메뉴 건너뛰기




Volumn 7, Issue 8, 2012, Pages

Modified recombinant proteins can be exported via the sec pathway in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ACYL CARRIER PROTEIN; BIOTIN CARBOXYL CARRIER PROTEIN; BIOTIN LIGASE; CARRIER PROTEIN; HYBRID PROTEIN; LIGASE; MALTOSE BINDING PROTEIN; RECOMBINANT PROTEIN; SECRETORY PROTEIN; UNCLASSIFIED DRUG; YEBE PROTEIN;

EID: 84865048608     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0042519     Document Type: Article
Times cited : (16)

References (43)
  • 1
    • 35848970747 scopus 로고    scopus 로고
    • Mapping protein post-translational modifications with mass spectrometry
    • Witze ES, Old WM, Resing KA, Ahn NG, (2007) Mapping protein post-translational modifications with mass spectrometry. Nat Methods 4: 798-806.
    • (2007) Nat Methods , vol.4 , pp. 798-806
    • Witze, E.S.1    Old, W.M.2    Resing, K.A.3    Ahn, N.G.4
  • 2
    • 37349097703 scopus 로고    scopus 로고
    • Overexpression of post-translationally modified peptides in Escherichia coli by co-expression with modifying enzymes
    • Sugase K, Landes MA, Wright PE, Martinez-Yamout M, (2008) Overexpression of post-translationally modified peptides in Escherichia coli by co-expression with modifying enzymes. Protein Expr Purif 57: 108-115.
    • (2008) Protein Expr Purif , vol.57 , pp. 108-115
    • Sugase, K.1    Landes, M.A.2    Wright, P.E.3    Martinez-Yamout, M.4
  • 3
    • 40949099577 scopus 로고    scopus 로고
    • Genetically encoding N(epsilon)-acetyllysine in recombinant proteins
    • Neumann H, Peak-Chew SY, Chin JW, (2008) Genetically encoding N(epsilon)-acetyllysine in recombinant proteins. Nat Chem Biol 4: 232-234.
    • (2008) Nat Chem Biol , vol.4 , pp. 232-234
    • Neumann, H.1    Peak-Chew, S.Y.2    Chin, J.W.3
  • 4
    • 59249096264 scopus 로고    scopus 로고
    • Strategies for the expression of SUMO-modified target proteins in Escherichia coli
    • Saitoh H, Uwada J, Azusa K, (2009) Strategies for the expression of SUMO-modified target proteins in Escherichia coli. Methods Mol Biol 497: 211-221.
    • (2009) Methods Mol Biol , vol.497 , pp. 211-221
    • Saitoh, H.1    Uwada, J.2    Azusa, K.3
  • 5
    • 76649117720 scopus 로고    scopus 로고
    • Phosphopantetheinylation and specificity of acyl carrier proteins in the mupirocin biosynthetic cluster
    • Shields JA, Rahman AS, Arthur CJ, Crosby J, Hothersall J, et al. (2010) Phosphopantetheinylation and specificity of acyl carrier proteins in the mupirocin biosynthetic cluster. Chembiochem 11: 248-255.
    • (2010) Chembiochem , vol.11 , pp. 248-255
    • Shields, J.A.1    Rahman, A.S.2    Arthur, C.J.3    Crosby, J.4    Hothersall, J.5
  • 6
    • 77956600125 scopus 로고    scopus 로고
    • In vivo biotinylation of bacterial magnetic particles by a truncated form of Escherichia coli biotin ligase and biotin acceptor peptide
    • Maeda Y, Yoshino T, Matsunaga T, (2010) In vivo biotinylation of bacterial magnetic particles by a truncated form of Escherichia coli biotin ligase and biotin acceptor peptide. Appl Environ Microbiol 76: 5785-5790.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 5785-5790
    • Maeda, Y.1    Yoshino, T.2    Matsunaga, T.3
  • 7
    • 50649104037 scopus 로고    scopus 로고
    • Protein translocation across the bacterial cytoplasmic membrane
    • Driessen AJ, Nouwen N, (2008) Protein translocation across the bacterial cytoplasmic membrane. Annu Rev Biochem 77: 643-667.
