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Volumn 9, Issue 1, 2014, Pages

Recombinant production of the amino terminal cytoplasmic region of dengue virus non-structural protein 4A for structural studies

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; ESCHERICHIA COLI PROTEIN; GLUTAMIC ACID; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; LEUCINE; METHIONINE; MUTANT PROTEIN; NONSTRUCTURAL PROTEIN 4A; PEPTIDE DERIVATIVE; PROTEIN GB1; PROTEINASE; SYNTHETIC DNA; UNCLASSIFIED DRUG;

EID: 84899813573     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0086482     Document Type: Article
Times cited : (7)

References (40)
  • 2
    • 33751254102 scopus 로고    scopus 로고
    • Recent advances in deciphering viral and host determinants of dengue virus replication and pathogenesis
    • DOI 10.1128/JVI.01257-06
    • Clyde K, Kyle JL, Harris E (2006) Recent advances in deciphering viral and host determinants of dengue virus replication and pathogenesis. J Virol 80: 11418-11431. (Pubitemid 44788858)
    • (2006) Journal of Virology , vol.80 , Issue.23 , pp. 11418-11431
    • Clyde, K.1    Kyle, J.L.2    Harris, E.3
  • 3
    • 34247848008 scopus 로고    scopus 로고
    • The non-structural protein 4A of dengue virus is an integral membrane protein inducing membrane alterations in a 2K-regulated manner
    • DOI 10.1074/jbc.M609919200
    • Miller S, Kastner S, Krijnse-Locker J, Buhler S, Bartenschlager R (2007) The non-structural protein 4A of dengue virus is an integral membrane protein inducing membrane alterations in a 2K-regulated manner. J Biol Chem 282: 8873-8882. (Pubitemid 47093477)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.12 , pp. 8873-8882
    • Miller, S.1    Kastner, S.2    Krijnse-Locker, J.3    Buhler, S.4    Bartenschlager, R.5
  • 4
    • 0032486487 scopus 로고    scopus 로고
    • Subcellular localization and some biochemical properties of the flavivirus Kunjin nonstructural proteins NS2A and NS4A
    • DOI 10.1006/viro.1998.9156
    • Mackenzie JM, Khromykh AA, Jones MK, Westaway EG (1998) Subcellular localization and some biochemical properties of the flavivirus Kunjin nonstructural proteins NS2A and NS4A. Virology 245: 203-215. (Pubitemid 28394183)
    • (1998) Virology , vol.245 , Issue.2 , pp. 203-215
    • MacKenzie, J.M.1    Khromykh, A.A.2    Jones, M.K.3    Westaway, E.G.4
  • 5
    • 33646167045 scopus 로고    scopus 로고
    • Regulated cleavages at the West Nile virus NS4A-2K-NS4B junctions play a major role in rearranging cytoplasmic membranes and Golgi trafficking of the NS4A protein
    • Roosendaal J, Westaway EG, Khromykh A, Mackenzie JM (2006) Regulated cleavages at the West Nile virus NS4A-2K-NS4B junctions play a major role in rearranging cytoplasmic membranes and Golgi trafficking of the NS4A protein. J Virol 80: 4623-4632.
    • (2006) J Virol , vol.80 , pp. 4623-4632
    • Roosendaal, J.1    Westaway, E.G.2    Khromykh, A.3    Mackenzie, J.M.4
  • 6
    • 84875504620 scopus 로고    scopus 로고
    • An N-terminal amphipathic helix in the Dengue virus nonstructural protein 4A mediates oligomerization and is essential for replication
    • Stern O, Hung YF, Valdau O, Yaffe Y, Harris E, et al. (2013) An N-terminal amphipathic helix in the Dengue virus nonstructural protein 4A mediates oligomerization and is essential for replication. J Virol.
    • (2013) J Virol
    • Stern, O.1    Hung, Y.F.2    Valdau, O.3    Yaffe, Y.4    Harris, E.5
  • 7
    • 33748881180 scopus 로고    scopus 로고
    • Prediction of amphipathic in-plane membrane anchors in monotopic proteins using a SVM classifier
    • Sapay N, Guermeur Y, Deleage G (2006) Prediction of amphipathic in-plane membrane anchors in monotopic proteins using a SVM classifier. BMC Bioinformatics 7: 255.
