메뉴 건너뛰기




Volumn 82, Issue 1, 2012, Pages 116-124

Isolation of Metarhizium anisopliae carboxypeptidase A with native disulfide bonds from the cytosol of Escherichia coli BL21(DE3)

Author keywords

Carboxypeptidase; DsbA; DsbC; gor; His tag; Maltose binding protein; MeCPA; Polyhistidine tag; Protein disulfide isomerase; Thermolysin; trxB

Indexed keywords

CARBOXYPEPTIDASE A; DISULFIDE; ESCHERICHIA COLI PROTEIN; HYBRID PROTEIN; MALTOSE BINDING PROTEIN;

EID: 84855487625     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2011.11.015     Document Type: Article
Times cited : (11)

References (38)
  • 1
    • 33646857665 scopus 로고    scopus 로고
    • Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins
    • DOI 10.1016/j.pep.2005.12.002, PII S1046592805004262
    • J. Arnau, C. Lauritzen, G.E. Petersen, and J. Pedersen Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins Protein Expr. Purif. 48 2006 1 13 (Pubitemid 43782626)
    • (2006) Protein Expression and Purification , vol.48 , Issue.1 , pp. 1-13
    • Arnau, J.1    Lauritzen, C.2    Petersen, G.E.3    Pedersen, J.4
  • 2
    • 0037255597 scopus 로고    scopus 로고
    • Overview of tag protein fusions: From molecular and biochemical fundamentals to commercial systems
    • K. Terpe Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems Appl. Microbiol. Biotechnol. 60 2003 523 533 (Pubitemid 36169526)
    • (2003) Applied Microbiology and Biotechnology , vol.60 , Issue.5 , pp. 523-533
    • Terpe, K.1
  • 3
    • 19444373996 scopus 로고    scopus 로고
    • Making the most of affinity tags
    • DOI 10.1016/j.tibtech.2005.03.012, PII S0167779905000843
    • D.S. Waugh Making the most of affinity tags Trends Biotechnol. 23 2005 316 320 (Pubitemid 40726273)
    • (2005) Trends in Biotechnology , vol.23 , Issue.6 , pp. 316-320
    • Waugh, D.S.1
  • 4
    • 60549102431 scopus 로고    scopus 로고
    • Efficient cleavage of problematic tobacco etch virus (TEV)-protein arginine methyltransferase constructs
    • B.B. Sun-Lailam, and J.M. Hevel Efficient cleavage of problematic tobacco etch virus (TEV)-protein arginine methyltransferase constructs Anal. Biochem. 387 2009 130 132
    • (2009) Anal. Biochem. , vol.387 , pp. 130-132
    • Sun-Lailam, B.B.1    Hevel, J.M.2
  • 5
    • 0033255928 scopus 로고    scopus 로고
    • 6)-tag dependent protein dimerization: A cautionary tale
    • J. Wu, and M. Filutowicz Hexahistidine (His6)-tag dependent protein dimerization: a cautionary tale Acta Biochim. Pol. 46 1999 591 599 (Pubitemid 129537278)
    • (1999) Acta Biochimica Polonica , vol.46 , Issue.3 , pp. 591-599
    • Wu, J.1    Filutowicz, M.2
  • 6
    • 3543050105 scopus 로고    scopus 로고
    • His tag effect on solubility of human proteins produced in Escherichia coli: A comparison between four expression vectors
    • DOI 10.1023/B:jsfg.0000031965.37625.0e
    • E.A. Woestenenk, and M. Hammarström S. van den Berg, T. Härd, H. Berglund, His tag effect on solubility of human proteins produced in Escherichia coli: a comparison between four expression vectors J. Struct. Funct. Genom. 5 2004 217 229 (Pubitemid 39030613)
    • (2004) Journal of Structural and Functional Genomics , vol.5 , Issue.3 , pp. 217-229
    • Woestenenk, E.A.1    Hammarstrom, M.2    Van Den Berg, S.3    Hard, T.4    Berglund, H.5