    • (2008) Annu Rev Biochem , vol.77 , pp. 643-667
    • Driessen, A.J.1    Nouwen, N.2
  • 8
    • 50049087513 scopus 로고    scopus 로고
    • Sec- and Tat-mediated protein secretion across the bacterial cytoplasmic membrane-distinct translocases and mechanisms
    • Natale P, Bruser T, Driessen AJ, (2008) Sec- and Tat-mediated protein secretion across the bacterial cytoplasmic membrane-distinct translocases and mechanisms. Biochim Biophys Acta 1778: 1735-1756.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 1735-1756
    • Natale, P.1    Bruser, T.2    Driessen, A.J.3
  • 9
    • 64049104169 scopus 로고    scopus 로고
    • The quest for a better resolution of protein-translocation processes. Conference on the Control, Co-ordination and Regulation of Protein Targeting and Translocation
    • Borgese N, Driessen AJ, Rapaport D, Robinson C, (2009) The quest for a better resolution of protein-translocation processes. Conference on the Control, Co-ordination and Regulation of Protein Targeting and Translocation. EMBO Rep 10: 337-342.
    • (2009) EMBO Rep , vol.10 , pp. 337-342
    • Borgese, N.1    Driessen, A.J.2    Rapaport, D.3    Robinson, C.4
  • 10
    • 70350283106 scopus 로고    scopus 로고
    • Extracellular recombinant protein production from Escherichia coli
    • Ni Y, Chen R, (2009) Extracellular recombinant protein production from Escherichia coli. Biotechnol Lett 31: 1661-1670.
    • (2009) Biotechnol Lett , vol.31 , pp. 1661-1670
    • Ni, Y.1    Chen, R.2
  • 11
    • 77952516669 scopus 로고    scopus 로고
    • Secretory production of recombinant proteins in Escherichia coli
    • Yoon SH, Kim SK, Kim JF, (2010) Secretory production of recombinant proteins in Escherichia coli. Recent Pat Biotechnol 4: 23-29.
    • (2010) Recent Pat Biotechnol , vol.4 , pp. 23-29
    • Yoon, S.H.1    Kim, S.K.2    Kim, J.F.3
  • 13
    • 79952174790 scopus 로고    scopus 로고
    • A secretory system for bacterial production of high-profile protein targets
    • Kotzsch A, Vernet E, Hammarstrom M, Berthelsen J, Weigelt J, et al. (2011) A secretory system for bacterial production of high-profile protein targets. Protein Sci 20: 597-609.
    • (2011) Protein Sci , vol.20 , pp. 597-609
    • Kotzsch, A.1    Vernet, E.2    Hammarstrom, M.3    Berthelsen, J.4    Weigelt, J.5
  • 14
    • 53549088613 scopus 로고    scopus 로고
    • Proteome-based identification of fusion partner for high-level extracellular production of recombinant proteins in Escherichia coli
    • Qian ZG, Xia XX, Choi JH, Lee SY, (2008) Proteome-based identification of fusion partner for high-level extracellular production of recombinant proteins in Escherichia coli. Biotechnol Bioeng 101: 587-601.
    • (2008) Biotechnol Bioeng , vol.101 , pp. 587-601
    • Qian, Z.G.1    Xia, X.X.2    Choi, J.H.3    Lee, S.Y.4
  • 15
    • 30544435865 scopus 로고    scopus 로고
    • Extracellular accumulation of recombinant proteins fused to the carrier protein YebF in Escherichia coli
    • Zhang G, Brokx S, Weiner JH, (2006) Extracellular accumulation of recombinant proteins fused to the carrier protein YebF in Escherichia coli. Nat Biotechnol 24: 100-104.
    • (2006) Nat Biotechnol , vol.24 , pp. 100-104
    • Zhang, G.1    Brokx, S.2    Weiner, J.H.3
  • 16
    • 54049122954 scopus 로고    scopus 로고
    • Post-translational enzyme modification by the phosphopantetheinyl transferase is required for lysine and penicillin biosynthesis but not for roquefortine or fatty acid formation in Penicillium chrysogenum
    • Garcia-Estrada C, Ullan RV, Velasco-Conde T, Godio RP, Teijeira F, et al. (2008) Post-translational enzyme modification by the phosphopantetheinyl transferase is required for lysine and penicillin biosynthesis but not for roquefortine or fatty acid formation in Penicillium chrysogenum. Biochem J 415: 317-324.
