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Volumn 195, Issue 10, 2013, Pages 2177-2186

Agl16, a thermophilic glycosyltransferase mediating the last step of N-Glycan biosynthesis in the thermoacidophilic crenarchaeon sulfolobus acidocaldarius

Author keywords

[No Author keywords available]

Indexed keywords

AGL16 PROTEIN; BACTERIAL ENZYME; GLYCOPEPTIDASE; GLYCOSYLTRANSFERASE; HEXOSE; PENTASACCHARIDE; UNCLASSIFIED DRUG;

EID: 84877305230     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00035-13     Document Type: Article
Times cited : (35)

References (44)
  • 2
    • 0032416590 scopus 로고    scopus 로고
    • 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
    • Zeitler R, Hochmuth E, Deutzmann R, Sumper M. 1998. 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. Glycobiology 8:1157-1164.
    • (1998) Glycobiology , vol.8 , pp. 1157-1164
    • Zeitler, R.1    Hochmuth, E.2    Deutzmann, R.3    Sumper, M.4
  • 3
    • 20444488776 scopus 로고    scopus 로고
    • Identification and characterization of the unique N-linked glycan common to the flagellins and S-layer glycoprotein of Methanococcus voltae
    • Voisin S, Houliston RS, Kelly J, Brisson JR, Watson D, Bardy SL, Jarrell KF, Logan SM. 2005. Identification and characterization of the unique N-linked glycan common to the flagellins and S-layer glycoprotein of Methanococcus voltae. J. Biol. Chem. 280:16586-16593.
    • (2005) J. Biol. Chem. , vol.280 , pp. 16586-16593
    • Voisin, S.1    Houliston, R.S.2    Kelly, J.3    Brisson, J.R.4    Watson, D.5    Bardy, S.L.6    Jarrell, K.F.7    Logan, S.M.8
  • 4
    • 0025605636 scopus 로고
    • Primary structure and glycosylation of the S-layer protein of Haloferax volcanii
    • Sumper M, Berg E, Mengele R, 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
  • 6
    • 0017278612 scopus 로고
    • Purification and characterization of a prokaryotic glycoprotein from cell envelope of Halobacterium salinarium
    • Mescher MF, Strominger JL. 1976. Purification and characterization of a prokaryotic glycoprotein from cell envelope of Halobacterium salinarium. J. Biol. Chem. 251:2005-2014.
    • (1976) J. Biol. Chem. , vol.251 , pp. 2005-2014
    • Mescher, M.F.1    Strominger, J.L.2
  • 7
    • 78249283543 scopus 로고    scopus 로고
    • The S-layer glycoprotein of the crenarchaeote Sulfolobus acidocaldarius is glycosylated at multiple sites with chitobioselinked N-glycans
    • doi:10.1155/2010/754101
    • Peyfoon E, Meyer B, Hitchen PG, Panico M, Morris HR, Haslam SM, Albers SV, Dell A. 2010. The S-layer glycoprotein of the crenarchaeote Sulfolobus acidocaldarius is glycosylated at multiple sites with chitobioselinked N-glycans. Archaea 2010:754101. doi:10.1155/2010/754101.
    • (2010) Archaea , vol.2010 , pp. 754101
    • Peyfoon, E.1    Meyer, B.2    Hitchen, P.G.3    Panico, M.4    Morris, H.R.5    Haslam, S.M.6    Albers, S.V.7    Dell, A.8
  • 8
    • 0025061226 scopus 로고
    • Three dimensional reconstruction of the surface protein of the extremely thermophilic archaebacterium Archaeoglobus fulgidus
    • Kessel M, Volker S, Santarius U, Huber R, Baumeister W. 1990. Three dimensional reconstruction of the surface protein of the extremely thermophilic archaebacterium Archaeoglobus fulgidus. Syst. Appl. Microbiol. 13:207-213.
    • (1990) Syst. Appl. Microbiol. , vol.13 , pp. 207-213
    • Kessel, M.1    Volker, S.2    Santarius, U.3    Huber, R.4    Baumeister, W.5
  • 9
    • 0000499006 scopus 로고
    • Three dimensional structure of the regular surface glycoprotein layer of Halobacterium volcanii from the Dead Sea
