메뉴 건너뛰기




Volumn 3, Issue 4, 2014, Pages 531-543

AglB, catalyzing the oligosaccharyl transferase step of the archaeal N-glycosylation process, is essential in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius

Author keywords

AglB; Archaea; Crenarchaeota; N glycosylation; Sulfolobus

Indexed keywords

AGLB PROTEIN; BACTERIAL ENZYME; UNCLASSIFIED DRUG; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE - PROTEIN GLYCOTRANSFERASE; GLYCOSYLTRANSFERASE; MEMBRANE PROTEIN; S-LAYER PROTEINS;

EID: 84906081667     PISSN: None     EISSN: 20458827     Source Type: Journal    
DOI: 10.1002/mbo3.185     Document Type: Article
Times cited : (26)

References (61)
  • 1
    • 36248931035 scopus 로고    scopus 로고
    • Haloferax volcanii AglB and AglD are involved in N-glycosylation of the S-layer glycoprotein and proper assembly of the surface layer
    • Abu-Qarn, M., S. Yurist-Doutsch, A. Giordano, A. Trauner, H. R. Morris, P. Hitchen, et al. 2007. Haloferax volcanii AglB and AglD are involved in N-glycosylation of the S-layer glycoprotein and proper assembly of the surface layer. J. Mol. Biol. 374:1224-1236.
    • (2007) J. Mol. Biol. , vol.374 , pp. 1224-1236
    • Abu-Qarn, M.1    Yurist-Doutsch, S.2    Giordano, A.3    Trauner, A.4    Morris, H.R.5    Hitchen, P.6
  • 2
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • Apweiler, R., H. Hermjakob, and N. Sharon. 1999. On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim. Biophys. Acta 1473:4-8.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 3
    • 0015275944 scopus 로고
    • Sulfolobus - new genus of sulfur-oxidizing bacteria living at low pH and high temperature
    • Brock, T. D., K. M. Brock, R. T. Belly, and R. L. Weiss. 1972. Sulfolobus - new genus of sulfur-oxidizing bacteria living at low pH and high temperature. Arch. Microbiol. 84:54-68.
    • (1972) Arch. Microbiol. , vol.84 , pp. 54-68
    • Brock, T.D.1    Brock, K.M.2    Belly, R.T.3    Weiss, R.L.4
  • 4
    • 36249022072 scopus 로고    scopus 로고
    • How sugars convey information on protein conformation in the endoplasmic reticulum
    • Caramelo, J. J., and A. J. Parodi. 2007. How sugars convey information on protein conformation in the endoplasmic reticulum. Semin. Cell Dev. Biol. 18:732-742.
    • (2007) Semin. Cell Dev. Biol. , vol.18 , pp. 732-742
    • Caramelo, J.J.1    Parodi, A.J.2
  • 5
    • 33745207351 scopus 로고    scopus 로고
    • Identification of genes involved in the biosynthesis and attachment of Methanococcus voltae N-linked glycans: insight into N-linked glycosylation pathways in Archaea
    • Chaban, B., S. Voisin, J. Kelly, S. M. Logan, and K. F. Jarrell. 2006. Identification of genes involved in the biosynthesis and attachment of Methanococcus voltae N-linked glycans: insight into N-linked glycosylation pathways in Archaea. Mol. Microbiol. 61:259-268.
    • (2006) Mol. Microbiol. , vol.61 , pp. 259-268
    • Chaban, B.1    Voisin, S.2    Kelly, J.3    Logan, S.M.4    Jarrell, K.F.5
  • 7
    • 70349462511 scopus 로고    scopus 로고
    • Unmarked gene deletion and host-vector system for the hyperthermophilic crenarchaeon Sulfolobus islandicus
    • Deng, L., H. Zhu, Z. Chen, Y. X. Liang, and Q. She. 2009. Unmarked gene deletion and host-vector system for the hyperthermophilic crenarchaeon Sulfolobus islandicus. Extremophiles 13:735-746.
