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Volumn 32, Issue 2, 1997, Pages 139-146

Characterization of the bip gene of Aspergillus awamori encoding a protein with an HDEL retention signal homologous to the mammalian BiP involved in polypeptide secretion

Author keywords

BiP protein; Endoplasmic reticulum; Fungi; Protein secretion

Indexed keywords

DNA FRAGMENT; MEMBRANE PROTEIN; MESSENGER RNA; POLYPEPTIDE; SIGNAL PEPTIDE;

EID: 0030759130     PISSN: 01728083     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002940050258     Document Type: Article
Times cited : (18)

References (36)
  • 2
    • 0016606396 scopus 로고
    • Carbon catabolite repression in Aspergillus nidulans
    • Bailey C, Arts HNJr (1975) Carbon catabolite repression in Aspergillus nidulans. Eur J Biochem 51:573-577
    • (1975) Eur J Biochem , vol.51 , pp. 573-577
    • Bailey, C.1    Arts Jr., H.N.2
  • 3
    • 0020645046 scopus 로고
    • Kilo-sequencing: Creation of an ordered nest of asymmetric deletions across a large target sequence carried on phage M13
    • Barnes WM, Bevan M, Son PH (1983) Kilo-sequencing: creation of an ordered nest of asymmetric deletions across a large target sequence carried on phage M13. Methods Enzymol 101:98-122
    • (1983) Methods Enzymol , vol.101 , pp. 98-122
    • Barnes, W.M.1    Bevan, M.2    Son, P.H.3
  • 4
    • 0025944347 scopus 로고
    • Analysis of the creA gene, a regulator of carbon catabolite repression in Aspergillus nidulans
    • Dowzer CEA, Kelly JM (1991) Analysis of the creA gene, a regulator of carbon catabolite repression in Aspergillus nidulans. Mol Cell Biol 11:5701-5709
    • (1991) Mol Cell Biol , vol.11 , pp. 5701-5709
    • Dowzer, C.E.A.1    Kelly, J.M.2
  • 5
    • 0030070112 scopus 로고    scopus 로고
    • Mutants blocked in penicillin biosynthesis show a deletion of the entire penicillin gene cluster at a specific site within a conserved hex-anucleotide sequence
    • Fierro F, Montenegro E, Gutiérrez S, Martín JF (1996) Mutants blocked in penicillin biosynthesis show a deletion of the entire penicillin gene cluster at a specific site within a conserved hex-anucleotide sequence. Appl Microbiol Biotechnol 44:597-604
    • (1996) Appl Microbiol Biotechnol , vol.44 , pp. 597-604
    • Fierro, F.1    Montenegro, E.2    Gutiérrez, S.3    Martín, J.F.4
  • 7
    • 0031054007 scopus 로고    scopus 로고
    • Efficient production of secreted proteins by Aspergillus: Progress, limitations and prospects
    • Gouka RJ, Punt PJ, van den Hondel CAMJJ (1997) Efficient production of secreted proteins by Aspergillus: progress, limitations and prospects. Appl Microbiol Biotechnol 47:1-11
    • (1997) Appl Microbiol Biotechnol , vol.47 , pp. 1-11
    • Gouka, R.J.1    Punt, P.J.2    Van den Hondel, C.A.M.J.J.3
  • 8
    • 0026692645 scopus 로고
    • Cloning of the HSP70 gene from Halo-bacterium marismortui: Relatedness of archaebacterial HSP70 to its eubacterial homologos and a model for the evolution of the HSP70 gene
    • Gupta RS, Singh B (1992) Cloning of the HSP70 gene from Halo-bacterium marismortui: relatedness of archaebacterial HSP70 to its eubacterial homologos and a model for the evolution of the HSP70 gene, J Bacteriol 174:4594-4605
    • (1992) J Bacteriol , vol.174 , pp. 4594-4605
    • Gupta, R.S.1    Singh, B.2
  • 9
    • 0026490708 scopus 로고
    • Expression of foreign proteins in the genus Aspergillus
    • Bennet JW, Klich MA (eds). Butterworth, London
    • Gwynne DI, Devchand M (1992) Expression of foreign proteins in the genus Aspergillus. In: Bennet JW, Klich MA (eds). Aspergillus, the biology and industrial applications. Butterworth, London, pp 203-214
    • (1992) Aspergillus, the Biology and Industrial Applications , pp. 203-214
    • Gwynne, D.I.1    Devchand, M.2
  • 10
    • 0029094253 scopus 로고
    • Quality control in the secretory pathway
    • Hammond C, Helenius A (1995) Quality control in the secretory pathway. Curr Opin Cell Biol 7:523-529
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 523-529
    • Hammond, C.1    Helenius, A.2
  • 11
    • 0020770479 scopus 로고
    • Patterns of amino acids near signal-sequence cleavage sites
    • Heijne G von (1983) Patterns of amino acids near signal-sequence cleavage sites. Eur J Biochem 133:17-21
    • (1983) Eur J Biochem , vol.133 , pp. 17-21
    • Von Heijne, G.1
  • 12
    • 0021856417 scopus 로고
