메뉴 건너뛰기




Volumn 16, Issue 22, 1997, Pages 6702-6712

Assembly of human prolyl 4-hydroxylase and type III collagen in the yeast Pichia pastoris: Formation of a stable enzyme tetramer requires coexpression with collagen and assembly of a stable collagen requires coexpression with prolyl 4-hydroxylase

Author keywords

Chaperone; Collagen; Expression; Prolyl 4 hydroxylase; Yeast

Indexed keywords

COLLAGEN TYPE 3; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; PROTEIN DISULFIDE ISOMERASE; RECOMBINANT ENZYME; TETRAMER;

EID: 0030732364     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.22.6702     Document Type: Article
Times cited : (141)

References (45)
  • 3
    • 0019062019 scopus 로고
    • The assembly of tetrameric prolyl hydroxylase in tendon fibroblasts from newly synthesized α-subunits and from preformed cross-reacting protein
    • Berg,R.A., Kao,W.W.-Y. and Kedersha,N.L. (1980) The assembly of tetrameric prolyl hydroxylase in tendon fibroblasts from newly synthesized α-subunits and from preformed cross-reacting protein. Biochem. J., 189, 491-199.
    • (1980) Biochem. J. , vol.189 , pp. 491-1199
    • Berg, R.A.1    Kao, W.W.-Y.2    Kedersha, N.L.3
  • 4
    • 0019880195 scopus 로고
    • Proteolytic enzymes as probes for the triple-helical conformation of procollagen
    • Bruckner,P. and Prockop,D.J. (1981) Proteolytic enzymes as probes for the triple-helical conformation of procollagen. Anal. Biochem., 110. 360-368.
    • (1981) Anal. Biochem. , vol.110 , pp. 360-368
    • Bruckner, P.1    Prockop, D.J.2
  • 5
    • 15444377148 scopus 로고
    • Yeast systems for the commercial production of helerologous proteins
    • Buckholz,R.G. and Gleeson,M.A. (1991) Yeast systems for the commercial production of helerologous proteins. Biotechnolgy, 9, 1067-1072.
    • (1991) Biotechnolgy , vol.9 , pp. 1067-1072
    • Buckholz, R.G.1    Gleeson, M.A.2
  • 6
    • 0029893377 scopus 로고    scopus 로고
    • Type-III procollagen assembly in semi-intact cells: Chain association, nucieation and triple-helix folding do not require formation of inter-chain disulphide bonds but triple-helix nuclealion does require hydroxylation
    • Bulleid,N.J., Wilson,R. and Lees,J.F. (1996) Type-III procollagen assembly in semi-intact cells: chain association, nucieation and triple-helix folding do not require formation of inter-chain disulphide bonds but triple-helix nuclealion does require hydroxylation. Biochem. J., 317, 195-202.
    • (1996) Biochem. J. , vol.317 , pp. 195-202
    • Bulleid, N.J.1    Wilson, R.2    Lees, J.F.3
  • 7
    • 0017046982 scopus 로고
    • In vivo labeling and turnover of prolyl hydroxylase and a related immunoreactive protein
    • Chichester III,C.O., Fuller,G.C. and Cardinale,G.J. (1976) In vivo labeling and turnover of prolyl hydroxylase and a related immunoreactive protein. Biochem. Biophys. Res. Commun., 73, 1056-1062.
    • (1976) Biochem. Biophys. Res. Commun. , vol.73 , pp. 1056-1062
    • Chichester III, C.O.1    Fuller, G.C.2    Cardinale, G.J.3
  • 9
    • 14744299579 scopus 로고
    • Recent advances in the expression of foreign genes in Pichia pastoris
    • Cregg,J.M., Vedvick,T.S. and Raschke,W.C. (1993) Recent advances in the expression of foreign genes in Pichia pastoris. Biotechnology, 11, 905-910.
