메뉴 건너뛰기




Volumn 519, Issue 2, 2013, Pages 311-317

The effect of α-mating factor secretion signal mutations on recombinant protein expression in Pichia pastoris

Author keywords

Mating factor secretion signal; Pichia pastoris; Recombinant protein expression

Indexed keywords

AMINO ACID; HORSERADISH PEROXIDASE; RECOMBINANT PROTEIN;

EID: 84875579379     PISSN: 03781119     EISSN: 18790038     Source Type: Journal    
DOI: 10.1016/j.gene.2013.01.062     Document Type: Article
Times cited : (131)

References (33)
  • 1
    • 0033607149 scopus 로고    scopus 로고
    • A eukaryotic protein, NOP-1, binds retinal to form an archaeal rhodopsin-like photochemically reactive pigment
    • Bieszke J.A., Spudich E.N., Scott K.L., Borkovich K.A., Spudich J.L. A eukaryotic protein, NOP-1, binds retinal to form an archaeal rhodopsin-like photochemically reactive pigment. Biochemistry 1999, 38:14138-14145.
    • (1999) Biochemistry , vol.38 , pp. 14138-14145
    • Bieszke, J.A.1    Spudich, E.N.2    Scott, K.L.3    Borkovich, K.A.4    Spudich, J.L.5
  • 2
    • 0000372323 scopus 로고
    • Alpha-factor-directed synthesis and secretion of mature foreign proteins in Saccharomyces cerevisiae
    • Brake A.J., et al. Alpha-factor-directed synthesis and secretion of mature foreign proteins in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U. S. A. 1984, 81:4642-4646.
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 4642-4646
    • Brake, A.J.1
  • 3
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein expression in the methylotrophic yeast Pichia pastoris
    • Cereghino J.L., Cregg J.M. Heterologous protein expression in the methylotrophic yeast Pichia pastoris. FEMS Microbiol. Rev. 2000, 24:45-66.
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 45-66
    • Cereghino, J.L.1    Cregg, J.M.2
  • 4
    • 0026664312 scopus 로고
    • The pro-region of the yeast prepro-alpha-factor is essential for membrane translocation of human insulin-like growth factor 1 in vivo
    • Chaudhuri B., Steube K., Stephan C. The pro-region of the yeast prepro-alpha-factor is essential for membrane translocation of human insulin-like growth factor 1 in vivo. Eur. J. Biochem. 1992, 206:793-800.
    • (1992) Eur. J. Biochem. , vol.206 , pp. 793-800
    • Chaudhuri, B.1    Steube, K.2    Stephan, C.3
  • 5
    • 48449106792 scopus 로고    scopus 로고
    • The Jpred 3 secondary structure prediction server
    • Cole C., Barber J.D., Barton G.J. The Jpred 3 secondary structure prediction server. Nucleic Acids Res. 2008, 36:W197-W201.
    • (2008) Nucleic Acids Res. , vol.36
    • Cole, C.1    Barber, J.D.2    Barton, G.J.3
  • 6
    • 0025805188 scopus 로고
    • Role of the proregion in the production and secretion of the Yarrowia lipolytica alkaline extracellular protease
    • Fabre E., Nicaud J.M., Lopez M.C., Gaillardin C. Role of the proregion in the production and secretion of the Yarrowia lipolytica alkaline extracellular protease. J. Biol. Chem. 1991, 266:3782-3790.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3782-3790
    • Fabre, E.1    Nicaud, J.M.2    Lopez, M.C.3    Gaillardin, C.4
  • 7
    • 33748937555 scopus 로고    scopus 로고
    • The surprising complexity of signal sequences
    • Hegde R.S., Bernstein H.D. The surprising complexity of signal sequences. Trends Biochem. Sci. 2006, 31:563-571.
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 563-571
    • Hegde, R.S.1    Bernstein, H.D.2
