메뉴 건너뛰기




Volumn 9, Issue , 2010, Pages

Protein solubility and differential proteomic profiling of recombinant Escherichia coli overexpressing double-tagged fusion proteins

Author keywords

[No Author keywords available]

Indexed keywords

GLUTATHIONE TRANSFERASE; ISOPROPYL THIOGALACTOSIDE; N ACETYLNEURAMINIC ACID; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE 2 EPIMERASE; CARRIER PROTEIN; CHAPERONE; EPIMERASE; ESCHERICHIA COLI PROTEIN; HEAT SHOCK PROTEIN; HYBRID PROTEIN; LYASE; N ACETYLNEURAMINATE LYASE; N ACYL D GLUCOSAMINE 2 EPIMERASE; N-ACETYLNEURAMINATE LYASE; N-ACYL-D-GLUCOSAMINE 2-EPIMERASE; PROTEOME;

EID: 77956481419     PISSN: None     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/1475-2859-9-63     Document Type: Article
Times cited : (19)

References (37)
  • 1
    • 0042193601 scopus 로고    scopus 로고
    • Protein aggregation in recombinant bacteria: biological role of inclusion bodies
    • 10.1023/A:1025024104862, 14514038
    • Villaverde A, Mar Carrió M. Protein aggregation in recombinant bacteria: biological role of inclusion bodies. Biotechnol Lett 2003, 25:1385-1395. 10.1023/A:1025024104862, 14514038.
    • (2003) Biotechnol Lett , vol.25 , pp. 1385-1395
    • Villaverde, A.1    Mar Carrió, M.2
  • 3
    • 0033589826 scopus 로고    scopus 로고
    • New fusion protein systems designed to give soluble expression in Escherichia coli
    • 10.1002/(SICI)1097-0290(19991120)65:4<382::AID-BIT2>3.0.CO;2-I, 10506413
    • Davis GD, Elisee C, Newham DM, Harrison RG. New fusion protein systems designed to give soluble expression in Escherichia coli. Biotechnol Bioeng 1999, 65:382-388. 10.1002/(SICI)1097-0290(19991120)65:4<382::AID-BIT2>3.0.CO;2-I, 10506413.
    • (1999) Biotechnol Bioeng , vol.65 , pp. 382-388
    • Davis, G.D.1    Elisee, C.2    Newham, D.M.3    Harrison, R.G.4
  • 4
    • 29244442950 scopus 로고    scopus 로고
    • Simplified screening for the detection of soluble fusion constructs expressed in E. coli using a modular set of vectors
    • 10.1186/1475-2859-4-34, 1326211, 16351710
    • Dümmler A, Lawrence A, de Marco A. Simplified screening for the detection of soluble fusion constructs expressed in E. coli using a modular set of vectors. Microb Cell Fact 2005, 4:34. 10.1186/1475-2859-4-34, 1326211, 16351710.
    • (2005) Microb Cell Fact , vol.4 , pp. 34
    • Dümmler, A.1    Lawrence, A.2    de Marco, A.3
  • 5
    • 68849112214 scopus 로고    scopus 로고
    • Production of N-acetyl-D-neuraminic acid using two sequential enzymes overexpressed as double-tagged fusion proteins
    • 10.1186/1472-6750-9-63, 2722590, 19586552
    • Wang T, Chen Y, Pan H, Wang F, Cheng C, Lee W. Production of N-acetyl-D-neuraminic acid using two sequential enzymes overexpressed as double-tagged fusion proteins. BMC Biotechnol 2009, 9:63. 10.1186/1472-6750-9-63, 2722590, 19586552.
    • (2009) BMC Biotechnol , vol.9 , pp. 63
    • Wang, T.1    Chen, Y.2    Pan, H.3    Wang, F.4    Cheng, C.5    Lee, W.6
  • 6
    • 0024709959 scopus 로고
    • Induction of a heat shock-like response by unfolded protein in Escherichia coli: dependence on protein level not protein degradation
    • Parsell DA, Sauer RT. Induction of a heat shock-like response by unfolded protein in Escherichia coli: dependence on protein level not protein degradation. Genes & Development 1989, 3:1226-1232.
    • (1989) Genes & Development , vol.3 , pp. 1226-1232
    • Parsell, D.A.1    Sauer, R.T.2
  • 7
    • 0026608065 scopus 로고
    • Isopropyl-β-d-thiogalactopyranoside influences the metabolism of Escherichia coli
    • Kosinski MJ, Rinas U, Bailey JE. Isopropyl-β-d-thiogalactopyranoside influences the metabolism of Escherichia coli. Appl Microbiol Biotechnol 1992, 36:782-784.
