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Volumn 366, Issue 3, 2002, Pages 959-964

Lipid modification of proteins in Archaea: Attachment of a mevalonic acid-based lipid moiety to the surface-layer glycoprotein of Haloferax volcanii follows protein translocation

Author keywords

Halophilic archaea; Isoprenylation; Plasma membrane; Post translational modification; Protein biosynthesis

Indexed keywords

BIOLOGICAL MEMBRANES; BIOSYNTHESIS; HYDROPHOBICITY; LIPIDS; PROTEINS;

EID: 0037106458     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20020757     Document Type: Article
Times cited : (48)

References (32)
  • 1
    • 0031047960 scopus 로고    scopus 로고
    • Bacterial glycoproteins
    • Messner, P. (1997) Bacterial glycoproteins. Glycoconi. J. 14, 3-11
    • (1997) Glycoconi. J. , vol.14 , pp. 3-11
    • Messner, P.1
  • 2
    • 0030825124 scopus 로고    scopus 로고
    • Glycoproteins in prokaryotes
    • Moens, S. and Vanderleyden, J. (1997) Glycoproteins in prokaryotes. Arch. Microbiol. 168, 169-175
    • (1997) Arch. Microbiol. , vol.168 , pp. 169-175
    • Moens, S.1    Vanderleyden, J.2
  • 3
    • 0023655597 scopus 로고
    • The primary structure of a procaryotic glycoprotein. Cloning and sequencing of the cell surface glycoprotein gene of halobacteria
    • Lechner, J. and Sumper, M. (1987) The primary structure of a procaryotic glycoprotein. Cloning and sequencing of the cell surface glycoprotein gene of halobacteria. J. Biol. Chem. 262, 9724-9729
    • (1987) J. Biol. Chem. , vol.262 , pp. 9724-9729
    • Lechner, J.1    Sumper, M.2
  • 4
    • 0026587424 scopus 로고
    • Crystalline bacterial cell-surface layers
    • Messner, P. and Steytr, U. B. (1992) Crystalline bacterial cell-surface layers. Adv. Microb. Physiol. 33, 213-275
    • (1992) Adv. Microb. Physiol. , vol.33 , pp. 213-275
    • Messner, P.1    Steytr, U.B.2
  • 5
    • 0023517503 scopus 로고
    • Characterization of pHV2 from Halobacterium volcanii and its use in demonstrating transformation of an archaebacterium
    • Charlebois, R. L., Lam, W. L., Cline, S. W. and Doolittle, W. F. (1987) Characterization of pHV2 from Halobacterium volcanii and its use in demonstrating transformation of an archaebacterium. Proc. Natl. Acad. Sci. U.S.A. 84, 8350-8354
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 8350-8354
    • Charlebois, R.L.1    Lam, W.L.2    Cline, S.W.3    Doolittle, W.F.4
  • 6
    • 0025605636 scopus 로고
    • Primary structure and glycosylation of the S-layer protein of Haloferax volcanii
    • Sumper, M., Berg, E., Mengele, R. and Strobel, I. (1990) Primary structure and glycosylation of the S-layer protein of Haloferax volcanii. J. Bacteriol. 172, 7111-7118
    • (1990) J. Bacteriol. , vol.172 , pp. 7111-7118
    • Sumper, M.1    Berg, E.2    Mengele, R.3    Strobel, I.4
  • 7
    • 0026662396 scopus 로고
    • Drastic differences in glycosylation of related S-layer glycoproteins from moderate and extreme halophiles
    • Mengete, R. and Sumper, M. (1992) Drastic differences in glycosylation of related S-layer glycoproteins from moderate and extreme halophiles. J. Biol. Chem. 267, 8182-8185
    • (1992) J. Biol. Chem. , vol.267 , pp. 8182-8185
    • Mengele, R.1    Sumper, M.2
  • 8
    • 0029033903 scopus 로고
    • Inhibition of glycosylation by amphomycin and sugar nucleotide analogs PP36 and PP55 indicates that Haloferax volcanii β glycosylates both glycoproteins and glycolipids through lipid-linked sugar intermediates
