메뉴 건너뛰기




Volumn 21, Issue 5, 2005, Pages 1357-1365

Cytoplasmic overexpression, folding, and processing of penicillin acylase precursor in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

CYTOLOGY; DRUG PRODUCTS; ENZYMES; ESCHERICHIA COLI; GENES; GENETIC ENGINEERING; PROTEINS; SOLUBILITY;

EID: 26644437704     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp0501120     Document Type: Article
Times cited : (12)

References (34)
  • 1
    • 0036535753 scopus 로고    scopus 로고
    • Recombinant protein expression for therapeutic applications
    • Andersen, D. C.; Krummen, L. Recombinant protein expression for therapeutic applications. Curr. Opin. Biotechnol. 2002, 13, 117-123.
    • (2002) Curr. Opin. Biotechnol. , vol.13 , pp. 117-123
    • Andersen, D.C.1    Krummen, L.2
  • 2
  • 3
    • 0032884573 scopus 로고    scopus 로고
    • Recombinant protein expression in Escherichia coli
    • Baneyx, F. Recombinant protein expression in Escherichia coli. Curr. Opin. Biotechnol. 1999, 10, 411-421.
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 411-421
    • Baneyx, F.1
  • 4
    • 8344256552 scopus 로고    scopus 로고
    • Recombinant protein folding and misfolding in Escherichia coli
    • Baneyx, F.; Mujacic, M. Recombinant protein folding and misfolding in Escherichia coli. Nat. Biotechnol. 2004, 22, 1399-1408.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1399-1408
    • Baneyx, F.1    Mujacic, M.2
  • 5
    • 14744269790 scopus 로고
    • Structure and morphology of protein inclusion bodies in Escherichia coli
    • Bowden, G. A.; Paredes, A. M.; Georgiou, G. Structure and morphology of protein inclusion bodies in Escherichia coli. Bio/Technology 1991, 9, 725-730.
    • (1991) Bio/Technology , vol.9 , pp. 725-730
    • Bowden, G.A.1    Paredes, A.M.2    Georgiou, G.3
  • 6
    • 0014674485 scopus 로고
    • A complementation analysis of the restriction and modification of DNA in Escherichia coli
    • Boyer, H. W.; Roulland-Dussoix, D. A complementation analysis of the restriction and modification of DNA in Escherichia coli. J. Mol. Biol. 1969, 41, 459-472.
    • (1969) J. Mol. Biol. , vol.41 , pp. 459-472
    • Boyer, H.W.1    Roulland-Dussoix, D.2
  • 7
    • 0008472227 scopus 로고    scopus 로고
    • Novel strategy for efficient screening and construction of host/vector systems to overproduce penicillin acylase in Escherichia coli
    • Chou, C. P.; Yu, C.-C.; Lin, W.-J.; Kuo, B.-Y.; Wang, W.-C. Novel strategy for efficient screening and construction of host/vector systems to overproduce penicillin acylase in Escherichia coli. Biotechnol. Bioeng. 1999a, 65, 219-226.
    • (1999) Biotechnol. Bioeng. , vol.65 , pp. 219-226
    • Chou, C.P.1    Yu, C.-C.2    Lin, W.-J.3    Kuo, B.-Y.4    Wang, W.-C.5
  • 8
    • 0033526409 scopus 로고    scopus 로고
    • Genetic manipulation to identify limiting steps and develop strategies for high-level expression of penicillin acylase in Escherichia coli
    • Chou, C. P.; Yu, C.-C.; Tseng, J.-H.; Lin, M.-I.; Lin, H.-K. Genetic manipulation to identify limiting steps and develop strategies for high-level expression of penicillin acylase in Escherichia coli. Biotechnol. Bioeng. 1999b, 63, 263-272.
    • (1999) Biotechnol. Bioeng. , vol.63 , pp. 263-272
    • Chou, C.P.1    Yu, C.-C.2    Tseng, J.-H.3    Lin, M.-I.4    Lin, H.-K.5
  • 9
    • 0027161270 scopus 로고
    • Preparation and storage of competent Escherichia coli cells
    • Chung, C. T.; Miller, R. H. Preparation and storage of competent Escherichia coli cells. Methods Enzymol. 1993, 218, 621-627.
    • (1993) Methods Enzymol. , vol.218 , pp. 621-627
    • Chung, C.T.1    Miller, R.H.2
  • 10
    • 4644285228 scopus 로고    scopus 로고
    • Protein folding in the cell: Reshaping the folding funnel
    • Clark, P. L. Protein folding in the cell: reshaping the folding funnel. Trends Biochem. Sci. 2004, 29, 527-534.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 527-534
    • Clark, P.L.1
  • 11
    • 4944246094 scopus 로고    scopus 로고
    • Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins
