메뉴 건너뛰기




Volumn 38, Issue 1, 2004, Pages 69-78

BgK, a disulfide-containing sea anemone toxin blocking K + channels, can be produced in Escherichia coli cytoplasm as a functional tagged protein

Author keywords

Cytoplasmic production; Disulfide; Potassium channel; Sea anemone toxin

Indexed keywords

COELENTERATE VENOM; POTASSIUM CHANNEL BLOCKING AGENT; RECOMBINANT PROTEIN; TOXIN BGK;

EID: 5344279151     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2004.07.011     Document Type: Article
Times cited : (8)

References (43)
  • 2
    • 33747646924 scopus 로고    scopus 로고
    • An overview of the potassium channel family
    • C. Miller An overview of the potassium channel family Genome Biol. 1 2000 REVIEWS0004
    • (2000) Genome Biol. , vol.1
    • Miller, C.1
  • 3
    • 0033178906 scopus 로고    scopus 로고
    • Pharmacology of voltage-gated and calcium-activated potassium channels
    • G.J. Kaczorowski, and M.L. Garcia Pharmacology of voltage-gated and calcium-activated potassium channels Curr. Opin. Chem. Biol. 3 1999 448 458
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 448-458
    • Kaczorowski, G.J.1    Garcia, M.L.2
  • 4
    • 0035184148 scopus 로고    scopus 로고
    • Potassium channels: From scorpion venoms to high-resolution structure
    • M.L. Garcia, Y. Gao, O.B. McManus, and G.J. Kaczorowski Potassium channels: from scorpion venoms to high-resolution structure Toxicon 39 2001 739 748
    • (2001) Toxicon , vol.39 , pp. 739-748
    • Garcia, M.L.1    Gao, Y.2    McManus, O.B.3    Kaczorowski, G.J.4
  • 5
    • 0242331757 scopus 로고    scopus 로고
    • Therapeutic potential of venom peptides
    • R.J. Lewis, and M.L. Garcia Therapeutic potential of venom peptides Nat. Rev. Drug Discov. 2 2003 790 802
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 790-802
    • Lewis, R.J.1    Garcia, M.L.2
  • 6
    • 8044235836 scopus 로고    scopus 로고
    • A potassium-channel toxin from the sea anemone Bunodosoma granulifera, an inhibitor for Kv1 channels. Revision of the amino acid sequence, disulfide-bridge assignment, chemical synthesis, and biological activity
    • J. Cotton, M. Crest, F. Bouet, N. Alessandri, M. Gola, E. Forest, E. Karlsson, O. Castaneda, A.L. Harvey, C. Vita, and A. Menez A potassium-channel toxin from the sea anemone Bunodosoma granulifera, an inhibitor for Kv1 channels. Revision of the amino acid sequence, disulfide-bridge assignment, chemical synthesis, and biological activity Eur. J. Biochem. 244 1997 192 202
    • (1997) Eur. J. Biochem. , vol.244 , pp. 192-202
    • Cotton, J.1    Crest, M.2    Bouet, F.3    Alessandri, N.4    Gola, M.5    Forest, E.6    Karlsson, E.7    Castaneda, O.8    Harvey, A.L.9    Vita, C.10    Menez, A.11
  • 7
    • 0037040249 scopus 로고    scopus 로고
    • Characterization of a novel radiolabeled peptide selective for a subpopulation of voltage-gated potassium channels in mammalian brain
    • J. Racape, A. Lecoq, R. Romi-Lebrun, J. Liu, M. Kohler, M.L. Garcia, A. Menez, and S. Gasparini Characterization of a novel radiolabeled peptide selective for a subpopulation of voltage-gated potassium channels in mammalian brain J. Biol. Chem. 277 2002 3886 3893
    • (2002) J. Biol. Chem. , vol.277 , pp. 3886-3893
    • Racape, J.1    Lecoq, A.2    Romi-Lebrun, R.3    Liu, J.4    Kohler, M.5    Garcia, M.L.6    Menez, A.7    Gasparini, S.8
  • 9
    • 0037020077 scopus 로고    scopus 로고
    • Structure of the BgK-Kv1.1 complex based on distance restraints identified by double mutant cycles. Molecular basis for convergent evolution of Kv1 channel blockers
    • B. Gilquin, J. Racape, A. Wrisch, V. Visan, A. Lecoq, S. Grissmer, A. Menez, and S. Gasparini Structure of the BgK-Kv1.1 complex based on distance restraints identified by double mutant cycles. Molecular basis for convergent evolution of Kv1 channel blockers J. Biol. Chem. 277 2002 37406 37413