    • (2009) Extremophiles , vol.13 , pp. 735-746
    • Deng, L.1    Zhu, H.2    Chen, Z.3    Liang, Y.X.4    She, Q.5
  • 8
    • 0025367812 scopus 로고
    • Sequence differences between glycosylated and nonglycosylated Asn-X-Thr Ser acceptor sites - implications for protein engineering
    • Gavel, Y., and G. Vonheijne. 1990. Sequence differences between glycosylated and nonglycosylated Asn-X-Thr Ser acceptor sites - implications for protein engineering. Protein Eng. 3:433-442.
    • (1990) Protein Eng. , vol.3 , pp. 433-442
    • Gavel, Y.1    Vonheijne, G.2
  • 9
    • 26444545059 scopus 로고    scopus 로고
    • In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation
    • Glover, K. J., E. Weerapana, and B. Imperiali. 2005a. In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation. Proc. Natl. Acad. Sci. USA 102:14255-14259.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 14255-14259
    • Glover, K.J.1    Weerapana, E.2    Imperiali, B.3
  • 10
    • 28844508716 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of glycopeptides with PglB, a bacterial oligosaccharyl transferase from Campylobacter jejuni
    • Glover, K. J., E. Weerapana, S. Numao, and B. Imperiali. 2005b. Chemoenzymatic synthesis of glycopeptides with PglB, a bacterial oligosaccharyl transferase from Campylobacter jejuni. Chem. Biol. 12:1311-1315.
    • (2005) Chem. Biol. , vol.12 , pp. 1311-1315
    • Glover, K.J.1    Weerapana, E.2    Numao, S.3    Imperiali, B.4
  • 12
    • 54449094921 scopus 로고    scopus 로고
    • The Haemophilus influenzae HMW1 adhesin is a glycoprotein with an unusual N-linked carbohydrate modification
    • Gross, J., S. Grass, A. E. Davis, P. Gilmore-Erdmann, R. R. Townsend, and J. W. S. Geme. 2008. The Haemophilus influenzae HMW1 adhesin is a glycoprotein with an unusual N-linked carbohydrate modification. J. Biol. Chem. 283:26010-26015.
    • (2008) J. Biol. Chem. , vol.283 , pp. 26010-26015
    • Gross, J.1    Grass, S.2    Davis, A.E.3    Gilmore-Erdmann, P.4    Townsend, R.R.5    Geme, J.W.S.6
  • 13
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • Helenius, A., and M. Aebi. 2004. Roles of N-linked glycans in the endoplasmic reticulum. Annu. Rev. Biochem. 73:1019-1049.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 14
    • 58149339850 scopus 로고    scopus 로고
    • The yeast oligosaccharyltransferase complex can be replaced by STT3 from Leishmania major
    • Hese, K., C. Otto, F. H. Routier, and L. Lehle. 2009. The yeast oligosaccharyltransferase complex can be replaced by STT3 from Leishmania major. Glycobiology 19:160-171.
    • (2009) Glycobiology , vol.19 , pp. 160-171
    • Hese, K.1    Otto, C.2    Routier, F.H.3    Lehle, L.4
  • 15
    • 0032870181 scopus 로고    scopus 로고
    • Changes in cell size and DNA content in Sulfolobus cultures during dilution and temperature shift experiments
    • Hjort, K., and R. Bernander. 1999. Changes in cell size and DNA content in Sulfolobus cultures during dilution and temperature shift experiments. J. Bacteriol. 181:5669-5675.
    • (1999) J. Bacteriol. , vol.181 , pp. 5669-5675
    • Hjort, K.1    Bernander, R.2
  • 16
    • 34548405722 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary X-ray diffraction studies of the soluble domain of the oligosaccharyltransferase STT3 subunit from the thermophilic archaeon Pyrococcus furiosus
    • Igura, M., N. Maita, T. Obita, J. Kamishikiryo, K. Maenaka, and D. Kohda. 2007. Purification, crystallization and preliminary X-ray diffraction studies of the soluble domain of the oligosaccharyltransferase STT3 subunit from the thermophilic archaeon Pyrococcus furiosus. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63:798-801.
