메뉴 건너뛰기




Volumn 8, Issue 12, 1998, Pages 1157-1164

Exchange of Ser-4 for Val, Leu or Asn in the sequon Asn-Ala-Ser does not prevent N-glycosylation of the cell surface glycoprotein from Halobacterium halobium

Author keywords

Archaea; Gene replacement; Halobacteria; N glycosylation

Indexed keywords

ASPARAGINE; CELL SURFACE PROTEIN; GLYCOPROTEIN; LEUCINE; PENTASACCHARIDE; SERINE; VALINE;

EID: 0032416590     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/8.12.1157     Document Type: Article
Times cited : (37)

References (46)
  • 1
    • 0019880745 scopus 로고
    • Circular dichroism studies of synthetic Asn-X-Ser/Thr-containing peptides. Structure glycosylation relationship
    • Allbert, J., Helbecque, N. and Louchcheux-Lefebvre, M. (1981) Circular dichroism studies of synthetic Asn-X-Ser/Thr-containing peptides. Structure glycosylation relationship. Arch. Biochem. Biophys., 208, 20-29.
    • (1981) Arch. Biochem. Biophys. , vol.208 , pp. 20-29
    • Allbert, J.1    Helbecque, N.2    Louchcheux-Lefebvre, M.3
  • 2
    • 0019579733 scopus 로고
    • The role of the hydroxy amino acid in the triplet sequence Asn-Xaa-Thr(Ser) for the N-glycosylation step during glycoprotein biosynthesis
    • Hause, E. and Legler, G. (1981) The role of the hydroxy amino acid in the triplet sequence Asn-Xaa-Thr(Ser) for the N-glycosylation step during glycoprotein biosynthesis. Biochem. J., 195, 639-644.
    • (1981) Biochem. J. , vol.195 , pp. 639-644
    • Hause, E.1    Legler, G.2
  • 3
    • 0015858165 scopus 로고
    • New method for quantitative determination of uronic acids
    • Blumenkrantz, N. and Asboe-Hansen, G. (1973) New method for quantitative determination of uronic acids. Anal. Biochem., 54, 484-489.
    • (1973) Anal. Biochem. , vol.54 , pp. 484-489
    • Blumenkrantz, N.1    Asboe-Hansen, G.2
  • 4
    • 0023517503 scopus 로고
    • Characterization of pHV2 from Halobacterium volcanii and its use in demonstrating transformation of an archaebacterium
    • Charlebois, R., Lam, W., Cline, S. and Doolittle, W. (1987) Characterization of pHV2 from Halobacterium volcanii and its use in demonstrating transformation of an archaebacterium. Proc. Natl. Acad. Sci. USA, 84, 8530-8534.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 8530-8534
    • Charlebois, R.1    Lam, W.2    Cline, S.3    Doolittle, W.4
  • 5
    • 0023099215 scopus 로고
    • Efficient transfection of the Archaebacterium Halobacterium halobium
    • Cline, S., and Doolittle, F. (1987) Efficient transfection of the Archaebacterium Halobacterium halobium. J. Bacteriol., 169, 1341-1344.
    • (1987) J. Bacteriol. , vol.169 , pp. 1341-1344
    • Cline, S.1    Doolittle, F.2
  • 6
    • 33749946901 scopus 로고
    • Colorimetic method for determination of sugar and related substances
    • Dubois, M., Gilles, K.A., Hamilton, J.K., Rebers, P.A. and Smith, F. (1956) Colorimetic method for determination of sugar and related substances. Anal. Chem., 28, 350-356.
    • (1956) Anal. Chem. , vol.28 , pp. 350-356
    • Dubois, M.1    Gilles, K.A.2    Hamilton, J.K.3    Rebers, P.A.4    Smith, F.5
  • 7
    • 0020793569 scopus 로고
    • A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity
    • Feinberg, A. and Vogelstein, B. (1983) A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem., 132, 6-13.
    • (1983) Anal. Biochem. , vol.132 , pp. 6-13
    • Feinberg, A.1    Vogelstein, B.2
  • 9
    • 0027536538 scopus 로고
    • Homologous bacterio-opsin-encoding gene expression via site-specific vector integration
    • Ferrando, H., Schweiger, U. and Oesterhelt, D. (1993) Homologous bacterio-opsin-encoding gene expression via site-specific vector integration. Gene, 125, 41-47.