  • 7
    • 11844272620 scopus 로고    scopus 로고
    • Attachment of a histidine tag to the minimal zinc finger protein of the Aspergillus nidulans gene regulatory protein AreA causes a conformational change at the DNA-binding site
    • DOI 10.1016/j.pep.2004.10.017, PII S1046592804003547
    • A. Chant, C.M. Kraemer-Pecore, R. Watkin, and G.G. Kneale Attachment of a histidine tag to the minimal zinc finger protein of the Aspergillus nidulans gene regulatory protein AreA causes a conformational change at the DNA-binding site Protein Expr. Purif. 39 2005 152 159 (Pubitemid 40084600)
    • (2005) Protein Expression and Purification , vol.39 , Issue.2 , pp. 152-159
    • Chant, A.1    Kraemer-Pecore, C.M.2    Watkin, R.3    Kneale, G.G.4
  • 10
    • 0032793248 scopus 로고    scopus 로고
    • Histidines in affinity tags and surface clusters for immobilized metal-ion affinity chromatography of trimeric tumor necrosis factor α
    • DOI 10.1016/S0021-9673(99)00374-X, PII S002196739900374X
    • V. Gaberc-Porekar, V. Menart, S. Jevsevar, A. Vidensek, and A. Stalc Histidines in affinity tags and surface clusters for immobilized metal-ion affinity chromatography of trimeric tumor necrosis factor alpha J. Chromatogr. A 852 1999 117 128 (Pubitemid 29347063)
    • (1999) Journal of Chromatography A , vol.852 , Issue.1 , pp. 117-128
    • Gaberc-Porekar, V.1    Menart, V.2    Jevsevar, S.3    Vidensek, A.4    Stalc, A.5
  • 11
    • 77955773733 scopus 로고    scopus 로고
    • Heterologous expression and N-terminal His-tagging processes affect the catalytic properties of staphylococcal lipases: A monolayer study
    • H. Horchani, L. Sabrina, L. Régine, A. Sayari, Y. Gargouri, and R. Verger Heterologous expression and N-terminal His-tagging processes affect the catalytic properties of staphylococcal lipases: a monolayer study J. Colloid Interface Sci. 350 2010 586 594
    • (2010) J. Colloid Interface Sci. , vol.350 , pp. 586-594
    • Horchani, H.1    Sabrina, L.2    Régine, L.3    Sayari, A.4    Gargouri, Y.5    Verger, R.6
  • 13
    • 44949196798 scopus 로고    scopus 로고
    • Protein structure modeling indicates hexahistidine-tag interference with enzyme activity
    • DOI 10.1002/prot.21905
    • A.C. Freydank, W. Brandt, and B. Drager Protein structure modeling indicates hexahistidine-tag interference with enzyme activity Proteins 72 2008 173 183 (Pubitemid 351809156)
    • (2008) Proteins: Structure, Function and Genetics , vol.72 , Issue.1 , pp. 173-183
    • Freydank, A.-C.1    Brandt, W.2    Drager, B.3
  • 14
    • 40849085149 scopus 로고    scopus 로고
    • Effect of location of the His-tag on the production of soluble and functional Buthus martensii Karsch insect toxin
    • C.G. Xu, X.J. Fan, Y.J. Fu, and A.H. Liang Effect of location of the His-tag on the production of soluble and functional Buthus martensii Karsch insect toxin Protein Expr. Purif. 59 2008 103 109
    • (2008) Protein Expr. Purif. , vol.59 , pp. 103-109
    • Xu, C.G.1    Fan, X.J.2    Fu, Y.J.3    Liang, A.H.4
  • 15
    • 4344563213 scopus 로고    scopus 로고
    • Hexa-histidin tag position influences disulfide structure but not binding behavior of in vitro folded N-terminal domain of rat corticotropin-releasing factor receptor type 2a