    • Signal sequences. the limits of variation
    • Heijne G von (1985) Signal sequences. The limits of variation. J Mol Biol 184:99-105
    • (1985) J Mol Biol , vol.184 , pp. 99-105
    • Von Heijne, G.1
  • 13
    • 0001852858 scopus 로고
    • Heterologous gene expression in filamentous fungi
    • Bennett JW, Lasurre LL (eds). Academic Press, San Diego, California
    • Hondel CAMJJ van den, Punt PJ, van Gorcom RFM (1991) Heterologous gene expression in filamentous fungi. In: Bennett JW, Lasurre LL (eds). More gene manipulation in fungi. Academic Press, San Diego, California, pp 396-428
    • (1991) More Gene Manipulation in Fungi , pp. 396-428
    • Van den Hondel, C.A.M.J.J.1    Punt, P.J.2    Van Gorcom, R.F.M.3
  • 14
    • 0026656520 scopus 로고
    • Transient aggregation of nascent thyroglobulin in the endoplasmic reticulum: Relationship to the molecular chaperone BiP
    • Kim PS, Bole D, Arvan P (1992) Transient aggregation of nascent thyroglobulin in the endoplasmic reticulum: relationship to the molecular chaperone BiP. J Cell Biol 118:541-549
    • (1992) J Cell Biol , vol.118 , pp. 541-549
    • Kim, P.S.1    Bole, D.2    Arvan, P.3
  • 15
    • 0028928021 scopus 로고
    • Molecular chaperones involved in protein degradation in the endoplasmic reticulum: Quantitative interaction of the heat-shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum
    • Knittler MR, Dirks S, Haas IG (1995) Molecular chaperones involved in protein degradation in the endoplasmic reticulum: quantitative interaction of the heat-shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum. Proc Natl Acad Sci USA 92:1764-1768
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1764-1768
    • Knittler, M.R.1    Dirks, S.2    Haas, I.G.3
  • 16
    • 0024845992 scopus 로고
    • Identification of immunoglobulin heavy chain binding protein as glucose-regulated protein 78 on the basis of amino-acid sequence, immunological cross-reactivity, and functional activity
    • Kozutsumi Y, Normington K, Press E, Slaughter C, Sambrook J, Gething MJ (1989) Identification of immunoglobulin heavy chain binding protein as glucose-regulated protein 78 on the basis of amino-acid sequence, immunological cross-reactivity, and functional activity. J Cell Sci Suppl 11:115-137
    • (1989) J Cell Sci Suppl , vol.11 , pp. 115-137
    • Kozutsumi, Y.1    Normington, K.2    Press, E.3    Slaughter, C.4    Sambrook, J.5    Gething, M.J.6
  • 17
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157:105-132
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 18
    • 0027197130 scopus 로고
    • Translocation of proteins across the membrane of the endoplasmic reticulum: A place for Saccharomyces cerevisiae
    • Larriba G (1993) Translocation of proteins across the membrane of the endoplasmic reticulum: a place for Saccharomyces cerevisiae. Yeast 9:441-463
    • (1993) Yeast , vol.9 , pp. 441-463
    • Larriba, G.1
  • 19
    • 0030970268 scopus 로고    scopus 로고
    • Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP
    • Lyman SK, Schekman, R (1997) Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP. Cell 88:85-96
    • (1997) Cell , vol.88 , pp. 85-96
    • Lyman, S.K.1    Schekman, R.2
  • 20
    • 0026563680 scopus 로고
    • Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum
    • Marquard T, Helenius A (1992) Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum. J Cell Biol 117:505-513
    • (1992) J Cell Biol , vol.117 , pp. 505-513
    • Marquard, T.1    Helenius, A.2
  • 21
    • 0026628290 scopus 로고
    • A 22-bp cis-acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins
    • Mori K, Sant A, Kohno K, Normington K, Gething MJ, Sambrook JF (1992) A 22-bp cis-acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins. EMBO J 11:2583-2593
    • (1992) EMBO J , vol.11 , pp. 2583-2593
    • Mori, K.1    Sant, A.2    Kohno, K.3    Normington, K.4    Gething, M.J.5    Sambrook, J.F.6
  • 22
    • 0025970971 scopus 로고
    • Binding protein BiP is required for translocation of secretory proteins into the endoplasmic reticulum in Saccharomyces cerevisiae
    • Nguyen TH, Law DT, Williams DB (1991) Binding protein BiP is required for translocation of secretory proteins into the endoplasmic reticulum in Saccharomyces cerevisiae. Proc Natl Acad Sci USA 88:1565-1569
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 1565-1569