    • Zhu, C. R., Drake, R. R., Schweingruber, H. and Laine, R. A. (1995) Inhibition of glycosylation by amphomycin and sugar nucleotide analogs PP36 and PP55 indicates that Haloferax volcanii β glycosylates both glycoproteins and glycolipids through lipid-linked sugar intermediates. Arch. Biochem. Biophys. 319, 355-364
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 355-364
    • Zhu, C.R.1    Drake, R.R.2    Schweingruber, H.3    Laine, R.A.4
  • 9
    • 0030668547 scopus 로고    scopus 로고
    • Isolation and characterization of dolichol-linked oligosaccharides from Haloferax volcanii
    • Kuntz, C., Sonnenbichler, J., Sonnenbichler, I., Sumper, M. and Zeitler, R. (1997) Isolation and characterization of dolichol-linked oligosaccharides from Haloferax volcanii. Glycobiology 7, 897-904
    • (1997) Glycobiology , vol.7 , pp. 897-904
    • Kuntz, C.1    Sonnenbichler, J.2    Sonnenbichler, I.3    Sumper, M.4    Zeitler, R.5
  • 10
    • 0034832009 scopus 로고    scopus 로고
    • Post-translational modification unrelated to protein glycosylation follows translocation of the S-layer glycoprotein across the plasma membrane of the haloarchaeon Haloferax volcanii
    • Eichler, J. (2001) Post-translational modification unrelated to protein glycosylation follows translocation of the S-layer glycoprotein across the plasma membrane of the haloarchaeon Haloferax volcanii. Eur. J. Biochem. 268, 4366-4373
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4366-4373
    • Eichler, J.1
  • 11
    • 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
  • 12
    • 0027959458 scopus 로고
    • Acylation of proteins of the archaebacteria Halobacterium cutirubrum and Methanobacterium thermoautotrophicum
    • Pugh, E. L. and Kates, M. (1994) Acylation of proteins of the archaebacteria Halobacterium cutirubrum and Methanobacterium thermoautotrophicum. Biochim. Biophys. Acta 1196, 38-44
    • (1994) Biochim. Biophys. Acta , vol.1196 , pp. 38-44
    • Pugh, E.L.1    Kates, M.2
  • 13
    • 0031564485 scopus 로고    scopus 로고
    • The presence of GPI-linked protein(s) in an archaeobacterium, Sulfolobus acidocaldarius, closely related to eukaryotes
    • Kobayashi, T., Nishizaki, R. and Ikezawa, H. (1997) The presence of GPI-linked protein(s) in an archaeobacterium, Sulfolobus acidocaldarius, closely related to eukaryotes. Biochim., Biophys. Acta 1334, 1-4
    • (1997) Biochim., Biophys. Acta , vol.1334 , pp. 1-4
    • Kobayashi, T.1    Nishizaki, R.2    Ikezawa, H.3
  • 14
    • 0029020349 scopus 로고
    • A novel type of protein modification by isoprenoid derived materials. Diphytanylglycerylated proteins in Halobacteria
    • Sagami, H., Kikuchi, A. and Ogura, D. (1995) A novel type of protein modification by isoprenoid derived materials. Diphytanylglycerylated proteins in Halobacteria. J. Biol. Chem. 270, 14851-14854
    • (1995) J. Biol. Chem. , vol.270 , pp. 14851-14854
    • Sagami, H.1    Kikuchi, A.2    Ogura, D.3
  • 15
    • 0033580929 scopus 로고    scopus 로고
    • Evidence for covalent attachment of diphytanylglyceryl phosphate to the cell-surface glycoprotein of Halobacterium halobium
    • Kikuchi, A., Sagami, H. and Ogura, K. (1999) Evidence for covalent attachment of diphytanylglyceryl phosphate to the cell-surface glycoprotein of Halobacterium halobium. J. Biol. Chem. 274, 18011-18016
    • (1999) J. Biol. Chem. , vol.274 , pp. 18011-18016
    • Kikuchi, A.1    Sagami, H.2    Ogura, K.3
  • 16
    • 0022003836 scopus 로고
    • Genetic transfer in Halobacterium volcanii
    • Mevarech, M. and Werczberger, R. (1985) Genetic transfer in Halobacterium volcanii. J. Bacteriol. 162, 461-462
