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Volumn 50, Issue 3, 2003, Pages 169-175

Fusion protein system designed to provide color to aid in the expression and purification of proteins in Escherichia coli

Author keywords

Affinity purification; Bacterial hemoglobin; Expression vector; Recombinant plasmid; Vitreoscilla

Indexed keywords

CARBON MONOXIDE; CYTOCHROME B; HEMOGLOBIN; HISTIDINE; HYBRID PROTEIN; INTEGRASE; PROTEIN SUBUNIT; SOLUBILIZER; THROMBIN;

EID: 0142215592     PISSN: 0147619X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0147-619X(03)00046-5     Document Type: Article
Times cited : (15)

References (30)
  • 1
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair A., Finley D., Varshavsky A. In vivo half-life of a protein is a function of its amino-terminal residue. Science. 234:1986;179-186. Bujard H., Gentz R., Lanzer M., Stueber D., Mueller M., Ibrahimi I., Haeuptle M.T., Dobberstein B. A T5 promoter-based transcription-translation system for the analysis of proteins in vitro and in vivo. Methods Enzymol. 155:1987;416-433.
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 3
    • 0027456715 scopus 로고
    • Domains of the integrase protein of human immunodeficiency virus type 1 responsible for polynucleotidyl transfer and zinc binding
    • Bushman F.D., Engelman A., Palmer I., Wingfield P., Craigie R. Domains of the integrase protein of human immunodeficiency virus type 1 responsible for polynucleotidyl transfer and zinc binding. Proc. Natl. Acad. Sci. USA. 90:1993;3428-3432.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3428-3432
    • Bushman, F.D.1    Engelman, A.2    Palmer, I.3    Wingfield, P.4    Craigie, R.5
  • 4
    • 0034799404 scopus 로고    scopus 로고
    • Chromosomal integration of the Vitreoscilla hemoglobin gene in Burkholderia and Pseudomonas for the purpose of producing stable engineered strains with enhanced bioremediating ability
    • Chung J.W., Webster D.A., Pagilla K.R., Stark B.C. Chromosomal integration of the Vitreoscilla hemoglobin gene in Burkholderia and Pseudomonas for the purpose of producing stable engineered strains with enhanced bioremediating ability. J. Ind. Microbiol. Biotechnol. 27:2001;27-33.
    • (2001) J. Ind. Microbiol. Biotechnol. , vol.27 , pp. 27-33
    • Chung, J.W.1    Webster, D.A.2    Pagilla, K.R.3    Stark, B.C.4
  • 5
    • 0023680201 scopus 로고
    • Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein
    • di Guan C., Li P., Riggs P.D., Inouye H. Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein. Gene. 67:1988;21-30.
    • (1988) Gene , vol.67 , pp. 21-30
    • Di Guan, C.1    Li, P.2    Riggs, P.D.3    Inouye, H.4
  • 6
    • 0023756153 scopus 로고
    • Cloning, characterization and expression of the bacterial globin gene from Vitreoscilla in Escherichia coli
    • Dikshit K.L., Webster D.A. Cloning, characterization and expression of the bacterial globin gene from Vitreoscilla in Escherichia coli. Gene. 70:1988;377-386.
    • (1988) Gene , vol.70 , pp. 377-386
    • Dikshit, K.L.1    Webster, D.A.2
  • 7
    • 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
  • 8
    • 0026533385 scopus 로고
    • The bacterial hemoglobin from Vitreoscilla can support the aerobic growth of Eschericia coli lacking terminal oxidases
    • Dikshit R.P., Dikshit K.L., Liu Y., Webster D.A. The bacterial hemoglobin from Vitreoscilla can support the aerobic growth of Eschericia coli lacking terminal oxidases. Arch. Biochem. Biophys. 293:1992;241-245.
    • (1992) Arch. Biochem. Biophys. , vol.293 , pp. 241-245
    • Dikshit, R.P.1    Dikshit, K.L.2    Liu, Y.3    Webster, D.A.4
  • 9
    • 0031819672 scopus 로고    scopus 로고
    • Site-directed mutagenesis of bacterial hemoglobin: The role of glutamine (E7) in oxygen-binding in the distal heme pocket
    • Dikshit K.L., Orii Y., Navani N., Patel S., Huang H.Y., Stark B.C., Webster D.A. Site-directed mutagenesis of bacterial hemoglobin: the role of glutamine (E7) in oxygen-binding in the distal heme pocket. Arch. Biochem. Biophys. 349:1998;161-166.