    • Kessel M, Wildhaber I, Cohen S, Baumeister 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    Wildhaber, I.2    Cohen, S.3    Baumeister, W.4
  • 12
    • 0035057117 scopus 로고    scopus 로고
    • Sugar transport in Sulfolobus solfataricus is mediated by two families of binding protein-dependent ABC transporters
    • Elferink MG, Albers SV, Konings WN, Driessen AJ. 2001. Sugar transport in Sulfolobus solfataricus is mediated by two families of binding protein-dependent ABC transporters. Mol. Microbiol. 39:1494-1503.
    • (2001) Mol. Microbiol. , vol.39 , pp. 1494-1503
    • Elferink, M.G.1    Albers, S.V.2    Konings, W.N.3    Driessen, A.J.4
  • 13
    • 33748757929 scopus 로고    scopus 로고
    • Archaeal flagella, bacterial flagella and type IV pili: a comparison of genes and posttranslational modifications
    • Ng SY, Chaban B, Jarrell KF. 2006. Archaeal flagella, bacterial flagella and type IV pili: a comparison of genes and posttranslational modifications. J. Mol. Microbiol. Biotechnol. 11:167-191.
    • (2006) J. Mol. Microbiol. Biotechnol. , vol.11 , pp. 167-191
    • Ng, S.Y.1    Chaban, B.2    Jarrell, K.F.3
  • 15
    • 84862754646 scopus 로고    scopus 로고
    • The archaellum: an old motility structure with a new name
    • Jarrell KF, Albers SV. 2012. The archaellum: an old motility structure with a new name. Trends Microbiol. 20:307-312.
    • (2012) Trends Microbiol. , vol.20 , pp. 307-312
    • Jarrell, K.F.1    Albers, S.V.2
  • 16
    • 84862953864 scopus 로고    scopus 로고
    • How hydrophobicity and the glycosylation site of glycans affect protein folding and stability: a molecular dynamics simulation
    • Lu D, Yang C, Liu Z. 2012. How hydrophobicity and the glycosylation site of glycans affect protein folding and stability: a molecular dynamics simulation. J. Phys. Chem. B 116:390-400.
    • (2012) J. Phys. Chem. B , vol.116 , pp. 390-400
    • Lu, D.1    Yang, C.2    Liu, Z.3
  • 17
    • 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, You J, Temel S, Onder O, Brisson D, Pohlschroder M. 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
  • 18
    • 77958099601 scopus 로고    scopus 로고
    • Protein glycosylation in bacteria: sweeter than ever
    • Nothaft H, Szymanski CM. 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
  • 19
    • 70349689931 scopus 로고    scopus 로고
    • Glycosyltransferases and oligosaccharyltransferases in Archaea: putative components of theN-glycosylation pathway in the third domain of life
    • Magidovich H, Eichler J. 2009. Glycosyltransferases and oligosaccharyltransferases in Archaea: putative components of theN-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
  • 20
    • 77950861521 scopus 로고    scopus 로고
    • Comparative structural biology of eubacterial and archaeal oligosaccharyltransferases
    • Maita N, Nyirenda J, Igura M, Kamishikiryo J, Kohda D. 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
  • 21
    • 77955433290 scopus 로고    scopus 로고
    • Protein glycosylation in Archaea: Sweet and extreme
    • Calo D, Kaminski L, Eichler J. 2010. Protein glycosylation in Archaea: Sweet and extreme. Glycobiology 20:1065-1076.
    • (2010) Glycobiology , vol.20 , pp. 1065-1076
    • Calo, D.1    Kaminski, L.2    Eichler, J.3
  • 22
    • 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, Voisin S, Kelly J, Logan SM, Jarrell KF. 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
  • 24
    • 0032808951 scopus 로고    scopus 로고
    • Glucose transport in the extremely thermoacidophilic Sulfolobus solfataricus involves a high-affinity membrane-integrated binding protein