    • Ferbitz, L.; Maier, T.; Patzelt, H.; Bukau, B.; Deuerling, E.; Ban, N. Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins. Nature 2004, 431, 590-596.
    • (2004) Nature , vol.431 , pp. 590-596
    • Ferbitz, L.1    Maier, T.2    Patzelt, H.3    Bukau, B.4    Deuerling, E.5    Ban, N.6
  • 12
    • 0017259809 scopus 로고
    • Regulation of penicillin acylase in Escherichia coli by cyclic AMP
    • Gang, D. M.; Shaikh, K. Regulation of penicillin acylase in Escherichia coli by cyclic AMP. Biochim. Biophys. Acta 1976, 425, 110-114.
    • (1976) Biochim. Biophys. Acta , vol.425 , pp. 110-114
    • Gang, D.M.1    Shaikh, K.2
  • 13
    • 0037040541 scopus 로고    scopus 로고
    • Protein folding-Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl, F. U.; Hayer-Hartl, M. Protein folding-Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 2002, 295, 1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 14
    • 0031026329 scopus 로고    scopus 로고
    • Trigger factor associates with GroEl in vivo and promotes its binding to certain polypeptides
    • Kandror, O.; Sherman, M.; Moerschell, R.; Goldberg, A. L. Trigger factor associates with GroEl in vivo and promotes its binding to certain polypeptides. J. Biol. Chem. 1997, 272, 1730-1734.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1730-1734
    • Kandror, O.1    Sherman, M.2    Moerschell, R.3    Goldberg, A.L.4
  • 15
    • 0028849206 scopus 로고
    • Trigger factor is involved in GroEL-dependent protein degradation in Escherichia coli and promotes binding of GroEL to unfolded proteins
    • Kandror, O.; Sherman, M.; Rhode, M.; Goldberg, A. L. Trigger factor is involved in GroEL-dependent protein degradation in Escherichia coli and promotes binding of GroEL to unfolded proteins. EMBO J. 1995, 14, 6021-6027.
    • (1995) EMBO J. , vol.14 , pp. 6021-6027
    • Kandror, O.1    Sherman, M.2    Rhode, M.3    Goldberg, A.L.4
  • 16
  • 17
    • 0035919127 scopus 로고    scopus 로고
    • DegP coexpression minimizes inclusion body formation upon overproduction of recombinant penicillin acylase in Escherichia coli
    • Lin, W.-J.; Huang, S.-W.; Chou, C. P. DegP coexpression minimizes inclusion body formation upon overproduction of recombinant penicillin acylase in Escherichia coli. Biotechnol. Bioeng. 2001, 73, 484-492.
    • (2001) Biotechnol. Bioeng. , vol.73 , pp. 484-492
    • Lin, W.-J.1    Huang, S.-W.2    Chou, C.P.3
  • 18
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • Makrides, S. C. Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol. Rev. 1996, 60, 512-538.
    • (1996) Microbiol. Rev. , vol.60 , pp. 512-538
    • Makrides, S.C.1
  • 19
    • 0021027558 scopus 로고
    • Simple screening method for isolation of penicillin acylase-producing bacteria
    • Meevootisom, V.; Somsuk, P.; Prachaktam, R.; Flegel, T. W. Simple screening method for isolation of penicillin acylase-producing bacteria. Appl. Environ. Microbiol. 1983, 46, 1227-1229.
    • (1983) Appl. Environ. Microbiol. , vol.46 , pp. 1227-1229
    • Meevootisom, V.1    Somsuk, P.2    Prachaktam, R.3    Flegel, T.W.4
  • 20
    • 0034050548 scopus 로고    scopus 로고
    • Overexpression of trigger factor prevents aggregation of recombinant proteins in Escherichia coli
    • Nishihara, K.; Kanemori, M.; Yanagi, H.; Yura, T. Overexpression of trigger factor prevents aggregation of recombinant proteins in Escherichia coli. Appl. Environ. Microbiol. 2000, 66, 884-889.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 884-889
    • Nishihara, K.1    Kanemori, M.2    Yanagi, H.3    Yura, T.4
  • 21
    • 0038643369 scopus 로고    scopus 로고
    • Roles of DegP in prevention of protein misfolding in the periplasm upon overexpression of penicillin acylase in Escherichia coli
    • Pan, K.-L.; Hsiao, H.-C.; Weng, C.-L.; Wu, M.-S.; Chou, C. P. Roles of DegP in prevention of protein misfolding in the periplasm upon overexpression of penicillin acylase in Escherichia coli. J. Bacteriol. 2003, 185, 3020-3030.
    • (2003) J. Bacteriol. , vol.185 , pp. 3020-3030
    • Pan, K.-L.1    Hsiao, H.-C.2    Weng, C.-L.3    Wu, M.-S.4    Chou, C.P.5