    • (1985) J. Bacteriol. , vol.162 , pp. 461-462
    • Mevarech, M.1    Werczberger, R.2
  • 17
    • 0017613305 scopus 로고
    • Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis
    • Cleveland, D. W., Fischer, S. G., Kirschner, M. W. and Laemmli, U. K. (1977) Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. J. Biol. Chem. 252, 1102-1106
    • (1977) J. Biol. Chem. , vol.252 , pp. 1102-1106
    • Cleveland, D.W.1    Fischer, S.G.2    Kirschner, M.W.3    Laemmli, U.K.4
  • 18
    • 0020084688 scopus 로고
    • A highly sensitive periodic acid-silver stain for 1,2-diol groups of glycoproteins and polysaccharides in polyacrylamide gels
    • Dubray, G. and Bezard, G. (1982) A highly sensitive periodic acid-silver stain for 1,2-diol groups of glycoproteins and polysaccharides in polyacrylamide gels. Anal. Biochem. 119, 325-329
    • (1982) Anal. Biochem. , vol.119 , pp. 325-329
    • Dubray, G.1    Bezard, G.2
  • 19
    • 0034045403 scopus 로고    scopus 로고
    • Novel glycoproteins of the halophilic archaeon Haloferax volcanii
    • Eichler, J. (2000) Novel glycoproteins of the halophilic archaeon Haloferax volcanii. Arch. Microbiol. 173, 445-448
    • (2000) Arch. Microbiol. , vol.173 , pp. 445-448
    • Eichler, J.1
  • 20
    • 0027918584 scopus 로고
    • Biology of halophilic bacteria. Part II. Membrane lipids of extreme halophiles: Biosynthesis, function and evolutionary significance
    • Kates, M. (1993) Biology of halophilic bacteria, Part II. Membrane lipids of extreme halophiles: biosynthesis, function and evolutionary significance. Experientia 9, 1027-1036
    • (1993) Experientia , vol.9 , pp. 1027-1036
    • Kates, M.1
  • 21
    • 0022965218 scopus 로고
    • Isoprenoid synthesis in Halobacterium halobium. Modulation of 3-hydroxy-3-methylglutaryl coenzyme A concentration in response to mevalonate availability
    • Cabrera, J. A., Bolds, J., Shields, P. E., Havel, C. M. and Watson, J. A. (1986) Isoprenoid synthesis in Halobacterium halobium. Modulation of 3-hydroxy-3-methylglutaryl coenzyme A concentration in response to mevalonate availability. J. Biol. Chem. 261, 3578-3583
    • (1986) J. Biol. Chem. , vol.261 , pp. 3578-3583
    • Cabrera, J.A.1    Bolds, J.2    Shields, P.E.3    Havel, C.M.4    Watson, J.A.5
  • 22
    • 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. L. and Doolittle, W. F. (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.L.1    Doolittle, W.F.2
  • 23
    • 0021849616 scopus 로고
    • Transient methylation of dolichyl oligosaccharides is an obligatory step in halobacterial sulfated glycoprotein biosynthesis
    • Lechner, J., Wieland, F. and Sumper, M. (1985) Transient methylation of dolichyl oligosaccharides is an obligatory step in halobacterial sulfated glycoprotein biosynthesis. J. Biol. Chem. 260, 8984-8989
    • (1985) J. Biol. Chem. , vol.260 , pp. 8984-8989
    • Lechner, J.1    Wieland, F.2    Sumper, M.3
  • 24
    • 0034630098 scopus 로고    scopus 로고
    • Functional aspects of polyisoprenoid protein substituents: Roles in protein-protein interaction and trafficking
    • Sinensky, M. (2000) Functional aspects of polyisoprenoid protein substituents: roles in protein-protein interaction and trafficking. Biochim. Biophys. Acta 1484, 93-106
    • (2000) Biochim. Biophys. Acta , vol.1484 , pp. 93-106
    • Sinensky, M.1
  • 25
    • 0032851111 scopus 로고    scopus 로고
    • Sterols and isoprenoids: Signaling molecules derived from the cholesterol biosynthetic pathway