    • (1992) Appl Microbiol Biotechnol , vol.36 , pp. 782-784
    • Kosinski, M.J.1    Rinas, U.2    Bailey, J.E.3
  • 8
    • 10644255526 scopus 로고    scopus 로고
    • Advanced genetic strategies for recombinant protein expression in Escherichia coli
    • 10.1016/j.jbiotec.2004.08.004, 15607230
    • Sørensen HP, Mortensen KK. Advanced genetic strategies for recombinant protein expression in Escherichia coli. J Biotechnol 2005, 115:113-128. 10.1016/j.jbiotec.2004.08.004, 15607230.
    • (2005) J Biotechnol , vol.115 , pp. 113-128
    • Sørensen, H.P.1    Mortensen, K.K.2
  • 9
    • 34347374452 scopus 로고    scopus 로고
    • Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli
    • 10.1186/1472-6750-7-32, 1904446, 17565681
    • de Marco A, Deuerling E, Mogk A, Tomoyasu T, Bukau B. Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli. BMC Biotechnol 2007, 7:32. 10.1186/1472-6750-7-32, 1904446, 17565681.
    • (2007) BMC Biotechnol , vol.7 , pp. 32
    • de Marco, A.1    Deuerling, E.2    Mogk, A.3    Tomoyasu, T.4    Bukau, B.5
  • 11
    • 33745127048 scopus 로고    scopus 로고
    • The Escherichia coli proteome: past, present, and future prospects
    • 10.1128/MMBR.00036-05, 1489533, 16760308
    • Han M, Lee SY. The Escherichia coli proteome: past, present, and future prospects. Microbiol Mol Biol Rev 2006, 70:362-439. 10.1128/MMBR.00036-05, 1489533, 16760308.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 362-439
    • Han, M.1    Lee, S.Y.2
  • 12
    • 0347132485 scopus 로고    scopus 로고
    • Escherichia coli--a model system that benefits from and contributes to the evolution of proteomics
    • 10.1002/bit.10848, 14708121
    • Lee PS, Lee KH. Escherichia coli--a model system that benefits from and contributes to the evolution of proteomics. Biotechnol Bioeng 2003, 84:801-814. 10.1002/bit.10848, 14708121.
    • (2003) Biotechnol Bioeng , vol.84 , pp. 801-814
    • Lee, P.S.1    Lee, K.H.2
  • 13
    • 0042665851 scopus 로고    scopus 로고
    • Comparison of the Escherichia coli proteomes for recombinant human growth hormone producing and nonproducing fermentations
    • 10.1002/pmic.200300430, 12872237
    • Champion KM, Nishihara JC, Aldor IS, Moreno GT, Andersen D, Stults KL, Vanderlaan M. Comparison of the Escherichia coli proteomes for recombinant human growth hormone producing and nonproducing fermentations. Proteomics 2003, 3:1365-1373. 10.1002/pmic.200300430, 12872237.
    • (2003) Proteomics , vol.3 , pp. 1365-1373
    • Champion, K.M.1    Nishihara, J.C.2    Aldor, I.S.3    Moreno, G.T.4    Andersen, D.5    Stults, K.L.6    Vanderlaan, M.7
  • 14
    • 0034693456 scopus 로고    scopus 로고
    • Monitoring of genes that respond to overproduction of an insoluble recombinant protein in Escherichia coli glucose-limited fed-batch fermentations
    • 10.1002/1097-0290(20001020)70:2<217::AID-BIT11>3.0.CO;2-W, 10972933
    • Jürgen B, Lin HY, Riemschneider S, Scharf C, Neubauer P, Schmid R, Hecker M, Schweder T. Monitoring of genes that respond to overproduction of an insoluble recombinant protein in Escherichia coli glucose-limited fed-batch fermentations. Biotechnol Bioeng 2000, 70:217-224. 10.1002/1097-0290(20001020)70:2<217::AID-BIT11>3.0.CO;2-W, 10972933.
    • (2000) Biotechnol Bioeng , vol.70 , pp. 217-224
    • Jürgen, B.1    Lin, H.Y.2    Riemschneider, S.3    Scharf, C.4    Neubauer, P.5    Schmid, R.6    Hecker, M.7    Schweder, T.8
  • 15
    • 26644440190 scopus 로고    scopus 로고
    • Proteomic profiling of Escherichia coli proteins under high cell density fed-batch cultivation with overexpression of phosphogluconolactonase
    • 10.1021/bp050048m, 16209543
    • Wang Y, Wu S, Hancock WS, Trala R, Kessler M, Taylor AH, Patel PS, Aon JC. Proteomic profiling of Escherichia coli proteins under high cell density fed-batch cultivation with overexpression of phosphogluconolactonase. Biotechnol Prog 2005, 21:1401-1411. 10.1021/bp050048m, 16209543.