    • (1998) Arch. Biochem. Biophys. , vol.349 , pp. 161-166
    • Dikshit, K.L.1    Orii, Y.2    Navani, N.3    Patel, S.4    Huang, H.Y.5    Stark, B.C.6    Webster, D.A.7
  • 10
    • 0025977037 scopus 로고
    • Eukaryotic proteins expressed in Escherichia coli: An improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase
    • Guan K.L., Dixon I.E. Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase. Anal. Biochem. 192:1991;262-267.
    • (1991) Anal. Biochem. , vol.192 , pp. 262-267
    • Guan, K.L.1    Dixon, I.E.2
  • 11
    • 0027973067 scopus 로고
    • Biophysical and enzymatic properties of the catalytic domain of HIV-1 integrase
    • Hickman A.B., Palmer I., Engelman A., Craigie R., Wingfield P. Biophysical and enzymatic properties of the catalytic domain of HIV-1 integrase. J. Biol. Chem. 269:1994;29279-29287.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29279-29287
    • Hickman, A.B.1    Palmer, I.2    Engelman, A.3    Craigie, R.4    Wingfield, P.5
  • 12
    • 0037313950 scopus 로고    scopus 로고
    • Isolation, sequencing, and characterization of the cytochrome bo operon from Vitreoscilla
    • Hwang K.W., Kim S.K., Kim K.J., Chung Y.T., Stark B.C., Webster D.A. Isolation, sequencing, and characterization of the cytochrome bo operon from Vitreoscilla. DNA Sequence. 14:2003;53-59.
    • (2003) DNA Sequence , vol.14 , pp. 53-59
    • Hwang, K.W.1    Kim, S.K.2    Kim, K.J.3    Chung, Y.T.4    Stark, B.C.5    Webster, D.A.6
  • 13
    • 0025645664 scopus 로고
    • Presence of the bacterial hemoglobin gene improves α-amylase production of a recombinant Escherichia coli strain
    • Khosravi M., Webster D.A., Stark B.C. Presence of the bacterial hemoglobin gene improves α-amylase production of a recombinant Escherichia coli strain. Plasmid. 24:1990;190-194.
    • (1990) Plasmid , vol.24 , pp. 190-194
    • Khosravi, M.1    Webster, D.A.2    Stark, B.C.3
  • 14
    • 0023874286 scopus 로고
    • Heterologous expression of a bacterial hemoglobin improves the growth properties of recombinant Escherichia coli
    • Khosla C., Bailey J.E. Heterologous expression of a bacterial hemoglobin improves the growth properties of recombinant Escherichia coli. Nature. 331:1988;633-635.
    • (1988) Nature , vol.331 , pp. 633-635
    • Khosla, C.1    Bailey, J.E.2
  • 16
    • 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
  • 17
    • 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., De Modena J.A., Curtis J.E., Bailey J.E., Galazzo J.A., Hughes D.E. Actinorhodin production by Streptomyces coelicolor and growth of Streptomyces lividans are improved by the expression of a bacterial hemoglobin. Biotechnology. 9:1991;473-476.
    • (1991) Biotechnology , vol.9 , pp. 473-476
    • Magnolo, S.K.1    Leenutaphong, D.L.2    De Modena, J.A.3    Curtis, J.E.4    Bailey, J.E.5    Galazzo, J.A.6    Hughes, D.E.7
  • 18
    • 0024215242 scopus 로고
    • An Escherichia coli vector to express and purify foreign proteins by fusion to and separation from maltose-binding protein
    • Maina C.V., Riggs P.D., Grandea A.G., Slatko B.E., Moran L.S., Tagliamonte J.A., McReynolds L.A., Guan C.D. An Escherichia coli vector to express and purify foreign proteins by fusion to and separation from maltose-binding protein. Gene. 74:1988;365-373.
    • (1988) Gene , vol.74 , pp. 365-373
    • Maina, C.V.1    Riggs, P.D.2    Grandea, A.G.3    Slatko, B.E.4    Moran, L.S.5    Tagliamonte, J.A.6    McReynolds, L.A.7    Guan, C.D.8
  • 19
    • 0034723151 scopus 로고    scopus 로고
    • Selection of amino acid substitutions restoring activity of HIV-1 integrase mutated in its catalytic site using the yeast Saccharomyces cerevisiae