    • (1993) Gene , vol.125 , pp. 41-47
    • Ferrando, H.1    Schweiger, U.2    Oesterhelt, D.3
  • 10
    • 0025367812 scopus 로고
    • Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: Implications for protein engineering
    • Gavel, Y. and Heijne, G. (1990) Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineering. Protein Engineering, 3, 433-442.
    • (1990) Protein Engineering , vol.3 , pp. 433-442
    • Gavel, Y.1    Heijne, G.2
  • 11
    • 0025738011 scopus 로고
    • Construction and use of halobacterial shuttle vectors and further studies on haloferax DNA gyrase
    • Holmes, M., Nuttall, S. and Dyall-Smith, M. (1991) Construction and use of halobacterial shuttle vectors and further studies on haloferax DNA gyrase. J. Bacteriol., 173, 3807-3813.
    • (1991) J. Bacteriol. , vol.173 , pp. 3807-3813
    • Holmes, M.1    Nuttall, S.2    Dyall-Smith, M.3
  • 12
    • 0027968264 scopus 로고
    • Improved shuttle vectors for Haloferax volcanii including a dual-resistance plasmid
    • Holmes, M., Pfeifer, F. and Dyall-Smith, M. (1994) Improved shuttle vectors for Haloferax volcanii including a dual-resistance plasmid. Gene, 146, 117-121.
    • (1994) Gene , vol.146 , pp. 117-121
    • Holmes, M.1    Pfeifer, F.2    Dyall-Smith, M.3
  • 13
    • 0029041308 scopus 로고
    • The hydroxy amino acid in an Asn-X-Ser/Thr sequon can influence N-linked core glycosylation efficiency and the level of expression of a cell surface glycoprotein
    • Kasturi, L., Eshleman, J., Wunner, W. and Shakin-Eshleman, S. (1995) The hydroxy amino acid in an Asn-X-Ser/Thr sequon can influence N-linked core glycosylation efficiency and the level of expression of a cell surface glycoprotein. J. Biol. Chem., 270, 14756-14761.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14756-14761
    • Kasturi, L.1    Eshleman, J.2    Wunner, W.3    Shakin-Eshleman, S.4
  • 15
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld, R. and Kornfeld, S. (1985) Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem., 54, 631-664.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 16
    • 0026023558 scopus 로고
    • Expression of the bacterioopsin gene in Halobacterium halobium using a multicopy plasmid
    • Krebs, M., Hauss, T., Heyn, M., Rajbhandary, U. and Khorana, G. (1991) Expression of the bacterioopsin gene in Halobacterium halobium using a multicopy plasmid. Proc. Natl. Acad. Sci. USA, 88, 859-863.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 859-863
    • Krebs, M.1    Hauss, T.2    Heyn, M.3    Rajbhandary, U.4    Khorana, G.5
  • 17
    • 0027513571 scopus 로고
    • Gene replacement in Halobacterium halobium and expression of bacteriorhodopsin mutants
    • Krebs, M., Mollaaghababa, R. and Khorana, G. (1993a) Gene replacement in Halobacterium halobium and expression of bacteriorhodopsin mutants. Proc. Natl. Acad. Sci. USA, 90, 1987-1991.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1987-1991
    • Krebs, M.1    Mollaaghababa, R.2    Khorana, G.3
  • 18
    • 0027413675 scopus 로고
    • Synthesis of a gene for sensory rhodopsin I and its functional expression in Halobacterium halobium
    • Krebs, M., Spudich, E., Khorana, G. and Spudich, J. (1993b) Synthesis of a gene for sensory rhodopsin I and its functional expression in Halobacterium halobium. Proc. Natl. Acad. Sci. USA, 90, 3486-3490.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3486-3490
    • Krebs, M.1    Spudich, E.2    Khorana, G.3    Spudich, J.4
  • 19
    • 0024706289 scopus 로고
    • Shuttle vectors for the archaebacterium Halobacterium volcanii
    • Lam, W. and Doolittle, W. (1989) Shuttle vectors for the archaebacterium Halobacterium volcanii. Proc. Natl. Acad. Sci. USA, 86, 5478-5482.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5478-5482