    • Albers SV, Elferink MG, Charlebois RL, Sensen CW, Driessen AJ, Konings WN. 1999. Glucose transport in the extremely thermoacidophilic Sulfolobus solfataricus involves a high-affinity membrane-integrated binding protein. J. Bacteriol. 181:4285-4291.
    • (1999) J. Bacteriol. , vol.181 , pp. 4285-4291
    • Albers, S.V.1    Elferink, M.G.2    Charlebois, R.L.3    Sensen, C.W.4    Driessen, A.J.5    Konings, W.N.6
  • 25
    • 0033625671 scopus 로고    scopus 로고
    • Cytochrome b558/566 from the archaeon Sulfolobus acidocaldarius has a unique Asn-linked highly branched hexasaccharide chain containing 6-sulfoquinovose
    • Zahringer U, Moll H, Hettmann T, Knirel VA, Schafer G. 2000. Cytochrome b558/566 from the archaeon Sulfolobus acidocaldarius has a unique Asn-linked highly branched hexasaccharide chain containing 6-sulfoquinovose. Eur. J. Biochem. 267:4144-4149.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4144-4149
    • Zahringer, U.1    Moll, H.2    Hettmann, T.3    Knirel, V.A.4    Schafer, G.5
  • 27
    • 0031765216 scopus 로고    scopus 로고
    • Biosynthesis and function of the sulfolipid sulfoquinovosyl diacylglycerol
    • Benning C. 1998. Biosynthesis and function of the sulfolipid sulfoquinovosyl diacylglycerol. Annu. Rev. Plant Physiol. Plant Mol. Biol. 49:53-75.
    • (1998) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.49 , pp. 53-75
    • Benning, C.1
  • 29
    • 0015275944 scopus 로고
    • Sulfolobus: a new genus of sulfur-oxidizing bacteria living at low pH and high temperature
    • Brock TD, Brock KM, Belly RT, Weiss RL. 1972. Sulfolobus: a 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
  • 30
    • 34247515309 scopus 로고    scopus 로고
    • Identification of a system required for the functional surface localization of sugar binding proteins with class III signal peptides in Sulfolobus solfataricus
    • Zolghadr B, Weber S, Szabo Z, Driessen AJ, Albers SV. 2007. Identification of a system required for the functional surface localization of sugar binding proteins with class III signal peptides in Sulfolobus solfataricus. Mol. Microbiol. 64:795-806.
    • (2007) Mol. Microbiol. , vol.64 , pp. 795-806
    • Zolghadr, B.1    Weber, S.2    Szabo, Z.3    Driessen, A.J.4    Albers, S.V.5
  • 32
    • 27744478779 scopus 로고    scopus 로고
    • Homologous recombination of exogenousDNAwith the Sulfolobus acidocaldarius genome: properties and uses
    • Kurosawa N, Grogan DW. 2005. Homologous recombination of exogenousDNAwith 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
  • 34
    • 77951766898 scopus 로고    scopus 로고
    • Inducible and constitutive promoters for genetic systems in Sulfolobus acidocaldarius
    • Berkner S, Wlodkowski A, Albers SV, Lipps G. 2010. Inducible and constitutive promoters for genetic systems in Sulfolobus acidocaldarius. Extremophiles 14:249-259.
    • (2010) Extremophiles , vol.14 , pp. 249-259
    • Berkner, S.1    Wlodkowski, A.2    Albers, S.V.3    Lipps, G.4
  • 35
    • 0027311863 scopus 로고
    • Glycosyl transferases of O-antigen biosynthesis in Salmonella enterica: identification and characterization of transferase genes of groups B, C2, and E1
    • Liu D, Haase AM, Lindqvist L, Lindberg AA, Reeves PR. 1993. Glycosyl transferases of O-antigen biosynthesis in Salmonella enterica: identification and characterization of transferase genes of groups B, C2, and E1. J. Bacteriol. 175:3408-3413.
    • (1993) J. Bacteriol. , vol.175 , pp. 3408-3413
    • Liu, D.1    Haase, A.M.2    Lindqvist, L.3    Lindberg, A.A.4    Reeves, P.R.5
  • 36
    • 0033017192 scopus 로고    scopus 로고