    • DOI 10.1110/ps.04835904
    • J. Klose, N. Wendt, S. Kubald, E. Krause, K. Fechner, M. Beyermann, M. Bienert, R. Rudolph, and S. Rothemund Hexa-histidine tag position influences disulfide structure but not binding behavior of in vitro folded N-terminal domain of rat corticotropin-releasing factor receptor type 2a Protein Sci. 13 2004 2470 2475 (Pubitemid 39128867)
    • (2004) Protein Science , vol.13 , Issue.9 , pp. 2470-2475
    • Klose, J.1    Wendt, N.2    Kubald, S.3    Krause, E.4    Fechner, K.5    Beyermann, M.6    Bienert, M.7    Rudolph, R.8    Rothemund, S.9
  • 16
    • 80054052318 scopus 로고    scopus 로고
    • An overview of reagents for the removal of affinity tags
    • D.S. Waugh An overview of reagents for the removal of affinity tags Protein Expr. Purif. 80 2011 283 293
    • (2011) Protein Expr. Purif. , vol.80 , pp. 283-293
    • Waugh, D.S.1
  • 17
    • 79951959644 scopus 로고    scopus 로고
    • The substrate specificity of Metarhizium anisopliae and Bos taurus carboxypeptidases A: Insights into their use as tools for the removal of affinity tags
    • B.P. Austin, J. Tözsér, P. Bagossi, J.E. Tropea, and D.S. Waugh The substrate specificity of Metarhizium anisopliae and Bos taurus carboxypeptidases A: insights into their use as tools for the removal of affinity tags Protein Expr. Purif. 77 2011 53 61
    • (2011) Protein Expr. Purif. , vol.77 , pp. 53-61
    • Austin, B.P.1    Tözsér, J.2    Bagossi, P.3    Tropea, J.E.4    Waugh, D.S.5
  • 18
    • 0024297282 scopus 로고
    • A novel rat carboxypeptidase, CPA2: Characterization, molecular cloning and evolutionary implications on substrate specificity in the carboxypeptidase gene family
    • S.J. Gardell, C.S. Craik, E. Clauser, E.J. Goldsmith, C.-B. Stewart, M. Graf, and W.J. Rutter A novel rat carboxypeptidase, CPA2: characterization, molecular cloning and evolutionary implications on substrate specificity in the carboxypeptidase gene family J. Biol. Chem. 263 1988 17828 17836
    • (1988) J. Biol. Chem. , vol.263 , pp. 17828-17836
    • Gardell, S.J.1    Craik, C.S.2    Clauser, E.3    Goldsmith, E.J.4    Stewart, C.-B.5    Graf, M.6    Rutter, W.J.7
  • 19
    • 0037208811 scopus 로고    scopus 로고
    • Maltose-binding protein as a solubility enhancer
    • J.D. Fox, and D.S. Waugh Maltose-binding protein as a solubility enhancer Methods Mol. Biol. 205 2003 99 117
    • (2003) Methods Mol. Biol. , vol.205 , pp. 99-117
    • Fox, J.D.1    Waugh, D.S.2
  • 20
    • 0031453002 scopus 로고    scopus 로고
    • Balancing the production of two recombinant proteins in Escherichia coli by manipulating plasmid copy number: High-level expression of heterodimeric ras farnesyltransferase
    • DOI 10.1006/prep.1997.0794
    • K.L. Tsao, and D.S. Waugh Balancing the production of two recombinant proteins in Escherichia coli by manipulating plasmid copy number: high-level expression of heterodimeric Ras farnesyltransferase Protein Expr. Purif. 11 1997 233 240 (Pubitemid 28014095)
    • (1997) Protein Expression and Purification , vol.11 , Issue.3 , pp. 233-240
    • Tsao, K.-L.1    Waugh, D.S.2
  • 21
    • 0029872080 scopus 로고    scopus 로고
    • A versatile plasmid expression vector for the production of biotinylated proteins by site-specific, enzymatic modification in Escherichia coli