    • Lam, W.1    Doolittle, W.2
  • 20
    • 0026713882 scopus 로고
    • Mevinolin-resistant mutations identify a promoter and the gene for a eukaryote-like 3-hydroxy-3-methylglutaryl-coenzyme A reductase in the archaebacterium Haloferax volcanii
    • Lam, W. and Doolittle, W. (1992) Mevinolin-resistant mutations identify a promoter and the gene for a eukaryote-like 3-hydroxy-3-methylglutaryl-coenzyme A reductase in the archaebacterium Haloferax volcanii. J. Biol. Chem., 267, 5829-5834.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5829-5834
    • Lam, W.1    Doolittle, W.2
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0023655597 scopus 로고
    • The primary structure of a prokaryotic glycoprotein
    • Lechner, J. and Sumper, M. (1987) The primary structure of a prokaryotic glycoprotein. J. Biol. Chem., 262, 9724-9729.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9724-9729
    • Lechner, J.1    Sumper, M.2
  • 23
    • 0024346543 scopus 로고
    • Structure and biosynthesis of prokaryotic glycoproteins
    • Lechner, J. and Wieland, F. (1989) Structure and biosynthesis of prokaryotic glycoproteins. Annu. Rev. Biochem., 58, 173-194.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 173-194
    • Lechner, J.1    Wieland, F.2
  • 24
    • 0027346495 scopus 로고
    • Analysis of bacterial glycoproteins
    • Hounsell, E. (ed.), Humana Press, Totowa, NJ
    • Lechner, J. and Wieland, F. (1992) Analysis of bacterial glycoproteins. In Hounsell, E. (ed.), Methods in Molecular Biology, Vol. 14. Humana Press, Totowa, NJ, pp. 119-129.
    • (1992) Methods in Molecular Biology , vol.14 , pp. 119-129
    • Lechner, J.1    Wieland, F.2
  • 25
    • 48549113950 scopus 로고
    • Primary structural requirements for N- and O-glycosylation of yeast mannoproteins
    • Lehle, L. and Bause, E. (1984) Primary structural requirements for N- And O-glycosylation of yeast mannoproteins. Biochim. Biophys. Acta, 799, 246-251.
    • (1984) Biochim. Biophys. Acta , vol.799 , pp. 246-251
    • Lehle, L.1    Bause, E.2
  • 26
    • 0027519943 scopus 로고
    • Protein glycosylation
    • Lis, H. and Sharon, N. (1993) Protein glycosylation. Eur. J. Biochem., 218, 1-27.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 1-27
    • Lis, H.1    Sharon, N.2
  • 28
    • 0016342403 scopus 로고
    • The nature and metabolism of the carbohydrate-peptide linkages of glycoproteins
    • Marshall, K.D. (1974) The nature and metabolism of the carbohydrate-peptide linkages of glycoproteins. Biochem. Soc. Symp., 40, 17-26.
    • (1974) Biochem. Soc. Symp. , vol.40 , pp. 17-26
    • Marshall, K.D.1
  • 29
    • 0022003836 scopus 로고
    • Genetic ransfer in Halobacterium volcanii
    • Mevarech, M. and Werczberger, R. (1985) Genetic ransfer in Halobacterium volcanii. J. Bacteriol., 162, 461-462.
    • (1985) J. Bacteriol. , vol.162 , pp. 461-462
    • Mevarech, M.1    Werczberger, R.2
  • 30
    • 0025303033 scopus 로고
    • An efficient system for the synthesis of bacteriorhodopsin in Halobacterium halobium
    • Ni, B., Chang, M., Duschl, A., Lanyi, J. and Needleman, R. (1990) An efficient system for the synthesis of bacteriorhodopsin in Halobacterium halobium. Gene, 90, 169-172.
    • (1990) Gene , vol.90 , pp. 169-172
    • Ni, B.1    Chang, M.2    Duschl, A.3    Lanyi, J.4    Needleman, R.5
  • 31
    • 0023655552 scopus 로고
    • Sequence of the halobacterial glycosaminoglycan
    • Paul, G. and Wieland, F. (1987) Sequence of the halobacterial glycosaminoglycan. J. Biol. Chem., 262, 9587-9593.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9587-9593
    • Paul, G.1    Wieland, F.2
  • 32