    • (1993) Biotechnology , vol.11 , pp. 905-910
    • Cregg, J.M.1    Vedvick, T.S.2    Raschke, W.C.3
  • 10
    • 0021774436 scopus 로고
    • Stoichiometry and kinetics of the prolyl 4-hydroxylase partial reaction
    • de Jong,I., and Kemp,A. (1984) Stoichiometry and kinetics of the prolyl 4-hydroxylase partial reaction. Biochem. Biophys. 787, 105-111.
    • (1984) Biochem. Biophys. , vol.787 , pp. 105-111
    • De Jong, I.1    Kemp, A.2
  • 11
    • 0027959156 scopus 로고
    • Protein disulphideisomerase: Building bridges in protein folding
    • Freedman,R.B., Hirst,T.R. and Tuite,M.K (1994) Protein disulphideisomerase: building bridges in protein folding. Trends Biochem. Sci., 19, 331-336.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 331-336
    • Freedman, R.B.1    Hirst, T.R.2    Tuite, M.K.3
  • 13
    • 0020620967 scopus 로고
    • The association between prolyl hydroxylase metabolism and cell growth in cultured L-929 fibroblasts
    • Hehda,P.A., Ebert,J., Chou,K.-L.L., Shields,M. and Kao,W.W.-Y. (1983) The association between prolyl hydroxylase metabolism and cell growth in cultured L-929 fibroblasts. Biochem. Biophys. Acta. 758. 128-134.
    • (1983) Biochem. Biophys. Acta. , vol.758 , pp. 128-134
    • Hehda, P.A.1    Ebert, J.2    Chou, K.-L.L.3    Shields, M.4    Kao, W.W.-Y.5
  • 14
    • 0008363155 scopus 로고
    • Molecular cloning of the α-subunii of human prolyl 4-hydroxylase: The complete cDNA-derivcd amino acid sequence and evidence for alternative splicing of RNA transcripts
    • Helaakoski,T., Vuori,K., Myllylä.R., Kivirikko,K.I. and Pihlajaniemi,T. (1989) Molecular cloning of the α-subunii of human prolyl 4-hydroxylase: The complete cDNA-derivcd amino acid sequence and evidence for alternative splicing of RNA transcripts. Proc. Natl Acad. Sci. USA. 86. 4392-4396.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 4392-4396
    • Helaakoski, T.1    Vuori, K.2    Myllylä, R.3    Kivirikko, K.I.4    Pihlajaniemi, T.5
  • 16
    • 0029795764 scopus 로고    scopus 로고
    • Intracellular dissociation and reassembly of prolyl 4-hydroxylase: The α-suhunits associate with the immunoglobulin-heavy-chain binding protein (BiP) allowing reassembly with the β'-subunit
    • John,D.C.A. and Bulleid,N.J. (1996) Intracellular dissociation and reassembly of prolyl 4-hydroxylase: the α-suhunits associate with the immunoglobulin-heavy-chain binding protein (BiP) allowing reassembly with the β'-subunit. Biochem. J., 317, 659-665.
    • (1996) Biochem. J. , vol.317 , pp. 659-665
    • John, D.C.A.1    Bulleid, N.J.2
  • 17
    • 0027415488 scopus 로고
    • Cell-tree synthesis and assembly of prolyl 4-hydroxylase: The role of the β-subunit (PDI) in preventing misfolding and aggregation of the α-suhunit
    • John,D.C.A., Gram,M.E. and Bulleid,N.J. (1993) Cell-tree synthesis and assembly of prolyl 4-hydroxylase: the role of the β-subunit (PDI) in preventing misfolding and aggregation of the α-suhunit. EMBO J., 12. 1587-1595.
    • (1993) EMBO J. , vol.12 , pp. 1587-1595
    • John, D.C.A.1    Gram, M.E.2    Bulleid, N.J.3
  • 19
    • 0020010503 scopus 로고
    • Posttranslational enzymes in the biosynthesis of collagen: Intraccllular enzymes
    • Kivirikko,K.I. and Myllylä.R. (1982) Posttranslational enzymes in the biosynthesis of collagen: Intraccllular enzymes. Methods Enzymol., 82, 245-304.