    • (2008) Biochem J , vol.415 , pp. 317-324
    • Garcia-Estrada, C.1    Ullan, R.V.2    Velasco-Conde, T.3    Godio, R.P.4    Teijeira, F.5
  • 17
    • 21344468147 scopus 로고    scopus 로고
    • Molecular genetics of biotin metabolism: old vitamin, new science
    • Gravel RA, Narang MA, (2005) Molecular genetics of biotin metabolism: old vitamin, new science. J Nutr Biochem 16: 428-431.
    • (2005) J Nutr Biochem , vol.16 , pp. 428-431
    • Gravel, R.A.1    Narang, M.A.2
  • 18
    • 65549118633 scopus 로고    scopus 로고
    • De novo biosynthesis of vanillin in fission yeast (Schizosaccharomyces pombe) and baker's yeast (Saccharomyces cerevisiae)
    • Hansen EH, Moller BL, Kock GR, Bunner CM, Kristensen C, et al. (2009) De novo biosynthesis of vanillin in fission yeast (Schizosaccharomyces pombe) and baker's yeast (Saccharomyces cerevisiae). Appl Environ Microbiol 75: 2765-2774.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 2765-2774
    • Hansen, E.H.1    Moller, B.L.2    Kock, G.R.3    Bunner, C.M.4    Kristensen, C.5
  • 19
    • 79551556820 scopus 로고    scopus 로고
    • The role of histone H4 biotinylation in the structure of nucleosomes
    • Filenko NA, Kolar C, West JT, Smith SA, Hassan YI, et al. (2011) The role of histone H4 biotinylation in the structure of nucleosomes. PLoS One 6: e16299.
    • (2011) PLoS One , vol.6
    • Filenko, N.A.1    Kolar, C.2    West, J.T.3    Smith, S.A.4    Hassan, Y.I.5
  • 20
    • 84886012022 scopus 로고    scopus 로고
    • High-throughput biotinylation of proteins
    • Kay BK, Thai S, Volgina VV, (2009) High-throughput biotinylation of proteins. Methods Mol Biol 498: 185-196.
    • (2009) Methods Mol Biol , vol.498 , pp. 185-196
    • Kay, B.K.1    Thai, S.2    Volgina, V.V.3
  • 21
    • 80055084063 scopus 로고    scopus 로고
    • Rational development of caged-biotin protein-labeling agents and some applications in live cells
    • Terai T, Maki E, Sugiyama S, Takahashi Y, Matsumura H, et al. (2011) Rational development of caged-biotin protein-labeling agents and some applications in live cells. Chem Biol 18: 1261-1272.
    • (2011) Chem Biol , vol.18 , pp. 1261-1272
    • Terai, T.1    Maki, E.2    Sugiyama, S.3    Takahashi, Y.4    Matsumura, H.5
  • 22
    • 0035813096 scopus 로고    scopus 로고
    • The biotinyl domain of Escherichia coli acetyl-CoA carboxylase. Evidence that the "thumb" structure id essential and that the domain functions as a dimer
    • Cronan JE Jr, (2001) The biotinyl domain of Escherichia coli acetyl-CoA carboxylase. Evidence that the "thumb" structure id essential and that the domain functions as a dimer. J Biol Chem 276: 37355-37364.
    • (2001) J Biol Chem , vol.276 , pp. 37355-37364
    • Cronan Jr., J.E.1
  • 23
    • 84934444524 scopus 로고    scopus 로고
    • Expression and purification of soluble His(6)-tagged TEV protease
    • Tropea JE, Cherry S, Waugh DS, (2009) Expression and purification of soluble His(6)-tagged TEV protease. Methods Mol Biol 498: 297-307.
    • (2009) Methods Mol Biol , vol.498 , pp. 297-307
    • Tropea, J.E.1    Cherry, S.2    Waugh, D.S.3
  • 24
    • 0033955033 scopus 로고    scopus 로고
    • Holo-(acyl carrier protein) synthase and phosphopantetheinyl transfer in Escherichia coli
    • Flugel RS, Hwangbo Y, Lambalot RH, Cronan JE Jr, Walsh CT, (2000) Holo-(acyl carrier protein) synthase and phosphopantetheinyl transfer in Escherichia coli. J Biol Chem 275: 959-968.