    • Nguyen, T.H.1    Law, D.T.2    Williams, D.B.3
  • 23
    • 0024395160 scopus 로고
    • Saccharomyces cerevisiae encodes an essential protein homologous in sequence and function to mamalian BiP
    • Normington K, Kohno K, Kozutsumi Y, Gething M-J, Sambrook J (1989) Saccharomyces cerevisiae encodes an essential protein homologous in sequence and function to mamalian BiP. Cell 57:1223-1236
    • (1989) Cell , vol.57 , pp. 1223-1236
    • Normington, K.1    Kohno, K.2    Kozutsumi, Y.3    Gething, M.-J.4    Sambrook, J.5
  • 24
    • 0026583674 scopus 로고
    • Analysis of the BiP gene and identification of an ER retention signal in Schizosaccharomyces pombe
    • Pidoux AL, Armstrong J (1992) Analysis of the BiP gene and identification of an ER retention signal in Schizosaccharomyces pombe. EMBOJ 11:1583-1591
    • (1992) EMBOJ , vol.11 , pp. 1583-1591
    • Pidoux, A.L.1    Armstrong, J.2
  • 25
    • 0024338964 scopus 로고
    • KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene
    • Rose MD, Misra LM, Vogel JP (1989) KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene. Cell 57:1211-1221
    • (1989) Cell , vol.57 , pp. 1211-1221
    • Rose, M.D.1    Misra, L.M.2    Vogel, J.P.3
  • 26
    • 0028967755 scopus 로고
    • Transduction of calcium stress through interaction of the human transcription factor CBF with the proximal CCAAT regulatory element of the grp78/BiP promoter
    • Roy B, Lee AS (1995) Transduction of calcium stress through interaction of the human transcription factor CBF with the proximal CCAAT regulatory element of the grp78/BiP promoter. Mol Cell Biol 15:2263-2274
    • (1995) Mol Cell Biol , vol.15 , pp. 2263-2274
    • Roy, B.1    Lee, A.S.2
  • 29
    • 0021268086 scopus 로고
    • Repression of β-lactam production in Cephalosporium acremonium by nitrogen sources
    • Shen Y-Q, Heim J, Solomon NA, Wolfe S, Demain AL (1984) Repression of β-lactam production in Cephalosporium acremonium by nitrogen sources. J Antibiot 37:503-511
    • (1984) J Antibiot , vol.37 , pp. 503-511
    • Shen, Y.-Q.1    Heim, J.2    Solomon, N.A.3    Wolfe, S.4    Demain, A.L.5
  • 30
    • 0025854858 scopus 로고
    • A protein-conducting channel in the endoplasmic reticulum
    • Simon SM, Blobel G (1991) A protein-conducting channel in the endoplasmic reticulum. Cell 65:371-380
    • (1991) Cell , vol.65 , pp. 371-380
    • Simon, S.M.1    Blobel, G.2
  • 31
    • 0020056204 scopus 로고
    • A method for extracting high-molecular-weight deoxyribonucleic acid from fungi
    • Specht CA, DiRusso CC, Novotny CP, Ullrich RC (1982) A method for extracting high-molecular-weight deoxyribonucleic acid from fungi, Anal Biochem 119:158-163
    • (1982) Anal Biochem , vol.119 , pp. 158-163
    • Specht, C.A.1    DiRusso, C.C.2    Novotny, C.P.3    Ullrich, R.C.4
  • 33
    • 0029077782 scopus 로고
    • Molecular genetic strain improvement for the over-production of fungal proteins by filamentous fungi
    • Verdoes JC, Punt PJ, van den Hondel CAMJJ (1995) Molecular genetic strain improvement for the over-production of fungal proteins by filamentous fungi. Appl Microbiol Biotechnol 43:195-1205
    • (1995) Appl Microbiol Biotechnol , vol.43 , pp. 195-1205
    • Verdoes, J.C.1    Punt, P.J.2    Van den Hondel, C.A.M.J.J.3
  • 34
    • 0021760521 scopus 로고
    • Compilation of published signal sequences
    • Watson MEE (1984) Compilation of published signal sequences. Nucleic Acids Res 12:5145-5164
    • (1984) Nucleic Acids Res , vol.12 , pp. 5145-5164
    • Watson, M.E.E.1
  • 35
    • 0025320002 scopus 로고
    • Improved production of chymosin in Aspergillus by expression as a glucoamylase-chymosin fusion
    • Ward M, Wilson LJ, Kodama KH, Rey MW, Berka RM (1990) Improved production of chymosin in Aspergillus by expression as a glucoamylase-chymosin fusion. Bio/Technology 8:435-440
    • (1990) Bio/Technology , vol.8 , pp. 435-440
    • Ward, M.1    Wilson, L.J.2    Kodama, K.H.3    Rey, M.W.4    Berka, R.M.5
  • 36
    • 0026011095 scopus 로고
    • Yeast signal peptidase contains a glycoprotein and the secII gene product
    • YaDeau JT, Klein C, Blobel G (1991) Yeast signal peptidase contains a glycoprotein and the secII gene product. Proc Natl Acad Sci USA 88:517-521
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 517-521
    • YaDeau, J.T.1    Klein, C.2    Blobel, G.3


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