    • (2007) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. , vol.63 , pp. 798-801
    • Igura, M.1    Maita, N.2    Obita, T.3    Kamishikiryo, J.4    Maenaka, K.5    Kohda, D.6
  • 17
    • 38049051311 scopus 로고    scopus 로고
    • Structure-guided identification of a new catalytic motif of oligosaccharyltransferase
    • Igura, M., N. Maita, J. Kamishikiryo, M. Yamada, T. Obita, K. Maenaka, et al. 2008. Structure-guided identification of a new catalytic motif of oligosaccharyltransferase. EMBO J. 27:234-243.
    • (2008) EMBO J. , vol.27 , pp. 234-243
    • Igura, M.1    Maita, N.2    Kamishikiryo, J.3    Yamada, M.4    Obita, T.5    Maenaka, K.6
  • 18
    • 77956846877 scopus 로고    scopus 로고
    • S-layer glycoproteins and flagellins: reporters of archaeal posttranslational modifications
    • Article ID 612948.
    • Jarrell, K. F., G. M. Jones, L. Kandiba, D. B. Nair, and J. Eichler. 2010. S-layer glycoproteins and flagellins: reporters of archaeal posttranslational modifications. Archaea 2010:Article ID 612948.
    • (2010) Archaea , vol.2010
    • Jarrell, K.F.1    Jones, G.M.2    Kandiba, L.3    Nair, D.B.4    Eichler, J.5
  • 21
    • 28844462711 scopus 로고    scopus 로고
    • Mapping the interaction of the STT3 subunit of the oligosaccharyl transferase complex with nascent polypeptide chains
    • Karamyshev, A. L., D. J. Kelleher, R. Gilmore, A. E. Johnson, G. von Heijne, and I. Nilsson. 2005. Mapping the interaction of the STT3 subunit of the oligosaccharyl transferase complex with nascent polypeptide chains. J. Biol. Chem. 280:40489-40493.
    • (2005) J. Biol. Chem. , vol.280 , pp. 40489-40493
    • Karamyshev, A.L.1    Kelleher, D.J.2    Gilmore, R.3    Johnson, A.E.4    von Heijne, G.5    Nilsson, I.6
  • 22
    • 33645103490 scopus 로고    scopus 로고
    • An evolving view of the eukaryotic oligosaccharyltransferase
    • Kelleher, D. J., and R. Gilmore. 2006. An evolving view of the eukaryotic oligosaccharyltransferase. Glycobiology 16:47R-62R.
    • (2006) Glycobiology , vol.16
    • Kelleher, D.J.1    Gilmore, R.2
  • 23
    • 20144378272 scopus 로고    scopus 로고
    • Membrane topology of the STT3 subunit of the oligosaccharyl transferase complex
    • Kim, H., G. von Heijne, and I. Nilsson. 2005. Membrane topology of the STT3 subunit of the oligosaccharyl transferase complex. J. Biol. Chem. 280:20261-20267.
    • (2005) J. Biol. Chem. , vol.280 , pp. 20261-20267
    • Kim, H.1    von Heijne, G.2    Nilsson, I.3
  • 24
    • 27744478779 scopus 로고    scopus 로고
    • Homologous recombination of exogenous DNA with the Sulfolobus acidocaldarius genome: properties and uses
    • Kurosawa, N., and D. W. Grogan. 2005. Homologous recombination of exogenous DNA with the Sulfolobus acidocaldarius genome: properties and uses. FEMS Microbiol. Lett. 253:141-149.
    • (2005) FEMS Microbiol. Lett. , vol.253 , pp. 141-149
    • Kurosawa, N.1    Grogan, D.W.2
  • 25
    • 79958165964 scopus 로고    scopus 로고
    • The expanding horizons of asparagine-linked glycosylation
    • Larkin, A., and B. Imperiali. 2011. The expanding horizons of asparagine-linked glycosylation. Biochemistry 50:4411-4426.