    • (2005) Biotechnol Prog , vol.21 , pp. 1401-1411
    • Wang, Y.1    Wu, S.2    Hancock, W.S.3    Trala, R.4    Kessler, M.5    Taylor, A.H.6    Patel, P.S.7    Aon, J.C.8
  • 16
    • 17444369061 scopus 로고    scopus 로고
    • Proteomic profiling of reconbinant Escherichia coli in high-cell-density fermentations for improved production of an antibody fragment biopharmaceutical
    • 10.1128/AEM.71.4.1717-1728.2005, 1082529, 15811994
    • Aldor IS, Krawitz DC, Forrest W, Chen C, Nishihara JC, Joly JC, Champion KM. Proteomic profiling of reconbinant Escherichia coli in high-cell-density fermentations for improved production of an antibody fragment biopharmaceutical. Appl Environ Microbiol 2005, 71:1717-1728. 10.1128/AEM.71.4.1717-1728.2005, 1082529, 15811994.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 1717-1728
    • Aldor, I.S.1    Krawitz, D.C.2    Forrest, W.3    Chen, C.4    Nishihara, J.C.5    Joly, J.C.6    Champion, K.M.7
  • 17
    • 0142072824 scopus 로고    scopus 로고
    • Engineering Escherichia coli for increased productivity of serine-rich proteins based on proteome profiling
    • 10.1128/AEM.69.10.5772-5781.2003, 201230, 14532024
    • Han M, Jeong KJ, Yoo J, Lee SY. Engineering Escherichia coli for increased productivity of serine-rich proteins based on proteome profiling. Appl Environ Microbiol 2003, 69:5772-5781. 10.1128/AEM.69.10.5772-5781.2003, 201230, 14532024.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 5772-5781
    • Han, M.1    Jeong, K.J.2    Yoo, J.3    Lee, S.Y.4
  • 18
    • 8844219685 scopus 로고    scopus 로고
    • Roles and applications of small heat shock proteins in the production of recombinant proteins in Escherichia coli
    • 10.1002/bit.20227, 15382106
    • Han M, Park SJ, Park TJ, Lee SY. Roles and applications of small heat shock proteins in the production of recombinant proteins in Escherichia coli. Biotechnol Bioeng 2004, 88:426-436. 10.1002/bit.20227, 15382106.
    • (2004) Biotechnol Bioeng , vol.88 , pp. 426-436
    • Han, M.1    Park, S.J.2    Park, T.J.3    Lee, S.Y.4
  • 19
    • 0033214149 scopus 로고    scopus 로고
    • Genome-wide expression profiling in Escherichia coli K-12
    • 10.1093/nar/27.19.3821, 148645, 10481021
    • Richmond CS, Glasner JD, Mau R, Jin H, Blattner FR. Genome-wide expression profiling in Escherichia coli K-12. Nucleic Acids Res 1999, 27:3821-3835. 10.1093/nar/27.19.3821, 148645, 10481021.
    • (1999) Nucleic Acids Res , vol.27 , pp. 3821-3835
    • Richmond, C.S.1    Glasner, J.D.2    Mau, R.3    Jin, H.4    Blattner, F.R.5
  • 20
    • 26844493677 scopus 로고    scopus 로고
    • Proteome analysis of a recombinant Bacillus megaterium strain during heterologous production of a glucosyltransferase
    • 10.1186/1477-5956-3-4, 1175100, 15927046
    • Wang W, Hollmann R, Fürch T, Nimtz M, Malten M, Jahn D, Deckwer WD. Proteome analysis of a recombinant Bacillus megaterium strain during heterologous production of a glucosyltransferase. Proteome Sci 2005, 3:4. 10.1186/1477-5956-3-4, 1175100, 15927046.
    • (2005) Proteome Sci , vol.3 , pp. 4
    • Wang, W.1    Hollmann, R.2    Fürch, T.3    Nimtz, M.4    Malten, M.5    Jahn, D.6    Deckwer, W.D.7
  • 21
    • 0037391699 scopus 로고    scopus 로고
    • Global metabolic regulation analysis for Escherichia coli K12 based on protein expression by 2-dimensional electrophoresis and enzyme activity measurement
    • Peng L, Shimizu K. Global metabolic regulation analysis for Escherichia coli K12 based on protein expression by 2-dimensional electrophoresis and enzyme activity measurement. Appl Microbiol Biotechnol 2003, 61:163-178.