    • (2006) BMC Bioinformatics , vol.7 , pp. 255
    • Sapay, N.1    Guermeur, Y.2    Deleage, G.3
  • 8
    • 77953751833 scopus 로고    scopus 로고
    • Roles of amphipathic helices and the bin/amphiphysin/rvs (BAR) domain of endophilin in membrane curvature generation
    • Jao CC, Hegde BG, Gallop JL, Hegde PB, McMahon HT, et al. (2010) Roles of amphipathic helices and the bin/amphiphysin/rvs (BAR) domain of endophilin in membrane curvature generation. J Biol Chem 285: 20164-20170.
    • (2010) J Biol Chem , vol.285 , pp. 20164-20170
    • Jao, C.C.1    Hegde, B.G.2    Gallop, J.L.3    Hegde, P.B.4    McMahon, H.T.5
  • 9
    • 23944488301 scopus 로고    scopus 로고
    • Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle
    • DOI 10.1016/j.cell.2005.07.025, PII S0092867405007567
    • Lee MC, Orci L, Hamamoto S, Futai E, Ravazzola M, et al. (2005) Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle. Cell 122: 605-617. (Pubitemid 41191158)
    • (2005) Cell , vol.122 , Issue.4 , pp. 605-617
    • Lee, M.C.S.1    Orci, L.2    Hamamoto, S.3    Futai, E.4    Ravazzola, M.5    Schekman, R.6
  • 10
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodelling
    • DOI 10.1038/nature04396
    • McMahon HT, Gallop JL (2005) Membrane curvature and mechanisms of dynamic cell membrane remodelling. Nature 438: 590-596. (Pubitemid 41740562)
    • (2005) Nature , vol.438 , Issue.7068 , pp. 590-596
    • McMahon, H.T.1    Gallop, J.L.2
  • 11
    • 0038415985 scopus 로고    scopus 로고
    • Amphipathic helix-dependent localization of NS5A mediates hepatitis C virus RNA replication
    • DOI 10.1128/JVI.77.10.6055-6061.2003
    • Elazar M, Cheong KH, Liu P, Greenberg HB, Rice CM, et al. (2003) Amphipathic helix-dependent localization of NS5A mediates hepatitis C virus RNA replication. J Virol 77: 6055-6061. (Pubitemid 36546191)
    • (2003) Journal of Virology , vol.77 , Issue.10 , pp. 6055-6061
    • Elazar, M.1    Cheong, K.H.2    Liu, P.3    Greenberg, H.B.4    Rice, C.M.5    Glenn, J.S.6
  • 12
    • 4644281168 scopus 로고    scopus 로고
    • An N-terminal amphipathic helix in Hepatitis C Virus (HCV) NS4B mediates membrane association, correct localization of replication complex proteins, and HCV RNA replication
    • DOI 10.1128/JVI.78.20.11393-11400.2004
    • Elazar M, Liu P, Rice CM, Glenn JS (2004) An N-terminal amphipathic helix in hepatitis C virus (HCV) NS4B mediates membrane association, correct localization of replication complex proteins, and HCV RNA replication. J Virol 78: 11393-11400. (Pubitemid 39299681)
    • (2004) Journal of Virology , vol.78 , Issue.20 , pp. 11393-11400
    • Elazar, M.1    Liu, P.2    Rice, C.M.3    Glenn, J.S.4
  • 13
    • 66149132203 scopus 로고    scopus 로고
    • Identification of a novel determinant for membrane association in hepatitis C virus nonstructural protein 4B
    • Gouttenoire J, Castet V, Montserret R, Arora N, Raussens V, et al. (2009) Identification of a novel determinant for membrane association in hepatitis C virus nonstructural protein 4B. J Virol 83: 6257-6268.