    • (1982) Methods Enzymol. , vol.82 , pp. 245-304
    • Kivirikko, K.I.1    Myllylä, R.2
  • 20
    • 0023081149 scopus 로고
    • Recent developments in posttranslational modification: Intracellular processing
    • Kivirikko,K.I. and Myllylä.R. (1987) Recent developments in posttranslational modification: Intracellular processing. Methods Enzymol., 144, 96-114.
    • (1987) Methods Enzymol. , vol.144 , pp. 96-114
    • Kivirikko, K.I.1    Myllylä, R.2
  • 21
    • 0024639221 scopus 로고
    • Protein hydroxylation: Prolyl 14-hydroxylase an enzyme with four cosubstrates and a multifunctional subunit
    • Kivirikko,K.I., Myllylä,R. and Pihlajaniemi,T. (1989) Protein hydroxylation: prolyl 14-hydroxylase an enzyme with four cosubstrates and a multifunctional subunit.FASEB J., 3, 1609-1617.
    • (1989) FASEB J. , vol.3 , pp. 1609-1617
    • Kivirikko, K.I.1    Myllylä, R.2    Pihlajaniemi, T.3
  • 22
    • 0002079883 scopus 로고
    • Hydroxylalion of proline and lysine residues in collagens and other animal and plant proteins
    • Harding,J.J. and Crabbe,M.J.C. (eds). CRC Press. Boca Raton. FL
    • Kivirikko,K.I., MyllyläR. and Pihlajaniemi,T. (1992) Hydroxylalion of proline and lysine residues in collagens and other animal and plant proteins. In Harding,J.J. and Crabbe,M.J.C. (eds). Post-translational Modifications of Proteins. CRC Press. Boca Raton. FL, pp. 1-51.
    • (1992) Post-translational Modifications of Proteins , pp. 1-51
    • Kivirikko, K.I.1    Myllylä, R.2    Pihlajaniemi, T.3
  • 23
    • 0023654667 scopus 로고
    • A single polypeptide acts both as the β subunit of prolyl 4-hydroxylase and as a protein disultide-isomerase
    • Koivu,J., Myllylä.R., Helaakoski,T., Pihlajaniemi,T., Tasanen,K. and Kivirikko,K.I. (1987) A single polypeptide acts both as the β subunit of prolyl 4-hydroxylase and as a protein disultide-isomerase. J. Biol. Chem., 262, 6447-6449.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6447-6449
    • Koivu, J.1    Myllylä, R.2    Helaakoski, T.3    Pihlajaniemi, T.4    Tasanen, K.5    Kivirikko, K.I.6
  • 24
    • 0029940986 scopus 로고    scopus 로고
    • Characterization of human type III collagen expressed in a baculovirus system. Production of a protein with a stable triple helix requires coexpression with the two types of recombinant prolyl 4-hydroxylase subunit
    • Lamberg,A., Helaakoski,T., Myllyharju,J., Peltonen,S., Notbohm,H., Pihlajaniemi,T. and Kivirikko,K.I. (1996) Characterization of human type III collagen expressed in a baculovirus system. Production of a protein with a stable triple helix requires coexpression with the two types of recombinant prolyl 4-hydroxylase subunit. J. Biol. Chem., 271, 11988-11995.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11988-11995
    • Lamberg, A.1    Helaakoski, T.2    Myllyharju, J.3    Peltonen, S.4    Notbohm, H.5    Pihlajaniemi, T.6    Kivirikko, K.I.7
  • 25
    • 0018378307 scopus 로고
    • Turnover of prolyl hydroxylase tetramers and the monomersize protein in chick-embryo cartilaginous bone and lung in vivo
    • Majamaa,K., Kuutti-Savolainen,E.R., Tuderman,L. and Kivirikko,K.I. (1979) Turnover of prolyl hydroxylase tetramers and the monomersize protein in chick-embryo cartilaginous bone and lung in vivo. Biochem. J., 178, 313-322.