  • 8
    • 84860769305 scopus 로고    scopus 로고
    • An amino acid packing code for α-helical structure and protein design
    • Joo H., Chavan A.G., Phan J., Day R., Tsai J. An amino acid packing code for α-helical structure and protein design. J. Mol. Biol. 2012, 419:234-254.
    • (2012) J. Mol. Biol. , vol.419 , pp. 234-254
    • Joo, H.1    Chavan, A.G.2    Phan, J.3    Day, R.4    Tsai, J.5
  • 9
    • 0023088363 scopus 로고
    • Many random sequences functionally replace the secretion signal sequence of yeast invertase
    • Kaiser C.A., Preuss D., Grisafi P., Botstein D. Many random sequences functionally replace the secretion signal sequence of yeast invertase. Science 1987, 235:312-317.
    • (1987) Science , vol.235 , pp. 312-317
    • Kaiser, C.A.1    Preuss, D.2    Grisafi, P.3    Botstein, D.4
  • 10
    • 0030005908 scopus 로고    scopus 로고
    • A removable spacer peptide in an alpha-factor-leader/insulin precursor fusion protein improves processing and concomitant yield of the insulin precursor in Saccharomyces cerevisiae
    • Kjeldsen T., et al. A removable spacer peptide in an alpha-factor-leader/insulin precursor fusion protein improves processing and concomitant yield of the insulin precursor in Saccharomyces cerevisiae. Gene 1996, 170:107-112.
    • (1996) Gene , vol.170 , pp. 107-112
    • Kjeldsen, T.1
  • 11
    • 0031127906 scopus 로고    scopus 로고
    • Synthetic leaders with potential BiP binding mediate high-yield secretion of correctly folded insulin precursors from Saccharomyces cerevisiae
    • Kjeldsen T., et al. Synthetic leaders with potential BiP binding mediate high-yield secretion of correctly folded insulin precursors from Saccharomyces cerevisiae. Protein Expr. Purif. 1997, 9:331-336.
    • (1997) Protein Expr. Purif. , vol.9 , pp. 331-336
    • Kjeldsen, T.1
  • 12
    • 84856790732 scopus 로고    scopus 로고
    • Recombinant protein expression in Pichia pastoris strains with an engineered methanol utilization pathway
    • Krainer F.W., Dietzsch C., Hajek T., Herwig C., Spadiut O., Glieder A. Recombinant protein expression in Pichia pastoris strains with an engineered methanol utilization pathway. Microb. Cell Fact. 2012, 11:22.
    • (2012) Microb. Cell Fact. , vol.11 , pp. 22
    • Krainer, F.W.1    Dietzsch, C.2    Hajek, T.3    Herwig, C.4    Spadiut, O.5    Glieder, A.6
  • 13
    • 0020365369 scopus 로고
    • Structure of a yeast pheromone gene (MF alpha): a putative alpha-factor precursor contains four tandem copies of mature alpha-factor
    • Kurjan J., Herskowitz I. Structure of a yeast pheromone gene (MF alpha): a putative alpha-factor precursor contains four tandem copies of mature alpha-factor. Cell 1982, 30:933-943.
    • (1982) Cell , vol.30 , pp. 933-943
    • Kurjan, J.1    Herskowitz, I.2
  • 14
    • 77951119205 scopus 로고    scopus 로고
    • Secretion and proteolysis of heterologous proteins fused to the Escherichia coli maltose binding protein in Pichia pastoris
    • Li Z., et al. Secretion and proteolysis of heterologous proteins fused to the Escherichia coli maltose binding protein in Pichia pastoris. Protein Expr. Purif. 2010, 72:113-124.
    • (2010) Protein Expr. Purif. , vol.72 , pp. 113-124
    • Li, Z.1
  • 15
    • 31344458747 scopus 로고    scopus 로고
    • Mxr1p, a key regulator of the methanol utilization pathway and peroxisomal genes in Pichia pastoris