    • Gene products required for surface expression of the capsular form of the group 1 K antigen in Escherichia coli (O9a:K30)
    • Drummelsmith J, Whitfield C. 1999. Gene products required for surface expression of the capsular form of the group 1 K antigen in Escherichia coli (O9a:K30). Mol. Microbiol. 31:1321-1332.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1321-1332
    • Drummelsmith, J.1    Whitfield, C.2
  • 37
    • 84155172916 scopus 로고    scopus 로고
    • Influence of cell surface structures on crenarchaeal biofilm formation using a thermostable green fluorescent protein
    • Henche AL, Koerdt A, Ghosh A, Albers SV. 2012. Influence of cell surface structures on crenarchaeal biofilm formation using a thermostable green fluorescent protein. Environ. Microbiol. 14:779-793.
    • (2012) Environ. Microbiol. , vol.14 , pp. 779-793
    • Henche, A.L.1    Koerdt, A.2    Ghosh, A.3    Albers, S.V.4
  • 38
    • 84873122419 scopus 로고    scopus 로고
    • Hot and sweet: protein glycosylation in Crenarchaeota
    • Meyer BH, Albers SV. 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
  • 39
    • 65549123777 scopus 로고    scopus 로고
    • Manual annotation, transcriptional analysis, and protein expression studies reveal novel genes in the agl cluster responsible for N-glycosylation in the halophilic archaeon Haloferax volcanii
    • Yurist-Doutsch S, Eichler J. 2009. Manual annotation, transcriptional analysis, and protein expression studies reveal novel genes in the agl cluster responsible for N-glycosylation in the halophilic archaeon Haloferax volcanii. J. Bacteriol. 191:3068-3075.
    • (2009) J. Bacteriol. , vol.191 , pp. 3068-3075
    • Yurist-Doutsch, S.1    Eichler, J.2
  • 40
    • 84870715118 scopus 로고    scopus 로고
    • AglS, a novel component of the Haloferax volcanii N-glycosylation pathway, is a dolichol phosphate-mannose mannosyltransferase
    • Cohen-Rosenzweig C, Yurist-Doutsch S, Eichler J. 2012. AglS, a novel component of the Haloferax volcanii N-glycosylation pathway, is a dolichol phosphate-mannose mannosyltransferase. J. Bacteriol. 194: 6909-6916.
    • (2012) J. Bacteriol. , vol.194 , pp. 6909-6916
    • Cohen-Rosenzweig, C.1    Yurist-Doutsch, S.2    Eichler, J.3
  • 41
    • 0032904470 scopus 로고    scopus 로고
    • The dolichol pathway of N-linked glycosylation
    • Burda P, Aebi M. 1999. The dolichol pathway of N-linked glycosylation. Biochim. Biophys. Acta 1426:239-257.
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 239-257
    • Burda, P.1    Aebi, M.2
  • 42
    • 33646892873 scopus 로고    scopus 로고
    • Asparagine-linked protein glycosylation: from eukaryotic to prokaryotic systems
    • Weerapana E, Imperiali B. 2006. Asparagine-linked protein glycosylation: from eukaryotic to prokaryotic systems. Glycobiology 16:91R-101R.
    • (2006) Glycobiology , vol.16
    • Weerapana, E.1    Imperiali, B.2
  • 43
    • 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 DJ, Wu J, Logan SM, Kelly JF, Mizuno S, Aizawa S, Jarrell KF. 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    Jarrell, K.F.7
  • 44
    • 58149483373 scopus 로고    scopus 로고
    • AglC and AglK are involved in biosynthesis and attachment of diacetylated glucuronic acid to the N-glycan in Methanococcus voltae
    • Chaban B, Logan SM, Kelly JF, Jarrell KF. 2009. AglC and AglK are involved in biosynthesis and attachment of diacetylated glucuronic acid to the N-glycan in Methanococcus voltae. J. Bacteriol. 191:187-195.
    • (2009) J. Bacteriol. , vol.191 , pp. 187-195
    • Chaban, B.1    Logan, S.M.2    Kelly, J.F.3    Jarrell, K.F.4


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