    • DOI 10.1016/0378-1119(95)00762-8
    • K.L. Tsao, B. DeBarbieri, H. Michel, and D.S. Waugh A versatile plasmid expression vector for the production of biotinylated proteins by site-specific, enzymatic modification in Escherichia coli Gene 169 1996 59 64 (Pubitemid 26076614)
    • (1996) Gene , vol.169 , Issue.1 , pp. 59-64
    • Tsao, K.-L.1    DeBarbieri, B.2    Michel, H.3    Waugh, D.S.4
  • 22
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • DOI 10.1016/0378-1119(89)90358-2
    • S.N. Ho, H.D. Hunt, R.M. Horton, J.K. Pullen, and L.R. Pease Site-directed mutagenesis by overlap extension using the polymerase chain reaction Gene 77 1989 51 59 (Pubitemid 19125653)
    • (1989) Gene , vol.77 , Issue.1 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 23
    • 0020460249 scopus 로고
    • A unique activity assay for carboxypeptidase A in human serum
    • DOI 10.1016/0003-2697(82)90024-0
    • L.M. Peterson, B. Holmquist, and J.L. Bethune A unique activity assay for carboxypeptidase A in human serum Anal. Biochem. 125 1982 420 426 (Pubitemid 13219790)
    • (1982) Analytical Biochemistry , vol.125 , Issue.2 , pp. 420-426
    • Peterson, L.M.1    Holmquist, B.2    Bethune, J.L.3
  • 24
    • 0033515653 scopus 로고    scopus 로고
    • Cloning, expression, and substrate specificity of MeCPA, a zinc carboxypeptidase that is secreted into infected tissues by the fungal entomopathogen Metarhizium anisopliae
    • L. Joshi, and R.J. St Leger Cloning, expression, and substrate specificity of MeCPA, a zinc carboxypeptidase that is secreted into infected tissues by the fungal entomopathogen Metarhizium anisopliae J. Biol. Chem. 274 1999 9803 9811
    • (1999) J. Biol. Chem. , vol.274 , pp. 9803-9811
    • Joshi, L.1    St Leger, R.J.2
  • 25
    • 0025283867 scopus 로고
    • Use of T7 RNA polymerase to direct expression of cloned genes
    • DOI 10.1016/0076-6879(90)85008-C
    • F.W. Studier, A.H. Rosenberg, J.J. Dunn, and J.W. Dubendorf Use of T7 RNA polymerase to direct expression of cloned genes Methods Enzymol. 185 1990 60 89 (Pubitemid 20219811)
    • (1990) Methods in Enzymology , vol.185 , pp. 60-89
    • Studier, F.W.1    Rosenberg, A.H.2    Dunn, J.J.3    Dubendorff, J.W.4
  • 26
    • 0030941829 scopus 로고    scopus 로고
    • The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm
    • DOI 10.1074/jbc.272.25.15661
    • W.A. Prinz, F. Ashlund, A. Holmgren, and J. Beckwith The role of thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm J. Biol. Chem. 272 1997 15661 15667 (Pubitemid 27265536)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.25 , pp. 15661-15667
    • Prinz, W.A.1    Aslund, F.2    Holmgren, A.3    Beckwith, J.4
  • 27
    • 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. U.S.A. 96 1999 13703 13708
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 13703-13708
    • Bessette, P.H.1    Aslund, F.2    Beckwith, J.3    Georgiou, G.4
  • 28
    • 0029994544 scopus 로고    scopus 로고
    • Role of the prodomain in folding and secretion of rat pancreatic carboxypeptidase A1
    • DOI 10.1021/bi960113o
    • M.A. Phillips, and W.J. Rutter Role of the prodomain in folding and secretion of rat pancreatic carboxypeptidase A1 Biochemistry 35 1996 6771 6776 (Pubitemid 26172436)