    • Lin-Cereghino G.P., et al. Mxr1p, a key regulator of the methanol utilization pathway and peroxisomal genes in Pichia pastoris. Mol. Cell. Biol. 2006, 26:883-897.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 883-897
    • Lin-Cereghino, G.P.1
  • 16
    • 67650165167 scopus 로고    scopus 로고
    • Expression of protein in Pichia pastoris
    • Scion Publishing Limited, Oxfordshire, M. Dyson, Y. Durocher (Eds.)
    • Lin-Cereghino G.P., Leung W., Lin-Cereghino J. Expression of protein in Pichia pastoris. Expression Systems: Methods Express 2007, 123-145. Scion Publishing Limited, Oxfordshire. M. Dyson, Y. Durocher (Eds.).
    • (2007) Expression Systems: Methods Express , pp. 123-145
    • Lin-Cereghino, G.P.1    Leung, W.2    Lin-Cereghino, J.3
  • 17
    • 42549165096 scopus 로고    scopus 로고
    • Direct selection of Pichia pastoris expression strains using new G418 resistance vectors
    • Lin-Cereghino J., et al. Direct selection of Pichia pastoris expression strains using new G418 resistance vectors. Yeast 2008, 25:293-299.
    • (2008) Yeast , vol.25 , pp. 293-299
    • Lin-Cereghino, J.1
  • 18
    • 12344321400 scopus 로고    scopus 로고
    • Condensed protocol for competent cell preparation and transformation of the methylotrophic yeast Pichia pastoris
    • Lin-Cereghino J., et al. Condensed protocol for competent cell preparation and transformation of the methylotrophic yeast Pichia pastoris. Biotechniques 2005, 38:44-48.
    • (2005) Biotechniques , vol.38 , pp. 44-48
    • Lin-Cereghino, J.1
  • 19
    • 17244363998 scopus 로고    scopus 로고
    • Heterologous protein production using the Pichia pastoris expression system
    • Macauley-Patrick S., Fazenda M.L., McNeil B., Harvey L.M. Heterologous protein production using the Pichia pastoris expression system. Yeast 2005, 22:249-270.
    • (2005) Yeast , vol.22 , pp. 249-270
    • Macauley-Patrick, S.1    Fazenda, M.L.2    McNeil, B.3    Harvey, L.M.4
  • 20
    • 0034088553 scopus 로고    scopus 로고
    • Functional expression of horseradish peroxidase in Saccharomyces cerevisiae and Pichia pastoris
    • Morawski B., Lin Z., Cirino P., Joo H., Bandara G., Arnold F.H. Functional expression of horseradish peroxidase in Saccharomyces cerevisiae and Pichia pastoris. Protein Eng. 2000, 13:377-384.
    • (2000) Protein Eng. , vol.13 , pp. 377-384
    • Morawski, B.1    Lin, Z.2    Cirino, P.3    Joo, H.4    Bandara, G.5    Arnold, F.H.6
  • 21
    • 0036281211 scopus 로고    scopus 로고
    • Processing of gene expression data generated by quantitative real-time RT-PCR
    • (1376, 1378-9)
    • Muller P.Y., Janovjak H., Miserez A.R., Dobbie Z. Processing of gene expression data generated by quantitative real-time RT-PCR. Biotechniques 2002, 32:1372-1374. (1376, 1378-9).
    • (2002) Biotechniques , vol.32 , pp. 1372-1374
    • Muller, P.Y.1    Janovjak, H.2    Miserez, A.R.3    Dobbie, Z.4
  • 22
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-a visualization system for exploratory research and analysis
    • Pettersen E.F., et al. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 2004, 25:1605-1612.
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 23
    • 0033214215 scopus 로고    scopus 로고
    • Functional phytohemagglutinin (PHA) and Galanthus nivalis agglutinin (GNA) expressed in Pichia pastoris correct N-terminal processing and secretion of heterologous proteins expressed using the PHA-E signal peptide
