메뉴 건너뛰기




Volumn 34, Issue 1, 2004, Pages 118-125

Selection of an Escherichia coli host that expresses mutant forms of Mycobacterium tuberculosis 2-trans enoyl-ACP(CoA) reductase and 3-ketoacyl-ACP(CoA) reductase enzymes

Author keywords

Escherichia coli; Host selection; Mycobacteria; Protein expression

Indexed keywords

CORYNEBACTERINEAE; ESCHERICHIA COLI; MYCOBACTERIUM; MYCOBACTERIUM TUBERCULOSIS;

EID: 1442289348     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2003.10.009     Document Type: Article
Times cited : (6)

References (37)
  • 1
    • 0038182191 scopus 로고    scopus 로고
    • The TB epidemic from 1992 to 2002
    • M.C. Raviglione, The TB epidemic from 1992 to 2002, Tuberculosis 83 (2003) 4-14.
    • (2003) Tuberculosis , vol.83 , pp. 4-14
    • Raviglione, M.C.1
  • 2
    • 0026686943 scopus 로고
    • Tuberculosis: Commentary on a reemergent killer
    • B.R. Bloom, C.J.L. Murray, Tuberculosis: commentary on a reemergent killer, Science 257 (1992) 1055-1064.
    • (1992) Science , vol.257 , pp. 1055-1064
    • Bloom, B.R.1    Murray, C.J.L.2
  • 4
    • 0036273794 scopus 로고    scopus 로고
    • Controlling multidrug-resistant tuberculosis and access to expensive drugs: A rational framework
    • A. Plabos-Méndez, D.K. Gowda, T.R. Frieden, Controlling multidrug-resistant tuberculosis and access to expensive drugs: a rational framework, Bull. World Health Org. 80 (2002) 489-495.
    • (2002) Bull. World Health Org. , vol.80 , pp. 489-495
    • Plabos-Méndez, A.1    Gowda, D.K.2    Frieden, T.R.3
  • 7
    • 0035936760 scopus 로고    scopus 로고
    • Microbial pathogenesis of Mycobacterium tuberculosis: Dawn of a discipline
    • M.S. Glickman, W.R. Jacobs Jr., Microbial pathogenesis of Mycobacterium tuberculosis: dawn of a discipline, Cell 104 (2001) 477-485.
    • (2001) Cell , vol.104 , pp. 477-485
    • Glickman, M.S.1    Jacobs Jr., W.R.2
  • 8
    • 0028836762 scopus 로고
    • Molecular biology, virulence, and pathogenicity of mycobacteria
    • T.M. Shinnick, C.H. King, F.D. Quinn, Molecular biology, virulence, and pathogenicity of mycobacteria, Am. J. Med. Sci. 309 (1995) 92-98.
    • (1995) Am. J. Med. Sci. , vol.309 , pp. 92-98
    • Shinnick, T.M.1    King, C.H.2    Quinn, F.D.3
  • 9
    • 0032884573 scopus 로고    scopus 로고
    • Recombinant protein expression in Escherichia coli
    • F. Baneyx, Recombinant protein expression in Escherichia coli, Curr. Opin. Biotechnol. 10 (1999) 411-421.
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 411-421
    • Baneyx, F.1
  • 10
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • F.W. Studier, B.A. Moffat, Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes, J. Mol. Biol. 189 (1986) 113-130.
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffat, B.A.2
  • 12
    • 0035902542 scopus 로고    scopus 로고
    • Purine nucleoside phosphorylase from Mycobacterium tuberculosis analysis of inhibition by a transition-state analogue and dissection by parts
    • L.A. Basso, D.S. Santos, W. Shi, R.H. Furneaux, P.C. Tyler, V.L. Schramm, J.S. Blanchard, Purine nucleoside phosphorylase from Mycobacterium tuberculosis analysis of inhibition by a transition-state analogue and dissection by parts, Biochemistry 28 (2001) 8196-8203.
    • (2001) Biochemistry , vol.28 , pp. 8196-8203
    • Basso, L.A.1    Santos, D.S.2    Shi, W.3    Furneaux, R.H.4    Tyler, P.C.5    Schramm, V.L.6    Blanchard, J.S.7
  • 13
    • 0034889953 scopus 로고    scopus 로고
    • Cloning and overexpression in soluble form of functional shikimate kinase and 5-enolpyruvylshikimate 3-phosphate synthase enzymes from Mycobacterium tuberculosis