    • (2000) J Biol Chem , vol.275 , pp. 959-968
    • Flugel, R.S.1    Hwangbo, Y.2    Lambalot, R.H.3    Cronan Jr., J.E.4    Walsh, C.T.5
  • 25
    • 0033555541 scopus 로고    scopus 로고
    • Molecular recognition in a post-translational modification of exceptional specificity. Mutants of the biotinylated domain of acetyl-CoA carboxylase defective in recognition by biotin protein ligase
    • Chapman-Smith A, Morris TW, Wallace JC, Cronan JE Jr, (1999) Molecular recognition in a post-translational modification of exceptional specificity. Mutants of the biotinylated domain of acetyl-CoA carboxylase defective in recognition by biotin protein ligase. J Biol Chem 274: 1449-1457.
    • (1999) J Biol Chem , vol.274 , pp. 1449-1457
    • Chapman-Smith, A.1    Morris, T.W.2    Wallace, J.C.3    Cronan Jr., J.E.4
  • 26
    • 0021112871 scopus 로고
    • Ratio of active to inactive forms of acyl carrier protein in Escherichia coli
    • Jackowski S, Rock CO, (1983) Ratio of active to inactive forms of acyl carrier protein in Escherichia coli. J Biol Chem 258: 15186-15191.
    • (1983) J Biol Chem , vol.258 , pp. 15186-15191
    • Jackowski, S.1    Rock, C.O.2
  • 27
    • 0028108943 scopus 로고
    • Expression, biotinylation and purification of a biotin-domain peptide from the biotin carboxy carrier protein of Escherichia coli acetyl-CoA carboxylase
    • Chapman-Smith A, Turner DL, Cronan JE Jr, Morris TW, Wallace JC, (1994) Expression, biotinylation and purification of a biotin-domain peptide from the biotin carboxy carrier protein of Escherichia coli acetyl-CoA carboxylase. Biochem J 302 (Pt 3): 881-887.
    • (1994) Biochem J , vol.302 , Issue.Pt 3 , pp. 881-887
    • Chapman-Smith, A.1    Turner, D.L.2    Cronan Jr., J.E.3    Morris, T.W.4    Wallace, J.C.5
  • 28
    • 0029989316 scopus 로고    scopus 로고
    • The apparent coupling between synthesis and posttranslational modification of Escherichia coli acyl carrier protein is due to inhibition of amino acid biosynthesis
    • Keating DH, Zhang Y, Cronan JE Jr, (1996) The apparent coupling between synthesis and posttranslational modification of Escherichia coli acyl carrier protein is due to inhibition of amino acid biosynthesis. J Bacteriol 178: 2662-2667.
    • (1996) J Bacteriol , vol.178 , pp. 2662-2667
    • Keating, D.H.1    Zhang, Y.2    Cronan Jr., J.E.3
  • 29
    • 0019887843 scopus 로고
    • Molecular properties of acyl carrier protein derivatives
    • Rock CO, Cronan JE Jr, Armitage IM, (1981) Molecular properties of acyl carrier protein derivatives. J Biol Chem 256: 2669-2674.
    • (1981) J Biol Chem , vol.256 , pp. 2669-2674
    • Rock, C.O.1    Cronan Jr., J.E.2    Armitage, I.M.3
  • 30
    • 0024294402 scopus 로고
    • The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein
    • Collier DN, Bankaitis VA, Weiss JB, Bassford PJ Jr, (1988) The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein. Cell 53: 273-283.
    • (1988) Cell , vol.53 , pp. 273-283
    • Collier, D.N.1    Bankaitis, V.A.2    Weiss, J.B.3    Bassford Jr., P.J.4
  • 31
    • 79953898209 scopus 로고    scopus 로고
    • Biotinylation, a post-translational modification controlled by the rate of protein-protein association
    • Ingaramo M, Beckett D, (2011) Biotinylation, a post-translational modification controlled by the rate of protein-protein association. J Biol Chem 286: 13071-13078.
    • (2011) J Biol Chem , vol.286 , pp. 13071-13078
    • Ingaramo, M.1    Beckett, D.2
  • 32
    • 0025087137 scopus 로고
    • Azide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery
    • Oliver DB, Cabelli RJ, Dolan KM, Jarosik GP, (1990) Azide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery. Proc Natl Acad Sci U S A 87: 8227-8231.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 8227-8231
    • Oliver, D.B.1    Cabelli, R.J.2    Dolan, K.M.3    Jarosik, G.P.4
  • 33
    • 34547938895 scopus 로고    scopus 로고
    • Bacterial sec-translocase unfolds and translocates a class of folded protein domains
    • Nouwen N, Berrelkamp G, Driessen AJ, (2007) Bacterial sec-translocase unfolds and translocates a class of folded protein domains. J Mol Biol 372: 422-433.