    • (2011) Biochemistry , vol.50 , pp. 4411-4426
    • Larkin, A.1    Imperiali, B.2
  • 26
    • 33750468309 scopus 로고    scopus 로고
    • Protein glycosylation, conserved from yeast to man: a model organism helps elucidate congenital human diseases
    • Lehle, L., S. Strahl, and W. Tanner. 2006. Protein glycosylation, conserved from yeast to man: a model organism helps elucidate congenital human diseases. Angew. Chem. Int. Ed. Engl. 45:6802-6818.
    • (2006) Angew. Chem. Int. Ed. Engl. , vol.45 , pp. 6802-6818
    • Lehle, L.1    Strahl, S.2    Tanner, W.3
  • 27
    • 38149139290 scopus 로고    scopus 로고
    • Studies on oligosaccharyl transferase in yeast
    • Lennarz, W. J. 2007. Studies on oligosaccharyl transferase in yeast. Acta Biochim. Pol. 54:673-677.
    • (2007) Acta Biochim. Pol. , vol.54 , pp. 673-677
    • Lennarz, W.J.1
  • 28
    • 79959191882 scopus 로고    scopus 로고
    • X-ray structure of a bacterial oligosaccharyltransferase
    • Lizak, C., S. Gerber, S. Numao, M. Aebi, and K. P. Locher. 2011. X-ray structure of a bacterial oligosaccharyltransferase. Nature 474:350-355.
    • (2011) Nature , vol.474 , pp. 350-355
    • Lizak, C.1    Gerber, S.2    Numao, S.3    Aebi, M.4    Locher, K.P.5
  • 29
    • 70349689931 scopus 로고    scopus 로고
    • Glycosyltransferases and oligosaccharyltransferases in Archaea: putative components of the N-glycosylation pathway in the third domain of life
    • Magidovich, H., and J. Eichler. 2009. Glycosyltransferases and oligosaccharyltransferases in Archaea: putative components of the N-glycosylation pathway in the third domain of life. FEMS Microbiol. Lett. 300:122-130.
    • (2009) FEMS Microbiol. Lett. , vol.300 , pp. 122-130
    • Magidovich, H.1    Eichler, J.2
  • 30
    • 77950194523 scopus 로고    scopus 로고
    • AglP is a S-adenosyl-L-methionine-dependent methyltransferase that participates in the N-glycosylation pathway of Haloferax volcanii
    • Magidovich, H., S. Yurist-Doutsch, Z. Konrad, V. V. Ventura, A. Dell, P. G. Hitchen, et al. 2010. AglP is a S-adenosyl-L-methionine-dependent methyltransferase that participates in the N-glycosylation pathway of Haloferax volcanii. Mol. Microbiol. 76:190-199.
    • (2010) Mol. Microbiol. , vol.76 , pp. 190-199
    • Magidovich, H.1    Yurist-Doutsch, S.2    Konrad, Z.3    Ventura, V.V.4    Dell, A.5    Hitchen, P.G.6
  • 31
    • 77950861521 scopus 로고    scopus 로고
    • Comparative structural biology of eubacterial and archaeal oligosaccharyltransferases
    • Maita, N., J. Nyirenda, M. Igura, J. Kamishikiryo, and D. Kohda. 2010. Comparative structural biology of eubacterial and archaeal oligosaccharyltransferases. J. Biol. Chem. 285:4941-4950.
    • (2010) J. Biol. Chem. , vol.285 , pp. 4941-4950
    • Maita, N.1    Nyirenda, J.2    Igura, M.3    Kamishikiryo, J.4    Kohda, D.5
  • 32
    • 84861400022 scopus 로고    scopus 로고
    • Crystal structure of the C-terminal globular domain of oligosaccharyltransferase from Archaeoglobus fulgidus at 1.75 A resolution
    • Matsumoto, S., M. Igura, J. Nyirenda, M. Matsumoto, S. Yuzawa, N. Noda, et al. 2012. Crystal structure of the C-terminal globular domain of oligosaccharyltransferase from Archaeoglobus fulgidus at 1.75 A resolution. Biochemistry 51:4157-4166.