  • 22
    • 0029019782 scopus 로고
    • An arabinose-inducible expression vector, pAR3, compatible with ColE1-derived plasmids
    • Perez-Perez, J.; Gutierrez, J. An arabinose-inducible expression vector, pAR3, compatible with ColE1-derived plasmids. Gene 1995, 158, 141-142.
    • (1995) Gene , vol.158 , pp. 141-142
    • Perez-Perez, J.1    Gutierrez, J.2
  • 24
    • 0028036517 scopus 로고
    • Periplasmic aggregation limits the proteolytic maturation of the Escherichia coli Penicillin G amidase Precursor polypeptide
    • Scherrer, S.; Robas, N.; Zouheiry, H.; Branlant, G.; Branlant, C. Periplasmic aggregation limits the proteolytic maturation of the Escherichia coli Penicillin G amidase Precursor polypeptide. Appl. Microbiol. Biotechnol. 1994, 42, 85-91.
    • (1994) Appl. Microbiol. Biotechnol. , vol.42 , pp. 85-91
    • Scherrer, S.1    Robas, N.2    Zouheiry, H.3    Branlant, G.4    Branlant, C.5
  • 25
    • 0037071907 scopus 로고    scopus 로고
    • Prevention and reversion of protein aggregation by molecular chaperones in the E. coli cytosol: Implications for their applicability in biotechnology
    • Schlieker, C.; Bukau, B.; Mogk, A. Prevention and reversion of protein aggregation by molecular chaperones in the E. coli cytosol: implications for their applicability in biotechnology. J. Biotechnol. 2002, 96, 13-21.
    • (2002) J. Biotechnol. , vol.96 , pp. 13-21
    • Schlieker, C.1    Bukau, B.2    Mogk, A.3
  • 26
    • 0000903228 scopus 로고
    • Penicillin acylase: Enzyme production and its application in the manufacture of 6-APA
    • Shewale, J. G.; Sivaraman, H. Penicillin acylase: Enzyme production and its application in the manufacture of 6-APA. Process Biochem. 1989, 24, 146-154.
    • (1989) Process Biochem. , vol.24 , pp. 146-154
    • Shewale, J.G.1    Sivaraman, H.2
  • 27
    • 3543148392 scopus 로고    scopus 로고
    • Improved beta-lactam acylases and their use as industrial biocatalysts
    • Sio, C. F.; Quax, W. J. Improved beta-lactam acylases and their use as industrial biocatalysts. Curr. Opin. Biotechnol. 2004, 15, 349-355.
    • (2004) Curr. Opin. Biotechnol. , vol.15 , pp. 349-355
    • Sio, C.F.1    Quax, W.J.2
  • 28
    • 0025100583 scopus 로고
    • Primary structure requirements for the maturation in vivo of penicillin acylase from Escherichia coli ATCC 11105
    • Sizmann, D.; Keilmann, C.; Bock, A. Primary structure requirements for the maturation in vivo of penicillin acylase from Escherichia coli ATCC 11105. Eur. J. Biochem. 1990, 192, 143-151.
    • (1990) Eur. J. Biochem. , vol.192 , pp. 143-151
    • Sizmann, D.1    Keilmann, C.2    Bock, A.3
  • 29
    • 0030916974 scopus 로고    scopus 로고
    • Localization and characterization of inclusion bodies in recombinant Escherichia coli cells overproducing penicillin G acylase
    • Sriubolmas, N.; Panbangred, W.; Sriurairatana, S.; Meevootisom, V. Localization and characterization of inclusion bodies in recombinant Escherichia coli cells overproducing penicillin G acylase. Appl. Microbiol. Biotechnol. 1997, 47, 373-378.
    • (1997) Appl. Microbiol. Biotechnol. , vol.47 , pp. 373-378
    • Sriubolmas, N.1    Panbangred, W.2    Sriurairatana, S.3    Meevootisom, V.4
  • 30
  • 31
    • 0031157025 scopus 로고    scopus 로고
    • Molecular chaperones, folding catalysts, and the recovery of active recombinant proteins from E. coli
    • Thomas, J. G.; Ayling, A.; Baneyx, F. Molecular chaperones, folding catalysts, and the recovery of active recombinant proteins from E. coli. Appl. Biochem. Biotechnol. 1997, 66, 197-238.
    • (1997) Appl. Biochem. Biotechnol. , vol.66 , pp. 197-238
    • Thomas, J.G.1    Ayling, A.2    Baneyx, F.3
  • 32
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H.; Staehelin, T.; Gordon, J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 1979, 76, 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 33
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C.; Vieira, J.; Messing, J. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 1985, 33, 103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.