    • (2007) J Mol Biol , vol.372 , pp. 422-433
    • Nouwen, N.1    Berrelkamp, G.2    Driessen, A.J.3
  • 34
    • 0026001727 scopus 로고
    • Escherichia coli exports previously folded and biotinated protein domains
    • Reed KE, Cronan JE Jr, (1991) Escherichia coli exports previously folded and biotinated protein domains. J Biol Chem 266: 11425-11428.
    • (1991) J Biol Chem , vol.266 , pp. 11425-11428
    • Reed, K.E.1    Cronan Jr., J.E.2
  • 35
    • 33645365498 scopus 로고    scopus 로고
    • Coexpression of TorD enhances the transport of GFP via the TAT pathway
    • Li SY, Chang BY, Lin SC, (2006) Coexpression of TorD enhances the transport of GFP via the TAT pathway. J Biotechnol 122: 412-421.
    • (2006) J Biotechnol , vol.122 , pp. 412-421
    • Li, S.Y.1    Chang, B.Y.2    Lin, S.C.3
  • 36
    • 62649170149 scopus 로고    scopus 로고
    • Exploration of twin-arginine translocation for expression and purification of correctly folded proteins in Escherichia coli
    • Fisher AC, Kim JY, Perez-Rodriguez R, Tullman-Ercek D, Fish WR, et al. (2008) Exploration of twin-arginine translocation for expression and purification of correctly folded proteins in Escherichia coli. Microb Biotechnol 1: 403-415.
    • (2008) Microb Biotechnol , vol.1 , pp. 403-415
    • Fisher, A.C.1    Kim, J.Y.2    Perez-Rodriguez, R.3    Tullman-Ercek, D.4    Fish, W.R.5
  • 37
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension
    • Horton RM, Hunt HD, Ho SN, Pullen JK, Pease LR, (1989) Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene 77: 61-68.
    • (1989) Gene , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 39
    • 49149088292 scopus 로고    scopus 로고
    • The Tat system proofreads FeS protein substrates and directly initiates the disposal of rejected molecules
    • Matos CF, Robinson C, Di Cola A, (2008) The Tat system proofreads FeS protein substrates and directly initiates the disposal of rejected molecules. EMBO J 27: 2055-2063.
    • (2008) EMBO J , vol.27 , pp. 2055-2063
    • Matos, C.F.1    Robinson, C.2    Di Cola, A.3
  • 40
    • 64049116611 scopus 로고    scopus 로고
    • Bacterial fatty acid synthesis and its relationships with polyketide synthetic pathways
    • Cronan JE, Thomas J, (2009) Bacterial fatty acid synthesis and its relationships with polyketide synthetic pathways. Methods Enzymol 459: 395-433.
    • (2009) Methods Enzymol , vol.459 , pp. 395-433
    • Cronan, J.E.1    Thomas, J.2
  • 41
    • 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
  • 42
    • 0030868266 scopus 로고    scopus 로고
    • Covalent modification of an exposed surface turn alters the global conformation of the biotin carrier domain of Escherichia coli acetyl-CoA carboxylase
    • Chapman-Smith A, Forbes BE, Wallace JC, Cronan JE Jr, (1997) Covalent modification of an exposed surface turn alters the global conformation of the biotin carrier domain of Escherichia coli acetyl-CoA carboxylase. J Biol Chem 272: 26017-26022.
    • (1997) J Biol Chem , vol.272 , pp. 26017-26022
    • Chapman-Smith, A.1    Forbes, B.E.2    Wallace, J.C.3    Cronan Jr., J.E.4
  • 43
    • 0030037751 scopus 로고    scopus 로고
    • An isoleucine to valine substitution in Escherichia coli acyl carrier protein results in a functional protein of decreased molecular radius at elevated pH
    • Keating DH, Cronan JE Jr, (1996) An isoleucine to valine substitution in Escherichia coli acyl carrier protein results in a functional protein of decreased molecular radius at elevated pH. J Biol Chem 271: 15905-15910.
    • (1996) J Biol Chem , vol.271 , pp. 15905-15910
    • Keating, D.H.1    Cronan Jr., J.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.