    • (2012) Biochemistry , vol.51 , pp. 4157-4166
    • Matsumoto, S.1    Igura, M.2    Nyirenda, J.3    Matsumoto, M.4    Yuzawa, S.5    Noda, N.6
  • 33
    • 0026662396 scopus 로고
    • Drastic differences in glycosylation of related S-layer glycoproteins from moderate and extreme halophiles
    • Mengele, R., and M. Sumper. 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
  • 34
    • 84873122419 scopus 로고    scopus 로고
    • Hot and sweet: protein glycosylation in Crenarchaeota
    • Meyer, B. H., and S. V. Albers. 2013. Hot and sweet: protein glycosylation in Crenarchaeota. Biochem. Soc. Trans. 41:384-392.
    • (2013) Biochem. Soc. Trans. , vol.41 , pp. 384-392
    • Meyer, B.H.1    Albers, S.V.2
  • 35
    • 0026625352 scopus 로고
    • Characterization and purification of a membrane-bound archaebacterial pyrophosphatase from Sulfolobus acidocaldarius
    • Meyer, W., and G. Schafer. 1992. Characterization and purification of a membrane-bound archaebacterial pyrophosphatase from Sulfolobus acidocaldarius. Eur. J. Biochem. 207:741-746.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 741-746
    • Meyer, W.1    Schafer, G.2
  • 36
    • 82155175626 scopus 로고    scopus 로고
    • Sulfoquinovose synthase - an important enzyme in the N-glycosylation pathway of Sulfolobus acidocaldarius
    • Meyer, B. H., B. Zolghadr, E. Peyfoon, M. Pabst, M. Panico, H. R. Morris, et al. 2011. Sulfoquinovose synthase - an important enzyme in the N-glycosylation pathway of Sulfolobus acidocaldarius. Mol. Microbiol. 82:1150-1163.
    • (2011) Mol. Microbiol. , vol.82 , pp. 1150-1163
    • Meyer, B.H.1    Zolghadr, B.2    Peyfoon, E.3    Pabst, M.4    Panico, M.5    Morris, H.R.6
  • 37
    • 84877305230 scopus 로고    scopus 로고
    • Agl16, a thermophilic glycosyltransferase mediating the last step of N-glycan biosynthesis in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius
    • Meyer, B. H., E. Peyfoon, C. Dietrich, P. Hitchen, M. Panico, H. R. Morris, et al. 2013. Agl16, a thermophilic glycosyltransferase mediating the last step of N-glycan biosynthesis in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius. J. Bacteriol. 195:2177-2186.
    • (2013) J. Bacteriol. , vol.195 , pp. 2177-2186
    • Meyer, B.H.1    Peyfoon, E.2    Dietrich, C.3    Hitchen, P.4    Panico, M.5    Morris, H.R.6
  • 38
    • 0037684809 scopus 로고    scopus 로고
    • Photocross-linking of nascent chains to the STT3 subunit of the oligosaccharyltransferase complex
    • Nilsson, I., D. J. Kelleher, Y. Miao, Y. Shao, G. Kreibich, R. Gilmore, et al. 2003. Photocross-linking of nascent chains to the STT3 subunit of the oligosaccharyltransferase complex. J. Cell Biol. 161:715-725.
    • (2003) J. Cell Biol. , vol.161 , pp. 715-725
    • Nilsson, I.1    Kelleher, D.J.2    Miao, Y.3    Shao, Y.4    Kreibich, G.5    Gilmore, R.6
  • 39
    • 77958099601 scopus 로고    scopus 로고
    • Protein glycosylation in bacteria: sweeter than ever
    • Nothaft, H., and C. M. Szymanski. 2010. Protein glycosylation in bacteria: sweeter than ever. Nat. Rev. Microbiol. 8:765-778.
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 765-778
    • Nothaft, H.1    Szymanski, C.M.2
  • 40
    • 84874871322 scopus 로고    scopus 로고
    • Bacterial protein N-glycosylation: new perspectives and applications
    • Nothaft, H., and C. M. Szymanski. 2013. Bacterial protein N-glycosylation: new perspectives and applications. J. Biol. Chem. 288:6912-6920.