    • (2002) J. Biol. Chem. , vol.277 , pp. 37406-37413
    • Gilquin, B.1    Racape, J.2    Wrisch, A.3    Visan, V.4    Lecoq, A.5    Grissmer, S.6    Menez, A.7    Gasparini, S.8
  • 11
    • 0033598777 scopus 로고    scopus 로고
    • Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
    • P.H. Bessette, F. Aslund, J. Beckwith, and G. Georgiou Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm Proc. Natl. Acad. Sci. USA 96 1999 13703 13708
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13703-13708
    • Bessette, P.H.1    Aslund, F.2    Beckwith, J.3    Georgiou, G.4
  • 12
    • 0034966491 scopus 로고    scopus 로고
    • Accurate disulfide formation in Escherichia coli: Overexpression and characterization of the first domain (HF6478) of the multiple Kazal-type inhibitor LEKTI
    • T. Lauber, U.C. Marx, A. Schulz, P. Kreutzmann, P. Rosch, and S. Hoffmann Accurate disulfide formation in Escherichia coli: overexpression and characterization of the first domain (HF6478) of the multiple Kazal-type inhibitor LEKTI Protein Express. Purif. 22 2001 108 112
    • (2001) Protein Express. Purif. , vol.22 , pp. 108-112
    • Lauber, T.1    Marx, U.C.2    Schulz, A.3    Kreutzmann, P.4    Rosch, P.5    Hoffmann, S.6
  • 13
    • 0142245696 scopus 로고    scopus 로고
    • High-yield expression in Escherichia coli, purification, and characterization of properly folded major peanut allergen Ara h 2
    • K. Lehmann, S. Hoffmann, P. Neudecker, M. Suhr, W.M. Becker, and P. Rosch High-yield expression in Escherichia coli, purification, and characterization of properly folded major peanut allergen Ara h 2 Protein Express. Purif. 31 2003 250 259
    • (2003) Protein Express. Purif. , vol.31 , pp. 250-259
    • Lehmann, K.1    Hoffmann, S.2    Neudecker, P.3    Suhr, M.4    Becker, W.M.5    Rosch, P.6
  • 14
    • 0027512825 scopus 로고
    • Ribonuclease S-peptide as a carrier in fusion proteins
    • J.S. Kim, and R.T. Raines Ribonuclease S-peptide as a carrier in fusion proteins Protein Sci. 2 1993 348 356
    • (1993) Protein Sci. , vol.2 , pp. 348-356
    • Kim, J.S.1    Raines, R.T.2
  • 16
    • 84862428017 scopus 로고    scopus 로고
    • Phosphatase alcalines bactériennes modifiées et leurs applications, French Patent Application 95.07833 (1995)
    • J.C. Boulain, L. Cattolico, F. Ducancel, A. Ménez, Phosphatase alcalines bactériennes modifiées et leurs applications, French Patent Application 95.07833 (1995)
    • Boulain, J.C.1    Cattolico, L.2    Ducancel, F.3    Ménez, A.4
  • 17
    • 0031860811 scopus 로고    scopus 로고
    • Chaperone coexpression plasmids: Differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escherichia coli
    • K. Nishihara, M. Kanemori, M. Kitagawa, H. Yanagi, and T. Yura Chaperone coexpression plasmids: differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escherichia coli Appl. Environ. Microbiol. 64 1998 1694 1699
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 1694-1699
    • Nishihara, K.1    Kanemori, M.2    Kitagawa, M.3    Yanagi, H.4    Yura, T.5
  • 19
    • 0027050148 scopus 로고
    • Recursive PCR: A novel technique for total gene synthesis
    • C. Prodromou, and L.H. Pearl Recursive PCR: a novel technique for total gene synthesis Protein Eng. 5 1992 827 829
    • (1992) Protein Eng. , vol.5 , pp. 827-829
    • Prodromou, C.1    Pearl, L.H.2
  • 21
    • 0041888478 scopus 로고    scopus 로고
    • Ionworks HT: A new high-throughput electrophysiology measurement platform
    • K. Schroeder, B. Neagle, D.J. Trezise, and J. Worley Ionworks HT: a new high-throughput electrophysiology measurement platform J. Biomol. Screen. 8 2003 50 64
    • (2003) J. Biomol. Screen. , vol.8 , pp. 50-64