    • (1979) Biochem. J. , vol.178 , pp. 313-322
    • Majamaa, K.1    Kuutti-Savolainen, E.R.2    Tuderman, L.3    Kivirikko, K.I.4
  • 26
    • 0027682593 scopus 로고
    • New members of collagen superfamily
    • Mayne,R. and Brewton,R.G. (1993) New members of collagen superfamily. Curr. Opin. Cell Biol., 5, 883-890.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 883-890
    • Mayne, R.1    Brewton, R.G.2
  • 27
    • 0017742181 scopus 로고
    • Mechanism of the prolyl hydroxylasc reaction. 2. Kinetic analysis of the reaction sequence
    • Myllylä,R., Tuderman,L. and Kivirikko,K.I. (1977) Mechanism of the prolyl hydroxylasc reaction. 2. Kinetic analysis of the reaction sequence. Eur. J. Biochem., 80, 349-357.
    • (1977) Eur. J. Biochem. , vol.80 , pp. 349-357
    • Myllylä, R.1    Tuderman, L.2    Kivirikko, K.I.3
  • 28
    • 0021329173 scopus 로고
    • Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase
    • Myllylä,R., Majamaa,K., Günzler,V., Hanauske-Abel,H.M. and Kivirikko,K.I. (1984) Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase. J. Biol. Chem., 259, 5403-5405.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5403-5405
    • Myllylä, R.1    Majamaa, K.2    Günzler, V.3    Hanauske-Abel, H.M.4    Kivirikko, K.I.5
  • 29
    • 33646286416 scopus 로고    scopus 로고
    • Hsp47: A collagen-specific molecular chaperone
    • Nagata,K. (1996) Hsp47: a collagen-specific molecular chaperone. Trends Biochem. Sci., 21, 23-26.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 23-26
    • Nagata, K.1
  • 30
    • 0025225456 scopus 로고
    • The retention signal for soluble proteins of the endoplasmic reticulum
    • Pelham,H.R.B. (1990) The retention signal for soluble proteins of the endoplasmic reticulum. Trends Biochem. Sci., 15, 483-486.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 483-486
    • Pelham, H.R.B.1
  • 31
    • 0029158843 scopus 로고
    • Two new collagen subgroups: Membrane-associated collagens and types XV and XVIII
    • Pihlajaniemi,T. and Rehn,M. (1995) Two new collagen subgroups: Membrane-associated collagens and types XV and XVIII. Progr. Nucl. Acid Res. Mol. Biol., 50, 225-262.
    • (1995) Progr. Nucl. Acid Res. Mol. Biol. , vol.50 , pp. 225-262
    • Pihlajaniemi, T.1    Rehn, M.2
  • 32
    • 0023303619 scopus 로고
    • Molecular cloning of the β-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene
    • Pihlajaniemi,T., Helaakoski,T., Tasanen,K., Myllylä,R., Huhtala,M.-L., Koivu,J. and Kivirikko,K.I. (1987) Molecular cloning of the β-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene. EMBO J., 6, 643-649.
    • (1987) EMBO J. , vol.6 , pp. 643-649
    • Pihlajaniemi, T.1    Helaakoski, T.2    Tasanen, K.3    Myllylä, R.4    Huhtala, M.-L.5    Koivu, J.6    Kivirikko, K.I.7
  • 33
    • 0029006974 scopus 로고
    • Collagens: Molecular biology, diseases, and potentials for therapy
    • Prockop,D.J. and Kivirikko,K.I. (1995) Collagens: Molecular biology, diseases, and potentials for therapy. Anna. Rev. Biochem., 64, 403-434.