    • (2009) J Virol , vol.83 , pp. 6257-6268
    • Gouttenoire, J.1    Castet, V.2    Montserret, R.3    Arora, N.4    Raussens, V.5
  • 15
    • 33846052318 scopus 로고    scopus 로고
    • Role of the amphipathic peptide of Semliki Forest virus replicase protein nsP1 in membrane association and virus replication
    • DOI 10.1128/JVI.01785-06
    • Spuul P, Salonen A, Merits A, Jokitalo E, Kaariainen L, et al. (2007) Role of the amphipathic peptide of Semliki forest virus replicase protein nsP1 in membrane association and virus replication. J Virol 81: 872-883. (Pubitemid 46067912)
    • (2007) Journal of Virology , vol.81 , Issue.2 , pp. 872-883
    • Spuul, P.1    Salonen, A.2    Merits, A.3    Jokitalo, E.4    Kaariainen, L.5    Ahola, T.6
  • 16
    • 30044452234 scopus 로고    scopus 로고
    • Testing the modularity of the N-terminal amphipathic helix conserved in picornavirus 2C proteins and hepatitis C NS5A protein
    • DOI 10.1016/j.virol.2005.08.044, PII S0042682205005283
    • Teterina NL, Gorbalenya AE, Egger D, Bienz K, Rinaudo MS, et al. (2006) Testing the modularity of the N-terminal amphipathic helix conserved in picornavirus 2C proteins and hepatitis C NS5A protein. Virology 344: 453-467. (Pubitemid 43049632)
    • (2006) Virology , vol.344 , Issue.2 , pp. 453-467
    • Teterina, N.L.1    Gorbalenya, A.E.2    Egger, D.3    Bienz, K.4    Rinaudo, M.S.5    Ehrenfeld, E.6
  • 17
    • 77953016640 scopus 로고    scopus 로고
    • Identification of a class of HCV inhibitors directed against the nonstructural protein NS4B
    • Cho NJ, Dvory-Sobol H, Lee C, Cho SJ, Bryson P, et al. (2010) Identification of a class of HCV inhibitors directed against the nonstructural protein NS4B. Sci Transl Med 2: 15ra16.
    • (2010) Sci Transl Med , vol.2
    • Cho, N.J.1    Dvory-Sobol, H.2    Lee, C.3    Cho, S.J.4    Bryson, P.5
  • 18
    • 0037731254 scopus 로고    scopus 로고
    • A rapid method to attain isotope labeled small soluble peptides for NMR studies
    • DOI 10.1023/A:1023887412387
    • Koenig BW, Rogowski M, Louis JM (2003) A rapid method to attain isotope labeled small soluble peptides for NMR studies. J Biomol NMR 26: 193-202. (Pubitemid 36758440)
    • (2003) Journal of Biomolecular NMR , vol.26 , Issue.3 , pp. 193-202
    • Koenig, B.W.1    Rogowski, M.2    Louis, J.M.3
  • 19
    • 43549085008 scopus 로고    scopus 로고
    • High-Efficiency and Robust Expression System for Stable Isotope-Labeled Peptides
    • Kohno T, Xiang L, Inaoka Y, Hayashi K, Suzuki C, et al. (2008) High-Efficiency and Robust Expression System for Stable Isotope-Labeled Peptides. Int J Pept Res Ther 14: 157-165.
    • (2008) Int J Pept Res Ther , vol.14 , pp. 157-165
    • Kohno, T.1    Xiang, L.2    Inaoka, Y.3    Hayashi, K.4    Suzuki, C.5
  • 20
    • 0032111031 scopus 로고    scopus 로고
    • 13C
    • Kohno T, Kusunoki H, Sato K, Wakamatsu K (1998) A new general method for the biosynthesis of stable isotope-enriched peptides using a decahistidine-tagged ubiquitin fusion system: an application to the production of mastoparan-X uniformly enriched with 15N and 15N/13C. J Biomol NMR 12: 109-121. (Pubitemid 128512837)
    • (1998) Journal of Biomolecular NMR , vol.12 , Issue.1 , pp. 109-121
    • Kohno, T.1    Kusunoki, H.2    Sato, K.3    Wakamatsu, K.4
  • 21
    • 79952289327 scopus 로고    scopus 로고
    • Multiparameter RNA and codon optimization: A standardized tool to assess and enhance autologous mammalian gene expression
    • Fath S, Bauer AP, Liss M, Spriestersbach A, Maertens B, et al. (2011) Multiparameter RNA and codon optimization: a standardized tool to assess and enhance autologous mammalian gene expression. PLoS One 6: e17596.
