivity to nitric oxide and carbon monoxide inhibition. J. Biol. Chem. 275:2000;31581-31587.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31581-31587
    • Gardner, P.R.1    Gardner, A.M.2    Martin, L.A.3    Dou, Y.4    Li, T.5    Olson, J.S.6    Zhu, H.7    Riggs, A.F.8
  • 34
    • 0025287522 scopus 로고
    • Steady-state nitric oxide concentrations during denitrification
    • Goretski J., Zafiriou O.C., Hollocher T.C. Steady-state nitric oxide concentrations during denitrification. J. Biol. Chem. 265:1990;11535-11538.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11535-11538
    • Goretski, J.1    Zafiriou, O.C.2    Hollocher, T.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.