    • (1995) Anna. Rev. Biochem. , vol.64 , pp. 403-434
    • Prockop, D.J.1    Kivirikko, K.I.2
  • 34
    • 0026778048 scopus 로고
    • Foreign gene expression in yeast: A review
    • Romanos,M.A., Scorer,C.A. and Clare,J.J. (1992) Foreign gene expression in yeast: a review. Yeast. 8, 423-488.
    • (1992) Yeast , vol.8 , pp. 423-488
    • Romanos, M.A.1    Scorer, C.A.2    Clare, J.J.3
  • 35
    • 0029968576 scopus 로고    scopus 로고
    • Intracellular interaction of collagen-specific stress protein Hsp47 with newly synthesized procollagen
    • Satoh,M., Hirayoshi,K., Yokota,S., Hosokawa,N, and Nagata,K. (1996) Intracellular interaction of collagen-specific stress protein Hsp47 with newly synthesized procollagen. J. Cell Biol., 133, 469-483.
    • (1996) J. Cell Biol. , vol.133 , pp. 469-483
    • Satoh, M.1    Hirayoshi, K.2    Yokota, S.3    Hosokawa, N.4    Nagata, K.5
  • 36
    • 0025362399 scopus 로고
    • A rapid and simple method for preparation of RNA from S.cerevisiae
    • Schmitt,M.E. (1990) A rapid and simple method for preparation of RNA from S.cerevisiae. Nucleic Acids Res., 18, 3091-3092.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 3091-3092
    • Schmitt, M.E.1
  • 37
    • 14744304041 scopus 로고
    • Rapid selection using G418 of high copy number transformants of Pichia postoris for high-level foreign gene expression
    • Scorer,C.A., Clarc,J.J., McCombie,W.R., Romanos,M.A. and Sreekrishna,K. (1994) Rapid selection using G418 of high copy number transformants of Pichia postoris for high-level foreign gene expression. Biotechnology. 12, 181-184.
    • (1994) Biotechnology , vol.12 , pp. 181-184
    • Scorer, C.A.1    Clarc, J.J.2    McCombie, W.R.3    Romanos, M.A.4    Sreekrishna, K.5
  • 38
    • 0024532954 scopus 로고
    • A single base mutation that substitutes serine for glycine 790 of the α1(III) chain of type III procollagen exposes an arginine and causes Ehlers-Danlos syndrome IV
    • Tromp,G., Kuivaniemi,H., Shikata,H. and Prockop,D.J. (1989) A single base mutation that substitutes serine for glycine 790 of the α1(III) chain of type III procollagen exposes an arginine and causes Ehlers-Danlos syndrome IV. J. Biol. Chem., 264, 1349-1352.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1349-1352
    • Tromp, G.1    Kuivaniemi, H.2    Shikata, H.3    Prockop, D.J.4
  • 39
    • 0017697003 scopus 로고
    • Mechanism of the prolyl hydroxylase reaction. 1. Role of co-substrates
    • Tuderman,L., Myllylä,R. and Kivirikko,K.I. (1977) Mechanism of the prolyl hydroxylase reaction. 1. Role of co-substrates. Eur. J. Biochem., 80, 341-348.
    • (1977) Eur. J. Biochem. , vol.80 , pp. 341-348
    • Tuderman, L.1    Myllylä, R.2    Kivirikko, K.I.3
  • 40
    • 0028027778 scopus 로고
    • Cloning, baculovirus expression, and characterization of the α subunit of prolyl 4-hydroxylase from the nematode Caenorhahditis elegans. This α subunit forms an active αβ dimer with the human protein disulfide isomerase/β subunit
    • Veijola,J., Koivunen,P., Annunen,P., Pihlajaniemi,T. and Kivirikko,K.I. (1994) Cloning, baculovirus expression, and characterization of the α subunit of prolyl 4-hydroxylase from the nematode Caenorhahditis elegans. This α subunit forms an active αβ dimer with the human protein disulfide isomerase/β subunit. J. Biol. Chem., 269, 26746-26753.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26746-26753
    • Veijola, J.1    Koivunen, P.2    Annunen, P.3    Pihlajaniemi, T.4    Kivirikko, K.I.5
  • 41
    • 0029838075 scopus 로고    scopus 로고
    • Baculovirus expression of two protein disulphide isomerase isoforms from Caenorhabditis elegans and characterization of prolyl 4-hydroxylases containing one of these polypeptides as their βsubunit
    • Veijola,J., Annunen,P., Koivunen,P., Page,A.R., Pihlajaniemi,T. and Kivirikko,K.I. (1996a) Baculovirus expression of two protein disulphide isomerase isoforms from Caenorhabditis elegans and characterization of prolyl 4-hydroxylases containing one of these polypeptides as their βsubunit. Biochem. J., 317, 721-729.