    • J.S. Oliveira, C.A. Pinto, L.A. Basso, D.S. Santos, Cloning and overexpression in soluble form of functional shikimate kinase and 5-enolpyruvylshikimate 3-phosphate synthase enzymes from Mycobacterium tuberculosis, Protein Express. Purif. 3 (2001) 430-435.
    • (2001) Protein Express. Purif. , vol.3 , pp. 430-435
    • Oliveira, J.S.1    Pinto, C.A.2    Basso, L.A.3    Santos, D.S.4
  • 14
    • 0035902502 scopus 로고    scopus 로고
    • Structures of purine nucleoside phosphorylase from Mycobacterium tuberculosis in complex with immucillin-H and its pieces
    • W. Shi, L.A. Basso, D.S. Santos, P.C. Tyler, R.H. Furneaux, J.S. Blanchard, S.C. Almo, V.L. Schramm, Structures of purine nucleoside phosphorylase from Mycobacterium tuberculosis in complex with immucillin-H and its pieces, Biochemistry 28 (2001) 8204-8215.
    • (2001) Biochemistry , vol.28 , pp. 8204-8215
    • Shi, W.1    Basso, L.A.2    Santos, D.S.3    Tyler, P.C.4    Furneaux, R.H.5    Blanchard, J.S.6    Almo, S.C.7    Schramm, V.L.8
  • 15
    • 0035958944 scopus 로고    scopus 로고
    • Biochemical characterization of acyl carrier protein (AcpM) and malonyl-CoA:AcpM transacylase (mtFabD), two major components of Mycobacterium tuberculosis fatty acid synthase
    • L. Kremer, K.M. Nampoothiri, S. Lesjean, L.G. Dover, S. Graham, J. Betts, P.J. Brennan, D.E. Minnikin, C. Locht, G.S. Besra, Biochemical characterization of acyl carrier protein (AcpM) and malonyl-CoA:AcpM transacylase (mtFabD), two major components of Mycobacterium tuberculosis fatty acid synthase, J. Biol. Chem. 276 (2001) 27967-27974.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27967-27974
    • Kremer, L.1    Nampoothiri, K.M.2    Lesjean, S.3    Dover, L.G.4    Graham, S.5    Betts, J.6    Brennan, P.J.7    Minnikin, D.E.8    Locht, C.9    Besra, G.S.10
  • 16
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant host that allow synthesis of some membrane proteins and globular proteins at high levels
    • B. Miroux, J.E. Walker, Over-production of proteins in Escherichia coli: mutant host that allow synthesis of some membrane proteins and globular proteins at high levels, J. Mol. Biol. 260 (1996) 289-298.
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 20
    • 0031733687 scopus 로고    scopus 로고
    • The maba gene from the inha operon of Mycobacterium tuberculosis encodes a 3-ketoacyl reductase that fails to confer isoniazid resistance
    • A. Banerjee, M. Sugantino, J.C. Sacchettini, W.R. Jacobs Jr., The mabA gene from the inhA operon of Mycobacterium tuberculosis encodes a 3-ketoacyl reductase that fails to confer isoniazid resistance, Microbiology 144 (1998) 2697-2704.
    • (1998) Microbiology , vol.144 , pp. 2697-2704
    • Banerjee, A.1    Sugantino, M.2    Sacchettini, J.C.3    Jacobs Jr., W.R.4
  • 21
    • 0037844364 scopus 로고    scopus 로고
    • Structure, function, and biogenesis of the cell wall of Mycobacterium tuberculosis
    • P.J. Brennan, Structure, function, and biogenesis of the cell wall of Mycobacterium tuberculosis, Tuberculosis 83 (2003) 91-97.
    • (2003) Tuberculosis , vol.83 , pp. 91-97
    • Brennan, P.J.1
  • 23
    • 0033550048 scopus 로고    scopus 로고
    • Roles of tyrosine 158 and lysine 165 in the catalytic mechanism of InhA, the enoyl-ACP reductase from Mycobacterium tuberculosis
    • S. Parikh, D.P. Moynihan, G. Xiao, P.J. Tonge, Roles of tyrosine 158 and lysine 165 in the catalytic mechanism of InhA, the enoyl-ACP reductase from Mycobacterium tuberculosis, Biochemistry 38 (1999) 13623-13634.
    • (1999) Biochemistry , vol.38 , pp. 13623-13634
    • Parikh, S.1    Moynihan, D.P.2    Xiao, G.3    Tonge, P.J.4
  • 24
    • 0037324955 scopus 로고    scopus 로고
    • Coenzyme-based functional assignments of short-chain dehydrogenases/ reductases (SDRs) family