    • Parissi V., Caumont A.B., de Soultrait V.R., Calmels C., Pichuantes S., Litvak S., Dupont C.H. Selection of amino acid substitutions restoring activity of HIV-1 integrase mutated in its catalytic site using the yeast Saccharomyces cerevisiae. J. Mol. Biol. 295:2000;755-765.
    • (2000) J. Mol. Biol. , vol.295 , pp. 755-765
    • Parissi, V.1    Caumont, A.B.2    De Soultrait, V.R.3    Calmels, C.4    Pichuantes, S.5    Litvak, S.6    Dupont, C.H.7
  • 20
    • 0037031866 scopus 로고    scopus 로고
    • Vitreoscilla hemoglobin binds to subunit I of cytochrome bo ubiquinol oxidases
    • Park K.W., Kim K.J., Howard A.J., Stark B.C., Webster D.A. Vitreoscilla hemoglobin binds to subunit I of cytochrome bo ubiquinol oxidases. J. Biol. Chem. 277:2002;33334-33337.
    • (2002) J. Biol. Chem. , vol.277 , pp. 33334-33337
    • Park, K.W.1    Kim, K.J.2    Howard, A.J.3    Stark, B.C.4    Webster, D.A.5
  • 21
    • 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
  • 22
    • 0021886339 scopus 로고
    • Bacterial expression and characterization of proteins derived from the chicken calmodulin cDNA and a calmodulin processed gene
    • Putkey J.A., Slaughter G.R., Means A.R. Bacterial expression and characterization of proteins derived from the chicken calmodulin cDNA and a calmodulin processed gene. J. Biol. Chem. 260:1985;4704-4712.
    • (1985) J. Biol. Chem. , vol.260 , pp. 4704-4712
    • Putkey, J.A.1    Slaughter, G.R.2    Means, A.R.3
  • 24
    • 0025366844 scopus 로고
    • Human immunodeficiency virus integration protein expressed in Escherichia coli possesses selective DNA cleaving activity
    • Sherman P.A., Fyfe J.A. Human immunodeficiency virus integration protein expressed in Escherichia coli possesses selective DNA cleaving activity. Proc. Natl. Acad. Sci. USA. 87:1990;5119-5123.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5119-5123
    • Sherman, P.A.1    Fyfe, J.A.2
  • 25
    • 0023806075 scopus 로고
    • Single step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith D.B., Johnson K.S. Single step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene. 67:1988;31-34.
    • (1988) Gene , vol.67 , pp. 31-34
    • Smith, D.B.1    Johnson, K.S.2
  • 26
    • 0039353330 scopus 로고
    • Chicken triosephosphate isomerase complements an Escherichia coli deficiency
    • Straus D., Gilbert W. Chicken triosephosphate isomerase complements an Escherichia coli deficiency. Proc. Natl. Acad. Sci. USA. 82:1985;2014-2018.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 2014-2018
    • Straus, D.1    Gilbert, W.2
  • 28
    • 0030051960 scopus 로고
    • Effect of Vitreoscilla hemoglobin dosage on microaerobic Escherichia coli carbon and energy metabolism
    • Tsai P.S., Hatzimamikatis V., Bailey I.E. Effect of Vitreoscilla hemoglobin dosage on microaerobic Escherichia coli carbon and energy metabolism. Biotechnol. Bioeng. 49:1995;139-150.
    • (1995) Biotechnol. Bioeng. , vol.49 , pp. 139-150
    • Tsai, P.S.1    Hatzimamikatis, V.2    Bailey, I.E.3
  • 29
    • 0030034536 scopus 로고
    • Intracellular expression of Vitreoscilla hemoglobin modifies microaerobic Escherichia coli metabolism through elevated concentration and specific activity of cytochrome o
    • Tsai P.S., Nagely M., Bailey J.E. Intracellular expression of Vitreoscilla hemoglobin modifies microaerobic Escherichia coli metabolism through elevated concentration and specific activity of cytochrome o. Biotechnol. Bioeng. 49:1995;151-160.
    • (1995) Biotechnol. Bioeng. , vol.49 , pp. 151-160
    • Tsai, P.S.1    Nagely, M.2    Bailey, J.E.3
  • 30
    • 0016192420 scopus 로고
    • Reduced nicotinamide adenine dinucleotide cytochrome o reductase associated with cytochrome o purified from Vitreoscilla
    • Webster D.A., Liu C.Y. Reduced nicotinamide adenine dinucleotide cytochrome o reductase associated with cytochrome o purified from Vitreoscilla. J. Biol. Chem. 249:1974;4257-4260.
    • (1974) J. Biol. Chem. , vol.249 , pp. 4257-4260
    • Webster, D.A.1    Liu, C.Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.