    • (2003) Appl Microbiol Biotechnol , vol.61 , pp. 163-178
    • Peng, L.1    Shimizu, K.2
  • 22
    • 0033662220 scopus 로고    scopus 로고
    • DNA microarray detection of metabolic responses to protein overproduction in Escherichia coli
    • 10.1006/mben.2000.0149, 11056062
    • Oh M, Liao JC. DNA microarray detection of metabolic responses to protein overproduction in Escherichia coli. Metab Eng 2000, 2:201-209. 10.1006/mben.2000.0149, 11056062.
    • (2000) Metab Eng , vol.2 , pp. 201-209
    • Oh, M.1    Liao, J.C.2
  • 24
    • 33645508284 scopus 로고    scopus 로고
    • The Escherichia coli BarA-UvrY two-component system is a virulence determinant in the urinary tract
    • 10.1186/1471-2180-6-27, 1421404, 16529647
    • Tomenius H, Pernestig A, Jonas K, Georgellis D, Möllby R, Normark S, Melefors O. The Escherichia coli BarA-UvrY two-component system is a virulence determinant in the urinary tract. BMC Microbiol 2006, 6:27. 10.1186/1471-2180-6-27, 1421404, 16529647.
    • (2006) BMC Microbiol , vol.6 , pp. 27
    • Tomenius, H.1    Pernestig, A.2    Jonas, K.3    Georgellis, D.4    Möllby, R.5    Normark, S.6    Melefors, O.7
  • 25
    • 33845315054 scopus 로고    scopus 로고
    • Effects of the presence of ColE1 plasmid DNA in Escherichia coli on the host cell metabolism
    • 10.1186/1475-2859-5-34, 1664580, 17112383
    • Wang Z, Xiang L, Shao J, Wegrzyn A, Wegrzyn G. Effects of the presence of ColE1 plasmid DNA in Escherichia coli on the host cell metabolism. Microb Cell Fact 2006, 5:34. 10.1186/1475-2859-5-34, 1664580, 17112383.
    • (2006) Microb Cell Fact , vol.5 , pp. 34
    • Wang, Z.1    Xiang, L.2    Shao, J.3    Wegrzyn, A.4    Wegrzyn, G.5
  • 26
    • 21144443562 scopus 로고    scopus 로고
    • Homocysteine toxicity in Escherichia coli is caused by a perturbation of branched-chain amino acid biosynthesis
    • 10.1128/JB.187.13.4362-4371.2005, 1151774, 15968045
    • Tuite NL, Fraser KR, O'byrne CP. Homocysteine toxicity in Escherichia coli is caused by a perturbation of branched-chain amino acid biosynthesis. J Bacteriol 2005, 187:4362-4371. 10.1128/JB.187.13.4362-4371.2005, 1151774, 15968045.
    • (2005) J Bacteriol , vol.187 , pp. 4362-4371
    • Tuite, N.L.1    Fraser, K.R.2    O'byrne, C.P.3
  • 27
    • 0019877050 scopus 로고
    • Alternative pathways for editing non-cognate amino acids by aminoacyl-tRNA synthetases
    • 10.1093/nar/9.13.3105, 327334, 7024910
    • Jakubowski H, RFersht A. Alternative pathways for editing non-cognate amino acids by aminoacyl-tRNA synthetases. Nucleic Acids Res 1981, 9:3105-3117. 10.1093/nar/9.13.3105, 327334, 7024910.
    • (1981) Nucleic Acids Res , vol.9 , pp. 3105-3117
    • Jakubowski, H.1    R.Fersht, A.2
  • 28
    • 0035783169 scopus 로고    scopus 로고
    • Review: mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones
    • 10.1006/jsbi.2001.4352, 11580258
    • Ben-Zvi AP, Goloubinoff P. Review: mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones. J Struct Biol 2001, 135:84-93. 10.1006/jsbi.2001.4352, 11580258.