    • B. Persson, Y. Kallberg, U. Oppermann, H. Jörnvall, Coenzyme-based functional assignments of short-chain dehydrogenases/reductases (SDRs) family, Chem. Biol. Interact. 143-144 (2003) 271-278.
    • (2003) Chem. Biol. Interact. , vol.143-144 , pp. 271-278
    • Persson, B.1    Kallberg, Y.2    Oppermann, U.3    Jörnvall, H.4
  • 25
    • 0034048280 scopus 로고    scopus 로고
    • Overexpression and purification of the Escherichia coli inner membrane enzyme acyl acyl carrier protein synthase in an active form
    • J. Shanklin, Overexpression and purification of the Escherichia coli inner membrane enzyme acyl acyl carrier protein synthase in an active form, Protein Express. Purif. 18 (2000) 355-360.
    • (2000) Protein Express. Purif. , vol.18 , pp. 355-360
    • Shanklin, J.1
  • 26
    • 0024520745 scopus 로고
    • Site directed mutagenesis by overlap extension using the polymerase chain reaction
    • S.N. Ho, H.D. Hunt, R.M. Horton, J.K. Pullen, L.R. Pease, Site directed mutagenesis by overlap extension using the polymerase chain reaction, Gene 77 (1989) 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 29
    • 0028893947 scopus 로고
    • Visual detection method for identifying recombinant bacterial colonies
    • R.C. Austin, D. Singh, P.C.Y. Liaw, H.J. Craig, Visual detection method for identifying recombinant bacterial colonies, Bio.Techniques 18 (1995) 380-384.
    • (1995) Bio.Techniques , vol.18 , pp. 380-384
    • Austin, R.C.1    Singh, D.2    Liaw, P.C.Y.3    Craig, H.J.4
  • 30
    • 0031023683 scopus 로고    scopus 로고
    • Relationship between opacity of transformed E. coli colonies and over-expression of the recombinant transcript
    • S. Barik, Relationship between opacity of transformed E. coli colonies and over-expression of the recombinant transcript, BioTechniques 22 (1997) 112-118.
    • (1997) BioTechniques , vol.22 , pp. 112-118
    • Barik, S.1
  • 31
    • 0028907619 scopus 로고
    • Gratuitous overexpression of genes in Escherichia coli leads to growth, inhibition and ribosome destruction
    • H. Dong, L. Nilsson, C.G. Kurland, Gratuitous overexpression of genes in Escherichia coli leads to growth, inhibition and ribosome destruction, J. Bacteriol. 177 (1995) 1497-1504.
    • (1995) J. Bacteriol. , vol.177 , pp. 1497-1504
    • Dong, H.1    Nilsson, L.2    Kurland, C.G.3
  • 32
    • 0032536841 scopus 로고    scopus 로고
    • Spontaneous cAMP-dependent derepression of gene expression in stationary phase plays a role in recombinant expression instability
    • T.H. Grossman, E.S. Kawasaki, S.P. Punreddy, M.S. Osburne, Spontaneous cAMP-dependent derepression of gene expression in stationary phase plays a role in recombinant expression instability, Gene 209 (1998) 95-103.
    • (1998) Gene , vol.209 , pp. 95-103
    • Grossman, T.H.1    Kawasaki, E.S.2    Punreddy, S.P.3    Osburne, M.S.4
  • 34
    • 0037061460 scopus 로고    scopus 로고
    • A 'periodic table' for protein structures
    • W.R.A. Taylor, A 'periodic table' for protein structures, Nature 415 (2002) 657-660.
    • (2002) Nature , vol.415 , pp. 657-660
    • Taylor, W.R.A.1
  • 36
    • 0032007853 scopus 로고    scopus 로고
    • Strategies for optimizing heterologous protein expression in E. coli
    • G. Hannig, S.C. Makrides, Strategies for optimizing heterologous protein expression in E. coli, Trends Biotechnol. 16 (1998) 54-60.
    • (1998) Trends Biotechnol. , vol.16 , pp. 54-60
    • Hannig, G.1    Makrides, S.C.2
  • 37
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • S.C. Makrides, Strategies for achieving high-level expression of genes in Escherichia coli, Microbiol. Rev. 60 (1996) 512-538.
    • (1996) Microbiol. Rev. , vol.60 , pp. 512-538
    • Makrides, S.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.