    • (1996) Biochem. J. , vol.317 , pp. 721-729
    • Veijola, J.1    Annunen, P.2    Koivunen, P.3    Page, A.R.4    Pihlajaniemi, T.5    Kivirikko, K.I.6
  • 42
    • 0030005258 scopus 로고    scopus 로고
    • Co-expression of the α subunit of human prolyl 4-hydroxylase with BiP polypeptide in insect cells leads to the formation of soluble and insoluble complexes
    • Veijola,J., Pihlajaniemi,T. and Kivirikko,K.I. (1996b) Co-expression of the α subunit of human prolyl 4-hydroxylase with BiP polypeptide in insect cells leads to the formation of soluble and insoluble complexes. Biochem. J., 315, 613-618.
    • (1996) Biochem. J. , vol.315 , pp. 613-618
    • Veijola, J.1    Pihlajaniemi, T.2    Kivirikko, K.I.3
  • 43
    • 0026705344 scopus 로고
    • Expression and site-directed mutagenesis of human protein disulfide isomerase in Escherichia coli. This multifunctional polypeptide has two independently acting catalytic sites for the isomerase activity
    • Vuori,K., Myllylä,R., Pihlajaniemi,T. and Kivirikko,K.I. (1992a) Expression and site-directed mutagenesis of human protein disulfide isomerase in Escherichia coli. This multifunctional polypeptide has two independently acting catalytic sites for the isomerase activity. J. Biol. Chem., 267, 7211-7214.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7211-7214
    • Vuori, K.1    Myllylä, R.2    Pihlajaniemi, T.3    Kivirikko, K.I.4
  • 44
    • 0026725853 scopus 로고
    • Characterization of the human prolyl 4-hydroxylase tetramer and its multifunctional protein disulnde-isomerase subunit synthesized in a baculovirus expression system
    • Vuori,K., Pihlajaniemi,T., Marttila,M. and Kivirikko,K.I. (1992b) Characterization of the human prolyl 4-hydroxylase tetramer and its multifunctional protein disulnde-isomerase subunit synthesized in a baculovirus expression system. Proc. Natl Acad. Sci. USA. 89, 7467-7470.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 7467-7470
    • Vuori, K.1    Pihlajaniemi, T.2    Marttila, M.3    Kivirikko, K.I.4
  • 45
    • 0026672695 scopus 로고
    • Site-directed mutagenesis of human protein disulphide isomerase: Effect on the assembly, activity and endoplasmic reticulum retention of human prolyl 4-hydroxylase in Spadoptera frugiperda insect cells
    • Vuori,K., Pihlajaniemi,T., Myllylä,R. and Kivirikko,K.I. (1992c) Site-directed mutagenesis of human protein disulphide isomerase: effect on the assembly, activity and endoplasmic reticulum retention of human prolyl 4-hydroxylase in Spadoptera frugiperda insect cells. EMBO J. 11, 4213-4217.
    • (1992) EMBO J. , vol.11 , pp. 4213-4217
    • Vuori, K.1    Pihlajaniemi, T.2    Myllylä, R.3    Kivirikko, K.I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.