    • Raemaekers R.J., de Muro L., Gatehouse J.A., Fordham-Skelton A.P. Functional phytohemagglutinin (PHA) and Galanthus nivalis agglutinin (GNA) expressed in Pichia pastoris correct N-terminal processing and secretion of heterologous proteins expressed using the PHA-E signal peptide. Eur. J. Biochem. 1999, 265:394-403.
    • (1999) Eur. J. Biochem. , vol.265 , pp. 394-403
    • Raemaekers, R.J.1    de Muro, L.2    Gatehouse, J.A.3    Fordham-Skelton, A.P.4
  • 24
    • 68149137106 scopus 로고    scopus 로고
    • Directed evolution of a secretory leader for the improved expression of heterologous proteins and full-length antibodies in Saccharomyces cerevisiae
    • Rakestraw J.A., Sazinsky S.L., Piatesi A., Antipov E., Wittrup K.D. Directed evolution of a secretory leader for the improved expression of heterologous proteins and full-length antibodies in Saccharomyces cerevisiae. Biotechnol. Bioeng. 2009, 103:1192-1201.
    • (2009) Biotechnol. Bioeng. , vol.103 , pp. 1192-1201
    • Rakestraw, J.A.1    Sazinsky, S.L.2    Piatesi, A.3    Antipov, E.4    Wittrup, K.D.5
  • 25
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 1993, 234:779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 27
    • 0021878793 scopus 로고
    • Heterologous protein secretion from yeast
    • Smith R.A., Duncan M.J., Moir D.T. Heterologous protein secretion from yeast. Science 1985, 229:1219-1224.
    • (1985) Science , vol.229 , pp. 1219-1224
    • Smith, R.A.1    Duncan, M.J.2    Moir, D.T.3
  • 28
    • 80052456858 scopus 로고    scopus 로고
    • Improving mammalian cell factories: the selection of signal peptide has major impact on recombinant protein synthesis and secretion in mammalian cells
    • Stern B., Olsen L., Trosse C., Ravneberg H., Pryme I. Improving mammalian cell factories: the selection of signal peptide has major impact on recombinant protein synthesis and secretion in mammalian cells. Trends Cell Mol. Biol. 2007, 2:1-17.
    • (2007) Trends Cell Mol. Biol. , vol.2 , pp. 1-17
    • Stern, B.1    Olsen, L.2    Trosse, C.3    Ravneberg, H.4    Pryme, I.5
  • 29
    • 21644484985 scopus 로고    scopus 로고
    • Cloning and characterization of the Pichia pastoris MET2 gene as a selectable marker
    • Thor D., et al. Cloning and characterization of the Pichia pastoris MET2 gene as a selectable marker. FEMS Yeast Res. 2005, 5:935-942.
    • (2005) FEMS Yeast Res. , vol.5 , pp. 935-942
    • Thor, D.1
  • 30
  • 31
    • 5444226007 scopus 로고    scopus 로고
    • Reliable high-throughput screening with Pichia pastoris by limiting yeast cell death phenomena
    • Weis R., Luiten R., Skranc W., Schwab H., Wubbolts M., Glieder A. Reliable high-throughput screening with Pichia pastoris by limiting yeast cell death phenomena. FEMS Yeast Res. 2004, 2:179-189.
    • (2004) FEMS Yeast Res. , vol.2 , pp. 179-189
    • Weis, R.1    Luiten, R.2    Skranc, W.3    Schwab, H.4    Wubbolts, M.5    Glieder, A.6
  • 32
  • 33
    • 0141817121 scopus 로고    scopus 로고
    • Improving tolerance of Candida antarctica lipase B towards irreversible thermal inactivation through directed evolution
    • Zhang N., Suen W.C., Windsor W., Xiao L., Madison V., Zaks A. Improving tolerance of Candida antarctica lipase B towards irreversible thermal inactivation through directed evolution. Protein Eng. 2003, 16:599-605.
    • (2003) Protein Eng. , vol.16 , pp. 599-605
    • Zhang, N.1    Suen, W.C.2    Windsor, W.3    Xiao, L.4    Madison, V.5    Zaks, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.