    • (2013) J. Biol. Chem. , vol.288 , pp. 6912-6920
    • Nothaft, H.1    Szymanski, C.M.2
  • 41
    • 84899029290 scopus 로고    scopus 로고
    • A rhomboid protease gene deletion affects a novel oligosaccharide N-linked to the S-layer glycoprotein of Haloferax volcanii
    • Parente, J., A. Casabuono, M. C. Ferrari, R. A. Paggi, R. E. De Castro, A. S. Couto, et al. 2014. A rhomboid protease gene deletion affects a novel oligosaccharide N-linked to the S-layer glycoprotein of Haloferax volcanii. J. Biol. Chem. 289:11304-11317.
    • (2014) J. Biol. Chem. , vol.289 , pp. 11304-11317
    • Parente, J.1    Casabuono, A.2    Ferrari, M.C.3    Paggi, R.A.4    De Castro, R.E.5    Couto, A.S.6
  • 42
    • 78249283543 scopus 로고    scopus 로고
    • The S-layer glycoprotein of the crenarchaeote Sulfolobus acidocaldarius is glycosylated at multiple sites with chitobiose-linked N-glycans
    • Article ID 754101.
    • Peyfoon, E., B. Meyer, P. G. Hitchen, M. Panico, H. R. Morris, S. M. Haslam, et al. 2010. The S-layer glycoprotein of the crenarchaeote Sulfolobus acidocaldarius is glycosylated at multiple sites with chitobiose-linked N-glycans. Archaea 2010: Article ID 754101.
    • (2010) Archaea , vol.2010
    • Peyfoon, E.1    Meyer, B.2    Hitchen, P.G.3    Panico, M.4    Morris, H.R.5    Haslam, S.M.6
  • 43
    • 61649089751 scopus 로고    scopus 로고
    • Analysis of glycosylation site occupancy reveals a role for Ost3p and Ost6p in site-specific N-glycosylation efficiency
    • Schulz, B. L., and M. Aebi. 2009. Analysis of glycosylation site occupancy reveals a role for Ost3p and Ost6p in site-specific N-glycosylation efficiency. Mol. Cell. Proteomics 8:357-364.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 357-364
    • Schulz, B.L.1    Aebi, M.2
  • 44
    • 67650498261 scopus 로고    scopus 로고
    • Oxidoreductase activity of oligosaccharyltransferase subunits Ost3p and Ost6p defines site-specific glycosylation efficiency
    • Schulz, B. L., C. U. Stirnimann, J. P. Grimshaw, M. S. Brozzo, F. Fritsch, E. Mohorko, et al. 2009. Oxidoreductase activity of oligosaccharyltransferase subunits Ost3p and Ost6p defines site-specific glycosylation efficiency. Proc. Natl Acad. Sci. USA 106:11061-11066.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 11061-11066
    • Schulz, B.L.1    Stirnimann, C.U.2    Grimshaw, J.P.3    Brozzo, M.S.4    Fritsch, F.5    Mohorko, E.6
  • 45
    • 27944459619 scopus 로고    scopus 로고
    • Yeast oligosaccharyltransferase consists of two functionally distinct sub-complexes, specified by either the Ost3p or Ost6p subunit
    • Schwarz, M., R. Knauer, and L. Lehle. 2005. Yeast oligosaccharyltransferase consists of two functionally distinct sub-complexes, specified by either the Ost3p or Ost6p subunit. FEBS Lett. 579:6564-6568.