    • (2011) PLoS One , vol.6
    • Fath, S.1    Bauer, A.P.2    Liss, M.3    Spriestersbach, A.4    Maertens, B.5
  • 22
    • 0030691041 scopus 로고    scopus 로고
    • Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR
    • Huth JR, Bewley CA, Jackson BM, Hinnebusch AG, Clore GM, et al. (1997) Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR. Protein Sci 6: 2359-2364. (Pubitemid 27490746)
    • (1997) Protein Science , vol.6 , Issue.11 , pp. 2359-2364
    • Huth, J.R.1    Bewley, C.A.2    Jackson, B.M.3    Hinnebusch, A.G.4    Clore, G.M.5    Gronenborn, A.M.6
  • 23
    • 77957219390 scopus 로고
    • A simple method for site-directed mutagenesis using the polymerase chain reaction
    • Hemsley A, Arnheim N, Toney MD, Cortopassi G, Galas DJ (1989) A simple method for site-directed mutagenesis using the polymerase chain reaction. Nucleic Acids Res 17: 6545-6551. (Pubitemid 19215577)
    • (1989) Nucleic Acids Research , vol.17 , Issue.16 , pp. 6545-6551
    • Hemsley, A.1    Arnheim, N.2    Toney, M.D.3    Cortopassi, G.4    Galas, D.J.5
  • 24
    • 0035711194 scopus 로고    scopus 로고
    • Tobacco etch virus protease: Mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency
    • Kapust RB, Tozser J, Fox JD, Anderson DE, Cherry S, et al. (2001) Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency. Protein Eng 14: 993-1000. (Pubitemid 34137240)
    • (2001) Protein Engineering , vol.14 , Issue.12 , pp. 993-1000
    • Kapust, R.B.1    Tozser, J.2    Fox, J.D.3    Anderson, D.E.4    Cherry, S.5    Copeland, T.D.6    Waugh, D.S.7
  • 25
    • 79951549811 scopus 로고    scopus 로고
    • Recovering lost magnetization: Polarization enhancement in biomolecular NMR
    • Favier A, Brutscher B (2011) Recovering lost magnetization: polarization enhancement in biomolecular NMR. J Biomol NMR 49: 9-15.
    • (2011) J Biomol NMR , vol.49 , pp. 9-15
    • Favier, A.1    Brutscher, B.2
  • 26
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, et al. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6: 277-293.
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5
  • 28
    • 0028804911 scopus 로고
    • Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli
    • Kane JF (1995) Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli. Curr Opin Biotechnol 6: 494-500.
    • (1995) Curr Opin Biotechnol , vol.6 , pp. 494-500
    • Kane, J.F.1
  • 29
    • 33646596978 scopus 로고    scopus 로고
    • Highly efficient expression and purification system of small-size protein domains in Escherichia coli for biochemical characterization
    • Bao WJ, Gao YG, Chang YG, Zhang TY, Lin XJ, et al. (2006) Highly efficient expression and purification system of small-size protein domains in Escherichia coli for biochemical characterization. Protein Expr Purif 47: 599-606.
    • (2006) Protein Expr Purif , vol.47 , pp. 599-606
    • Bao, W.J.1    Gao, Y.G.2    Chang, Y.G.3    Zhang, T.Y.4    Lin, X.J.5
  • 31
    • 0343852701 scopus 로고    scopus 로고
    • Conformational stability of pGEX-expressed Schistosoma japonicum glutathione S-transferase: A detoxification enzyme and fusion-protein affinity tag
    • Kaplan W, Husler P, Klump H, Erhardt J, Sluis-Cremer N, et al. (1997) Conformational stability of pGEX-expressed Schistosoma japonicum glutathione S-transferase: a detoxification enzyme and fusion-protein affinity tag. Protein Sci 6: 399-406. (Pubitemid 27079932)
    • (1997) Protein Science , vol.6 , Issue.2 , pp. 399-406
    • Kaplan, W.1    Husler, P.2    Klump, H.3    Erhardt, J.4    Sluis-Cremer, N.5    Dirr, H.6
  • 32
    • 0028593398 scopus 로고
    • Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a sixamino acid conserved neutralizing epitope of gp41 from HIV
    • Lim K, Ho JX, Keeling K, Gilliland GL, Ji X, et al. (1994) Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a sixamino acid conserved neutralizing epitope of gp41 from HIV. Protein Sci 3: 2233-2244.