    • (2001) J Struct Biol , vol.135 , pp. 84-93
    • Ben-Zvi, A.P.1    Goloubinoff, P.2
  • 29
    • 0029973122 scopus 로고    scopus 로고
    • HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome
    • 10.1073/pnas.93.12.5808, 39143, 8650174
    • Rohrwild M, Coux O, Huang HC, Moerschell RP, Yoo SJ, Seol JH, Chung CH, Goldberg AL. HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome. Proc Natl Acad Sci USA 1996, 93:5808-5813. 10.1073/pnas.93.12.5808, 39143, 8650174.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5808-5813
    • Rohrwild, M.1    Coux, O.2    Huang, H.C.3    Moerschell, R.P.4    Yoo, S.J.5    Seol, J.H.6    Chung, C.H.7    Goldberg, A.L.8
  • 30
    • 0026784986 scopus 로고
    • Two novel heat shock genes encoding proteins produced in response to heterologous protein expression in Escherichia coli
    • 207373, 1356969
    • Allen SP, Polazzi JO, Gierse JK, Easton AM. Two novel heat shock genes encoding proteins produced in response to heterologous protein expression in Escherichia coli. J Bacteriol 1992, 174:6938-6947. 207373, 1356969.
    • (1992) J Bacteriol , vol.174 , pp. 6938-6947
    • Allen, S.P.1    Polazzi, J.O.2    Gierse, J.K.3    Easton, A.M.4
  • 32
    • 33646106328 scopus 로고    scopus 로고
    • Protein quality in bacterial inclusion bodies
    • 10.1016/j.tibtech.2006.02.007, 16503059
    • Ventura S, Villaverde A. Protein quality in bacterial inclusion bodies. Trends Biotechnol 2006, 24:179-185. 10.1016/j.tibtech.2006.02.007, 16503059.
    • (2006) Trends Biotechnol , vol.24 , pp. 179-185
    • Ventura, S.1    Villaverde, A.2
  • 33
    • 8644290874 scopus 로고    scopus 로고
    • A chaperone network controls the heat shock response in E. coli
    • 10.1101/gad.1219204, 528900, 15545634
    • Guisbert E, Herman C, Lu CZ, Gross CA. A chaperone network controls the heat shock response in E. coli. Genes Dev 2004, 18:2812-2821. 10.1101/gad.1219204, 528900, 15545634.
    • (2004) Genes Dev , vol.18 , pp. 2812-2821
    • Guisbert, E.1    Herman, C.2    Lu, C.Z.3    Gross, C.A.4
  • 34
    • 0033662168 scopus 로고    scopus 로고
    • A modified silver staining protocol for visualization of proteins compatible with matrix-assisted laser desorption/ionization and electrospray ionization-mass spectrometry
    • 10.1002/1522-2683(200011)21:17<3666::AID-ELPS3666>3.0.CO;2-6, 11271485
    • Yan JX, Wait R, Berkelman T, Harry RA, Westbrook JA, Wheeler CH, Dunn MJ. A modified silver staining protocol for visualization of proteins compatible with matrix-assisted laser desorption/ionization and electrospray ionization-mass spectrometry. Electrophoresis 2000, 21:3666-3672. 10.1002/1522-2683(200011)21:17<3666::AID-ELPS3666>3.0.CO;2-6, 11271485.
    • (2000) Electrophoresis , vol.21 , pp. 3666-3672
    • Yan, J.X.1    Wait, R.2    Berkelman, T.3    Harry, R.A.4    Westbrook, J.A.5    Wheeler, C.H.6    Dunn, M.J.7
  • 35
    • 69449093818 scopus 로고    scopus 로고
    • Proteomic changes in the hypothalamus and retroperitoneal fat from male F344 rats subjected to repeated light-dark shifts
    • 10.1002/pmic.200800813, 19658099
    • Mishra A, Cheng C, Lee W, Tsai L. Proteomic changes in the hypothalamus and retroperitoneal fat from male F344 rats subjected to repeated light-dark shifts. Proteomics 2009, 9:4017-4028. 10.1002/pmic.200800813, 19658099.
    • (2009) Proteomics , vol.9 , pp. 4017-4028
    • Mishra, A.1    Cheng, C.2    Lee, W.3    Tsai, L.4
  • 36
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • 10.1038/nprot.2006.468, 17406544
    • Shevchenko A, Tomas H, Havlis J, Olsen JV, Mann M. In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat Protoc 2006, 1:2856-2860. 10.1038/nprot.2006.468, 17406544.
    • (2006) Nat Protoc , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 37
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
    • 10.1038/nprot.2007.261, 17703201
    • Rappsilber J, Mann M, Ishihama Y. Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nat Protoc 2007, 2:1896-1906. 10.1038/nprot.2007.261, 17703201.
    • (2007) Nat Protoc , vol.2 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.