    • Edwards, P. A. and Ericsson, J. (1999) Sterols and isoprenoids: signaling molecules derived from the cholesterol biosynthetic pathway. Annu. Rev. Biochem. 68, 157-185
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 157-185
    • Edwards, P.A.1    Ericsson, J.2
  • 26
    • 0000499006 scopus 로고
    • Three-dimensional structure of the regular surface glycoprotein layer of Halobacterium volcanii from the Dead Sea
    • Kessel, M., Wildehaber, I., Cohen, S. and Baumeiser, W. (1988) Three-dimensional structure of the regular surface glycoprotein layer of Halobacterium volcanii from the Dead Sea. EMBO J. 7, 1549-1554
    • (1988) EMBO J. , vol.7 , pp. 1549-1554
    • Kessel, M.1    Wildehaber, I.2    Cohen, S.3    Baumeiser, W.4
  • 27
    • 0031061543 scopus 로고    scopus 로고
    • Cloning and sequencing of the gene encoding the cell surface glycoprotein of Haloarcula japonica strain TR-1
    • Wakai, H., Nakamura, S., Kawasaki, H., Takada, K., Mizutani, S., Aono, R. and Horikoshi, K. (1997) Cloning and sequencing of the gene encoding the cell surface glycoprotein of Haloarcula japonica strain TR-1. Extremophiles 1, 29-35
    • (1997) Extremophiles , vol.1 , pp. 29-35
    • Wakai, H.1    Nakamura, S.2    Kawasaki, H.3    Takada, K.4    Mizutani, S.5    Aono, R.6    Horikoshi, K.7
  • 28
    • 0017174797 scopus 로고
    • Structural (shape-maintaining) role of the cell surface glycoprotein of Halobacterium salinarium
    • Mescher, M. F. and Strominger, J. L. (1976) Structural (shape-maintaining) role of the cell surface glycoprotein of Halobacterium salinarium. Proc. Natl. Acad. Sci. U.S.A. 73, 2687-2691
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 2687-2691
    • Mescher, M.F.1    Strominger, J.L.2
  • 29
    • 0036176704 scopus 로고    scopus 로고
    • Archaeal signal peptidases from the genus Thermoplasma: Structural and mechanistic hybrids of the bacterial and eukaryal enzymes
    • Eichler, J. (2002) Archaeal signal peptidases from the genus Thermoplasma: structural and mechanistic hybrids of the bacterial and eukaryal enzymes. J. Mol. Evol. 54, 411-415
    • (2002) J. Mol. Evol. , vol.54 , pp. 411-415
    • Eichler, J.1
  • 30
    • 0027401732 scopus 로고
    • Membrane topology and biogenesis of eukaryotic signal peptidase
    • Shelness, G. S., Lin, L. and Nicchitta, C. V. (1993) Membrane topology and biogenesis of eukaryotic signal peptidase. J. Biol. Chem. 268, 5201-5208
    • (1993) J. Biol. Chem. , vol.268 , pp. 5201-5208
    • Shelness, G.S.1    Lin, L.2    Nicchitta, C.V.3
  • 31
    • 0033548673 scopus 로고    scopus 로고
    • Recognition of the carboxyl-terminal signal for GPI modification requires translocation of its hydrophobic domain across the ER membrane
    • Wang, J., Maziarz, K. and Ratnam, M. (1999) Recognition of the carboxyl-terminal signal for GPI modification requires translocation of its hydrophobic domain across the ER membrane. J. Mol. Biol. 286, 1303-1310
    • (1999) J. Mol. Biol. , vol.286 , pp. 1303-1310
    • Wang, J.1    Maziarz, K.2    Ratnam, M.3
  • 32
    • 0034743158 scopus 로고    scopus 로고
    • The ins(ide) and outs(ide) of dolichyl phosphate biosynthesis and recycling in the endoplasmic reticulum
    • Schenk, B., Fernandez, F. and Waechter, C. J. (2001) The ins(ide) and outs(ide) of dolichyl phosphate biosynthesis and recycling in the endoplasmic reticulum. Glycobiology 11, 61R-70R
    • (2001) Glycobiology , vol.11
    • Schenk, B.1    Fernandez, F.2    Waechter, C.J.3


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