    • Schroeder, K.1    Neagle, B.2    Trezise, D.J.3    Worley, J.4
  • 22
    • 0030893407 scopus 로고    scopus 로고
    • Protein folding in the bacterial periplasm
    • D. Missiakas, and S. Raina Protein folding in the bacterial periplasm J. Bacteriol. 179 1997 2465 2471
    • (1997) J. Bacteriol. , vol.179 , pp. 2465-2471
    • Missiakas, D.1    Raina, S.2
  • 24
    • 0032552974 scopus 로고    scopus 로고
    • A snake toxin inhibitor of inward rectifier potassium channel ROMK1
    • J.P. Imredy, C. Chen, and R. MacKinnon A snake toxin inhibitor of inward rectifier potassium channel ROMK1 Biochemistry 37 1998 14867 14874
    • (1998) Biochemistry , vol.37 , pp. 14867-14874
    • Imredy, J.P.1    Chen, C.2    MacKinnon, R.3
  • 25
    • 0028172049 scopus 로고
    • On the site by which alpha-dendrotoxin binds to voltage-dependent potassium channels: Site-directed mutagenesis reveals that the lysine triplet 28-30 is not essential for binding
    • J.M. Danse, E.G. Rowan, S. Gasparini, F. Ducancel, H. Vatanpour, L.C. Young, G. Poorheidari, E. Lajeunesse, P. Drevet, and R. Menez On the site by which alpha-dendrotoxin binds to voltage-dependent potassium channels: site-directed mutagenesis reveals that the lysine triplet 28-30 is not essential for binding FEBS Lett. 356 1994 153 158
    • (1994) FEBS Lett. , vol.356 , pp. 153-158
    • Danse, J.M.1    Rowan, E.G.2    Gasparini, S.3    Ducancel, F.4    Vatanpour, H.5    Young, L.C.6    Poorheidari, G.7    Lajeunesse, E.8    Drevet, P.9    Menez, R.10
  • 28
    • 0026606397 scopus 로고
    • Insertion of a disulfide-containing neurotoxin into E. coli alkaline phosphatase: The hybrid retains both biological activities
    • D. Gillet, F. Ducancel, E. Pradel, M. Leonetti, A. Menez, and J.C. Boulain Insertion of a disulfide-containing neurotoxin into E. coli alkaline phosphatase: the hybrid retains both biological activities Protein Eng. 5 1992 273 278
    • (1992) Protein Eng. , vol.5 , pp. 273-278
    • Gillet, D.1    Ducancel, F.2    Pradel, E.3    Leonetti, M.4    Menez, A.5    Boulain, J.C.6
  • 30
    • 0030941829 scopus 로고    scopus 로고
    • The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm
    • W.A. Prinz, F. Aslund, A. Holmgren, and J. Beckwith The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm J. Biol. Chem. 272 1997 15661 15667
    • (1997) J. Biol. Chem. , vol.272 , pp. 15661-15667
    • Prinz, W.A.1    Aslund, F.2    Holmgren, A.3    Beckwith, J.4
  • 31
    • 0030978089 scopus 로고    scopus 로고
    • Manipulating the aggregation and oxidation of human SPARC in the cytoplasm of Escherichia coli
    • E.L. Schneider, J.G. Thomas, J.A. Bassuk, E.H. Sage, and F. Baneyx Manipulating the aggregation and oxidation of human SPARC in the cytoplasm of Escherichia coli Nat. Bio/Technol. 15 1997 581 585
    • (1997) Nat. Bio/Technol. , vol.15 , pp. 581-585
    • Schneider, E.L.1    Thomas, J.G.2    Bassuk, J.A.3    Sage, E.H.4    Baneyx, F.5
  • 32
    • 0030885670 scopus 로고    scopus 로고
    • A new potassium channel toxin from the sea anemone Heteractis magnifica: Isolation, cDNA cloning, and functional expression
    • G.S. Gendeh, L.C. Young, C.L. de Medeiros, K. Jeyaseelan, A.L. Harvey, and M.C. Chung A new potassium channel toxin from the sea anemone Heteractis magnifica: isolation, cDNA cloning, and functional expression Biochemistry 36 1997 11461 11471
    • (1997) Biochemistry , vol.36 , pp. 11461-11471
    • Gendeh, G.S.1    Young, L.C.2    De Medeiros, C.L.3    Jeyaseelan, K.4    Harvey, A.L.5    Chung, M.C.6
  • 33
    • 0035854663 scopus 로고    scopus 로고
    • Functional significance of the beta hairpin in the insecticidal neurotoxin omega-atracotoxin-Hv1a
    • H.W. Tedford, J.I. Fletcher, and G.F. King Functional significance of the beta hairpin in the insecticidal neurotoxin omega-atracotoxin-Hv1a J. Biol. Chem. 276 2001 26568 26576