    • (1994) Protein Sci , vol.3 , pp. 2233-2244
    • Lim, K.1    Ho, J.X.2    Keeling, K.3    Gilliland, G.L.4    Ji, X.5
  • 33
    • 0028931691 scopus 로고
    • Crystal structures of a schistosomal drug and vaccine target: Glutathione S-transferase from Schistosoma japonica and its complex with the leading antischistosomal drug praziquantel
    • McTigue MA, Williams DR, Tainer JA (1995) Crystal structures of a schistosomal drug and vaccine target: glutathione S-transferase from Schistosoma japonica and its complex with the leading antischistosomal drug praziquantel. J Mol Biol 246: 21-27.
    • (1995) J Mol Biol , vol.246 , pp. 21-27
    • McTigue, M.A.1    Williams, D.R.2    Tainer, J.A.3
  • 34
    • 0032209665 scopus 로고    scopus 로고
    • GST-Induced dimerization of DNA-binding domains alters characteristics of their interaction with DNA
    • Niedziela-Majka A, Rymarczyk G, Kochman M, Ozyhar A (1998) GST-Induced dimerization of DNA-binding domains alters characteristics of their interaction with DNA. Protein Expr Purif 14: 208-220.
    • (1998) Protein Expr Purif , vol.14 , pp. 208-220
    • Niedziela-Majka, A.1    Rymarczyk, G.2    Kochman, M.3    Ozyhar, A.4
  • 35
    • 84856710211 scopus 로고    scopus 로고
    • Dynein achieves processive motion using both stochastic and coordinated stepping
    • Qiu W, Derr ND, Goodman BS, Villa E, Wu D, et al. (2012) Dynein achieves processive motion using both stochastic and coordinated stepping. Nat Struct Mol Biol 19: 193-200.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 193-200
    • Qiu, W.1    Derr, N.D.2    Goodman, B.S.3    Villa, E.4    Wu, D.5
  • 36
    • 0030842771 scopus 로고    scopus 로고
    • Glutathione S-transferase can be used as a C-terminal, enzymatically active dimerization module for a recombinant protease inhibitor, and functionally secreted into the periplasm of Escherichia cell
    • Tudyka T, Skerra A (1997) Glutathione S-transferase can be used as a C-terminal, enzymatically active dimerization module for a recombinant protease inhibitor, and functionally secreted into the periplasm of Escherichia coli. Protein Sci 6: 2180-2187. (Pubitemid 27449297)
    • (1997) Protein Science , vol.6 , Issue.10 , pp. 2180-2187
    • Tudyka, T.1    Skerra, A.2
  • 37
    • 84862814602 scopus 로고    scopus 로고
    • Tobacco etch virus protease retains its activity in various buffers and in the presence of diverse additives
    • Sun C, Liang J, Shi R, Gao X, Zhang R, et al. (2012) Tobacco etch virus protease retains its activity in various buffers and in the presence of diverse additives. Protein Expr Purif 82: 226-231.
    • (2012) Protein Expr Purif , vol.82 , pp. 226-231
    • Sun, C.1    Liang, J.2    Shi, R.3    Gao, X.4    Zhang, R.5
  • 38
    • 80054052318 scopus 로고    scopus 로고
    • An overview of enzymatic reagents for the removal of affinity tags
    • Waugh DS (2011) An overview of enzymatic reagents for the removal of affinity tags. Protein Expr Purif 80: 283-293.
    • (2011) Protein Expr Purif , vol.80 , pp. 283-293
    • Waugh, D.S.1
  • 39
    • 40649103150 scopus 로고    scopus 로고
    • Expression and purification of glutathione-Stransferase fusion proteins
    • Unit16 17
    • Smith DB, Corcoran LM (2001) Expression and purification of glutathione-Stransferase fusion proteins. Curr Protoc Mol Biol Chapter 16: Unit16 17.
    • (2001) Curr Protoc Mol Biol Chapter , vol.16
    • Smith, D.B.1    Corcoran, L.M.2


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