    • (2005) FEBS Lett. , vol.579 , pp. 6564-6568
    • Schwarz, M.1    Knauer, R.2    Lehle, L.3
  • 46
    • 79953174969 scopus 로고    scopus 로고
    • Simultaneous glycan-peptide characterization using hydrophilic interaction chromatography and parallel fragmentation by CID, higher energy collisional dissociation, and electron transfer dissociation MS applied to the N-Linked glycoproteome of Campylobacter jejuni
    • Scott, N. E., B. L. Parker, A. M. Connolly, J. Paulech, A. V. G. Edwards, B. Crossett, et al. 2011. Simultaneous glycan-peptide characterization using hydrophilic interaction chromatography and parallel fragmentation by CID, higher energy collisional dissociation, and electron transfer dissociation MS applied to the N-Linked glycoproteome of Campylobacter jejuni. Mol. Cell. Proteomics. 10:10.1074.
    • (2011) Mol. Cell. Proteomics. , vol.10 , pp. 101074
    • Scott, N.E.1    Parker, B.L.2    Connolly, A.M.3    Paulech, J.4    Edwards, A.V.G.5    Crossett, B.6
  • 47
    • 0025605636 scopus 로고
    • Primary structure and glycosylation of the S-layer protein of Haloferax volcanii
    • Sumper, M., E. Berg, R. Mengele, and I. Strobel. 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
  • 48
    • 14544282378 scopus 로고    scopus 로고
    • Protein glycosylation in bacterial mucosal pathogens
    • Szymanski, C. M., and B. W. Wren. 2005. Protein glycosylation in bacterial mucosal pathogens. Nat. Rev. Microbiol. 3:225-237.
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 225-237
    • Szymanski, C.M.1    Wren, B.W.2
  • 49
    • 0033024228 scopus 로고    scopus 로고
    • Evidence for a system of general protein glycosylation in Campylobacter jejuni
    • Szymanski, C. M., R. Yao, C. P. Ewing, T. J. Trust, and P. Guerry. 1999. Evidence for a system of general protein glycosylation in Campylobacter jejuni. Mol. Microbiol. 32:1022-1030.
    • (1999) Mol. Microbiol. , vol.32 , pp. 1022-1030
    • Szymanski, C.M.1    Yao, R.2    Ewing, C.P.3    Trust, T.J.4    Guerry, P.5
  • 50
    • 84866392761 scopus 로고    scopus 로고
    • N-glycosylation of Haloferax volcanii flagellins requires known Agl proteins and is essential for biosynthesis of stable flagella
    • Tripepi, M., J. You, S. Temel, O. Onder, D. Brisson, and M. Pohlschroder. 2012. N-glycosylation of Haloferax volcanii flagellins requires known Agl proteins and is essential for biosynthesis of stable flagella. J. Bacteriol. 194:4876-4887.
    • (2012) J. Bacteriol. , vol.194 , pp. 4876-4887
    • Tripepi, M.1    You, J.2    Temel, S.3    Onder, O.4    Brisson, D.5    Pohlschroder, M.6
  • 51
    • 65349147066 scopus 로고    scopus 로고
    • Identification of genes involved in the assembly and attachment of a novel flagellin N-linked tetrasaccharide important for motility in the archaeon Methanococcus maripaludis
    • Vandyke, D. J., J. Wu, S. M. Logan, J. F. Kelly, S. Mizuno, S. Aizawa, et al. 2009. Identification of genes involved in the assembly and attachment of a novel flagellin N-linked tetrasaccharide important for motility in the archaeon Methanococcus maripaludis. Mol. Microbiol. 72:633-644.
    • (2009) Mol. Microbiol. , vol.72 , pp. 633-644
    • Vandyke, D.J.1    Wu, J.2    Logan, S.M.3    Kelly, J.F.4    Mizuno, S.5    Aizawa, S.6
  • 52
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides - all of the theories are correct
    • Varki, A. 1993. Biological roles of oligosaccharides - all of the theories are correct. Glycobiology 3:97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 53
    • 0011928107 scopus 로고    scopus 로고
    • N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli
    • Wacker, M., D. Linton, P. G. Hitchen, M. Nita-Lazar, S. M. Haslam, S. J. North, et al. 2002. N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli. Science 298:1790-1793.