    • (1996) Biochemistry , vol.35 , Issue.21 , pp. 6771-6776
    • Phillips, M.A.1    Rutter, W.J.2
  • 29
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • R.B. Kapust, and D.S. Waugh Escherichia coli malotose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused Protein Sci. 8 1999 1668 1674 (Pubitemid 29379949)
    • (1999) Protein Science , vol.8 , Issue.8 , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 32
    • 78651484550 scopus 로고    scopus 로고
    • Disruption of reducing pathways is not essential for efficient disulfide bond formation in the cytoplasm of E. Coli
    • F. Hatahet, V.D. Nguyen, K.E.H. Salo, and L.W. Ruddock Disruption of reducing pathways is not essential for efficient disulfide bond formation in the cytoplasm of E. Coli Microb. Cell Fact. 9 2010 67
    • (2010) Microb. Cell Fact. , vol.9 , pp. 67
    • Hatahet, F.1    Nguyen, V.D.2    Salo, K.E.H.3    Ruddock, L.W.4
  • 34
    • 0034956228 scopus 로고    scopus 로고
    • A strategy for optimizing the monodispersity of fusion proteins: Application to purification of recombinant HPV E6 oncoprotein
    • Y. Nominé, T. Ristriani, C. Laurent, J.F. Lefvre, E. Weiss, and G. Travé A strategy for opttimizing the monodispersity of fusion proteins: application to purification of recombinant HPV E6 oncoprotein Protein Eng. 14 2001 297 305 (Pubitemid 32587276)
    • (2001) Protein Engineering , vol.14 , Issue.4 , pp. 297-305
    • Nomine, Y.1    Ristriani, T.2    Laurent, C.3    Lefevre, J.-F.4    Weiss, E.5    Trave, G.6
  • 36
    • 77449143169 scopus 로고    scopus 로고
    • Purifying natively folded proteins from inclusion bodies using sarkosyl, Triton X-100, and CHAPS
    • H. Tao, W. Liu, B.N. Simmons, H.K. Harris, T.C. Cox, and M.A. Massiah Purifying natively folded proteins from inclusion bodies using sarkosyl, Triton X-100, and CHAPS Biotechniques 48 2010 61 64
    • (2010) Biotechniques , vol.48 , pp. 61-64
    • Tao, H.1    Liu, W.2    Simmons, B.N.3    Harris, H.K.4    Cox, T.C.5    Massiah, M.A.6
  • 37
    • 79956055874 scopus 로고    scopus 로고
    • Improved recovery of active GST-fusion proteins from insoluble aggregates: Solubilization and purification conditions using PKM2 and HtrA2 as model proteins
    • D.W. Park, S.S. Kim, M.K. Nam, G.Y. Kim, J. Kim, and H. Rhim Improved recovery of active GST-fusion proteins from insoluble aggregates: solubilization and purification conditions using PKM2 and HtrA2 as model proteins BMB Rep. 44 2011 279 284
    • (2011) BMB Rep. , vol.44 , pp. 279-284
    • Park, D.W.1    Kim, S.S.2    Nam, M.K.3    Kim, G.Y.4    Kim, J.5    Rhim, H.6
  • 38
    • 78650965365 scopus 로고    scopus 로고
    • Pre-expression of a sylfhydryl oxidase significantly increases the yields of eukaryotic disulfide bond containing proteins expressed in the cytoplasm of E. Coli
    • V.D. Nguyen, F. Hatahet, K.E.H. Salo, E. Enlund, C. Zhang, and L.W. Ruddock Pre-expression of a sylfhydryl oxidase significantly increases the yields of eukaryotic disulfide bond containing proteins expressed in the cytoplasm of E. Coli Microb. Cell Fact. 10 2011 1
    • (2011) Microb. Cell Fact. , vol.10 , pp. 1
    • Nguyen, V.D.1    Hatahet, F.2    Salo, K.E.H.3    Enlund, E.4    Zhang, C.5    Ruddock, L.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.