    • 0022648410 scopus 로고
    • Asparaginyl-N-acelylgalactosamine
    • Paul, G., Lottspeich, F. and Wieland, F. (1986) Asparaginyl-N-acelylgalactosamine. J. Biol. Chem., 261, 1020-1024.
    • (1986) J. Biol. Chem. , vol.261 , pp. 1020-1024
    • Paul, G.1    Lottspeich, F.2    Wieland, F.3
  • 33
  • 37
    • 0028222069 scopus 로고
    • Novel N-glycosylation in eukaryotes: Laminin contains the linkage unit beta-glucosylasparagine
    • Schreiner, R., Schnabel, E. and Wieland, F. (1994) Novel N-glycosylation in eukaryotes: laminin contains the linkage unit beta-glucosylasparagine J. Cell Biol., 124, 1071-1081.
    • (1994) J. Cell Biol. , vol.124 , pp. 1071-1081
    • Schreiner, R.1    Schnabel, E.2    Wieland, F.3
  • 38
    • 0020491258 scopus 로고
    • Amino acid sequence of the heavy chain of bovine protein C
    • Stenflo, J., and Fernlund, P. (1982) Amino acid sequence of the heavy chain of bovine protein C. J. Mol. Chem., 257, 12180-12190.
    • (1982) J. Mol. Chem. , vol.257 , pp. 12180-12190
    • Stenflo, J.1    Fernlund, P.2
  • 39
    • 0023235232 scopus 로고
    • Halobacterial glycoprotein biosynthesis
    • Sumper, M. (1987) Halobacterial glycoprotein biosynthesis. Biochim. Biophys. Acta, 906, 69-79.
    • (1987) Biochim. Biophys. Acta , vol.906 , pp. 69-79
    • Sumper, M.1
  • 40
    • 0017820243 scopus 로고
    • Studies on the biosynthesis of bacterio-opsin
    • Sumper, M. and Herrmann, G. (1978) Studies on the biosynthesis of bacterio-opsin. Eur. J. Biochem., 89, 229-235.
    • (1978) Eur. J. Biochem. , vol.89 , pp. 229-235
    • Sumper, M.1    Herrmann, G.2
  • 41
    • 77956818765 scopus 로고
    • Montreuil, J., Schachter, H. and Vliegenhart, J.F.G. (eds.), Elsevier Science B.V., Amsterdam
    • Sumper, M. and Wieland, F. (1995) In Montreuil, J., Schachter, H. and Vliegenhart, J.F.G. (eds.), Glycoproteins, New Comprehensive Biochemistry, Vol. 29a. Elsevier Science B.V., Amsterdam, pp. 455-473.
    • (1995) Glycoproteins, New Comprehensive Biochemistry , vol.29 A , pp. 455-473
    • Sumper, M.1    Wieland, F.2
  • 43
    • 0019329774 scopus 로고
    • Halobacterial glycoprotein saccharides contain covalently linked sulphate
    • Wieland, F., Dompert, W., Bernhardt, G., and Sumper, M. (1980) Halobacterial glycoprotein saccharides contain covalently linked sulphate. FEBS Lett., 120, 110-114.
    • (1980) FEBS Lett. , vol.120 , pp. 110-114
    • Wieland, F.1    Dompert, W.2    Bernhardt, G.3    Sumper, M.4
  • 44
    • 0008954109 scopus 로고
    • Sulphation of a repetitive saccharide in halobacterial cell wall glycoprotein
    • Wieland, F., Lechner, J., Bernhardt, G. and Sumper, M. (1981) Sulphation of a repetitive saccharide in halobacterial cell wall glycoprotein. FEBS Lett., 132, 319-323.
    • (1981) FEBS Lett. , vol.132 , pp. 319-323
    • Wieland, F.1    Lechner, J.2    Bernhardt, G.3    Sumper, M.4
  • 45
    • 0020035801 scopus 로고
    • The cell wall glycoprotein of halobacteria: Structural, functional and biosynthetic aspects
    • Wieland, F., Lechner, J. and Sumper, M. (1982) The cell wall glycoprotein of halobacteria: structural, functional and biosynthetic aspects. Zbl. Bakt. Hyg. I. Abt. Orig., C3, 161-170.
    • (1982) Zbl. Bakt. Hyg. I. Abt. Orig. , vol.C3 , pp. 161-170
    • Wieland, F.1    Lechner, J.2    Sumper, M.3
  • 46
    • 0021079945 scopus 로고
    • Asparaginylglucose: Novel type of carbohydrate linkage
    • Wieland, F., Heitzer, R. and Schaefer, W. (1983) Asparaginylglucose: novel type of carbohydrate linkage. Proc. Natl. Acad. Sci. USA, 80, 5470-5474.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 5470-5474
    • Wieland, F.1    Heitzer, R.2    Schaefer, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.