    • (2002) Science , vol.298 , pp. 1790-1793
    • Wacker, M.1    Linton, D.2    Hitchen, P.G.3    Nita-Lazar, M.4    Haslam, S.M.5    North, S.J.6
  • 54
    • 59749097200 scopus 로고    scopus 로고
    • Expanding and understanding the genetic toolbox of the hyperthermophilic genus Sulfolobus
    • Wagner, M., S. Berkner, M. Ajon, A. J. Driessen, G. Lipps, and S. V. Albers. 2009. Expanding and understanding the genetic toolbox of the hyperthermophilic genus Sulfolobus. Biochem. Soc. Trans. 37:97-101.
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 97-101
    • Wagner, M.1    Berkner, S.2    Ajon, M.3    Driessen, A.J.4    Lipps, G.5    Albers, S.V.6
  • 56
    • 84892988931 scopus 로고    scopus 로고
    • Investigation of the malE promoter and MalR, a positive regulator of the maltose regulon, for an improved expression system in Sulfolobus acidocaldarius
    • Wagner, M., A. Wagner, X. Ma, J. C. Kort, A. Ghosh, B. Rauch, et al. 2014. Investigation of the malE promoter and MalR, a positive regulator of the maltose regulon, for an improved expression system in Sulfolobus acidocaldarius. Appl. Environ. Microbiol. 80:1072-1081.
    • (2014) Appl. Environ. Microbiol. , vol.80 , pp. 1072-1081
    • Wagner, M.1    Wagner, A.2    Ma, X.3    Kort, J.C.4    Ghosh, A.5    Rauch, B.6
  • 57
    • 33646892873 scopus 로고    scopus 로고
    • Asparagine-linked protein glycosylation: from eukaryotic to prokaryotic systems
    • Weerapana, E., and B. Imperiali. 2006. Asparagine-linked protein glycosylation: from eukaryotic to prokaryotic systems. Glycobiology 16:91R-101R.
    • (2006) Glycobiology , vol.16
    • Weerapana, E.1    Imperiali, B.2
  • 58
    • 0037226536 scopus 로고    scopus 로고
    • Targeted disruption of the alpha-amylase gene in the hyperthermophilic archaeon Sulfolobus solfataricus
    • Worthington, P., V. Hoang, F. Perez-Pomares, and P. Blum. 2003. Targeted disruption of the alpha-amylase gene in the hyperthermophilic archaeon Sulfolobus solfataricus. J. Bacteriol. 185:482-488.
    • (2003) J. Bacteriol. , vol.185 , pp. 482-488
    • Worthington, P.1    Hoang, V.2    Perez-Pomares, F.3    Blum, P.4
  • 59
    • 0037033113 scopus 로고    scopus 로고
    • Studies on the function of oligosaccharyl transferase subunits. Stt3p is directly involved in the glycosylation process
    • Yan, Q., and W. J. Lennarz. 2002. Studies on the function of oligosaccharyl transferase subunits. Stt3p is directly involved in the glycosylation process. J. Biol. Chem. 277:47692-47700.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47692-47700
    • Yan, Q.1    Lennarz, W.J.2
  • 60
    • 77953240454 scopus 로고    scopus 로고
    • Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints
    • Zielinska, D. F., F. Gnad, J. R. Wisniewski, and M. Mann. 2010. Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints. Cell 141:897-907.
    • (2010) Cell , vol.141 , pp. 897-907
    • Zielinska, D.F.1    Gnad, F.2    Wisniewski, J.R.3    Mann, M.4
  • 61
    • 0018928663 scopus 로고
    • The Sulfolobus-Caldariella group - taxonomy on the basis of the structure of DNA-dependent RNA polymerases
    • Zillig, W., K. O. Stetter, S. Wunderl, W. Schulz, H. Priess, and I. Scholz. 1980. The Sulfolobus-Caldariella group - taxonomy on the basis of the structure of DNA-dependent RNA polymerases. Arch. Microbiol. 125:259-269.
    • (1980) Arch. Microbiol. , vol.125 , pp. 259-269
    • Zillig, W.1    Stetter, K.O.2    Wunderl, S.3    Schulz, W.4    Priess, H.5    Scholz, I.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.