    • (2001) J. Biol. Chem. , vol.276 , pp. 26568-26576
    • Tedford, H.W.1    Fletcher, J.I.2    King, G.F.3
  • 36
    • 0036296338 scopus 로고    scopus 로고
    • Production of functional single-chain Fv antibodies in the cytoplasm of Escherichia coli
    • P. Jurado, D. Ritz, J. Beckwith, V. de Lorenzo, and L.A. Fernandez Production of functional single-chain Fv antibodies in the cytoplasm of Escherichia coli J. Mol. Biol. 320 2002 1 10
    • (2002) J. Mol. Biol. , vol.320 , pp. 1-10
    • Jurado, P.1    Ritz, D.2    Beckwith, J.3    De Lorenzo, V.4    Fernandez, L.A.5
  • 37
    • 0034756555 scopus 로고    scopus 로고
    • Production of correctly folded Fab antibody fragment in the cytoplasm of Escherichia coli trxB gor mutants via the coexpression of molecular chaperones
    • R. Levy, R. Weiss, G. Chen, B.L. Iverson, and G. Georgiou Production of correctly folded Fab antibody fragment in the cytoplasm of Escherichia coli trxB gor mutants via the coexpression of molecular chaperones Protein Express. Purif. 23 2001 338 347
    • (2001) Protein Express. Purif. , vol.23 , pp. 338-347
    • Levy, R.1    Weiss, R.2    Chen, G.3    Iverson, B.L.4    Georgiou, G.5
  • 38
    • 0346935999 scopus 로고    scopus 로고
    • DnaK and DnaJ facilitated the folding process and reduced inclusion body formation of magnesium transporter CorA overexpressed in Escherichia coli
    • Y. Chen, J. Song, S.F. Sui, and D.N. Wang DnaK and DnaJ facilitated the folding process and reduced inclusion body formation of magnesium transporter CorA overexpressed in Escherichia coli Protein Express. Purif. 32 2003 221 231
    • (2003) Protein Express. Purif. , vol.32 , pp. 221-231
    • Chen, Y.1    Song, J.2    Sui, S.F.3    Wang, D.N.4
  • 39
    • 0036406990 scopus 로고    scopus 로고
    • Chaperonin GroESL mediates the protein folding of human liver mitochondrial aldehyde dehydrogenase in Escherichia coli
    • K.H. Lee, H.S. Kim, H.S. Jeong, and Y.S. Lee Chaperonin GroESL mediates the protein folding of human liver mitochondrial aldehyde dehydrogenase in Escherichia coli Biochem. Biophys. Res. Commun. 298 2002 216 224
    • (2002) Biochem. Biophys. Res. Commun. , vol.298 , pp. 216-224
    • Lee, K.H.1    Kim, H.S.2    Jeong, H.S.3    Lee, Y.S.4
  • 40
    • 0042768090 scopus 로고    scopus 로고
    • Protein disulfide bond formation in prokaryotes
    • H. Kadokura, F. Katzen, and J. Beckwith Protein disulfide bond formation in prokaryotes Annu. Rev. Biochem. 72 2003 111 135
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 111-135
    • Kadokura, H.1    Katzen, F.2    Beckwith, J.3
  • 41
    • 0024536385 scopus 로고
    • Identification of C-terminal extensions that protect proteins from intracellular proteolysis
    • J.U. Bowie, and R.T. Sauer Identification of C-terminal extensions that protect proteins from intracellular proteolysis J. Biol. Chem. 264 1989 7596 7602
    • (1989) J. Biol. Chem. , vol.264 , pp. 7596-7602
    • Bowie, J.U.1    Sauer, R.T.2
  • 42
    • 0024554228 scopus 로고
    • The structural stability of a protein is an important determinant of its proteolytic susceptibility in Escherichia coli
    • D.A. Parsell, and R.T. Sauer The structural stability of a protein is an important determinant of its proteolytic susceptibility in Escherichia coli J. Biol. Chem. 264 1989 7590 7595
    • (1989) J. Biol. Chem. , vol.264 , pp. 7590-7595
    • Parsell, D.A.1    Sauer, R.T.2
  • 43
    • 0035254933 scopus 로고    scopus 로고
    • Stabilizing C-terminal tails on AraC
    • M. Ghosh, and R.F. Schleif Stabilizing C-terminal tails on AraC Proteins 42 2001 177 181
    • (2001) Proteins , vol.42 , pp. 177-181
    • Ghosh, M.1    Schleif, R.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.