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Volumn 80, Issue 2, 2014, Pages 486-496

Substrate Promiscuity: AglB, the Archaeal Oligosaccharyltransferase, Can Process a Variety of Lipid-Linked Glycans

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL COMPOSITIONS; FUNCTIONAL SIMILARITY; HALOFERAX VOLCANII; N-GLYCOSYLATION; OLIGOSACCHARYLTRANSFERASE; STRUCTURAL HOMOLOGY; SUBSTRATE SPECIFICITY; TARGET PROTEINS;

EID: 84892466104     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.03191-13     Document Type: Article
Times cited : (28)

References (45)
  • 1
    • 79961171901 scopus 로고    scopus 로고
    • Oligosaccharyltransferase: the central enzyme of N-linked protein glycosylation
    • Mohorko E, Glockshuber R, Aebi M. 2011. Oligosaccharyltransferase: the central enzyme of N-linked protein glycosylation. J. Inherit. Metab. Dis. 34:869-878. http://dx.doi.org/10.1007/s10545-011-9337-1.
    • (2011) J. Inherit. Metab. Dis. , vol.34 , pp. 869-878
    • Mohorko, E.1    Glockshuber, R.2    Aebi, M.3
  • 2
    • 79958165964 scopus 로고    scopus 로고
    • The expanding horizons of asparaginelinked glycosylation
    • Larkin A, Imperiali B. 2011. The expanding horizons of asparaginelinked glycosylation. Biochemistry 50:4411-4426. http://dx.doi.org/10.1021/bi200346n.
    • (2011) Biochemistry , vol.50 , pp. 4411-4426
    • Larkin, A.1    Imperiali, B.2
  • 3
    • 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. http://dx.doi.org/10.1038/nrmicro2383.
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 765-778
    • Nothaft, H.1    Szymanski, C.M.2
  • 4
    • 84874113719 scopus 로고    scopus 로고
    • Extreme sweetness: protein glycosylation in archaea
    • Eichler J. 2013. Extreme sweetness: protein glycosylation in archaea. Nat. Rev. Microbiol. 11:151-156. http://dx.doi.org/10.1038/nrmicro2957.
    • (2013) Nat. Rev. Microbiol. , vol.11 , pp. 151-156
    • Eichler, J.1
  • 5
    • 0032960606 scopus 로고    scopus 로고
    • The oligosaccharyltransferase complex from yeast
    • Knauer R, Lehle L. 1999. The oligosaccharyltransferase complex from yeast. Biochim. Biophys. Acta 1426:259-273. http://dx.doi.org/10.1016/S0304-4165(98)00128-7.
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 259-273
    • Knauer, R.1    Lehle, L.2
  • 7
    • 38049051311 scopus 로고    scopus 로고
    • Structure-guided identification of a new catalytic motif of oligosaccharyltransferase
    • Igura M, Maita N, Kamishikiryo J, Yamada M, Obita T, Maenaka K, Kohda D. 2008. Structure-guided identification of a new catalytic motif of oligosaccharyltransferase. EMBO J. 27:234-243. http://dx.doi.org/10.1038/sj.emboj.7601940.
    • (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    Kohda, D.7
  • 9
    • 80053469048 scopus 로고    scopus 로고
    • Mechanisms and principles of N-linked protein glycosylation
    • Schwarz F, Aebi M. 2011. Mechanisms and principles of N-linked protein glycosylation. Curr. Opin. Struct. Biol. 21:576-582. http://dx.doi.org/10.1016/j.sbi.2011.08.005.
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 576-582
    • Schwarz, F.1    Aebi, M.2
  • 11
    • 0019329774 scopus 로고
    • Halobacterial glycoprotein saccharides contain covalently linked sulphate
    • Wieland F, Dompert W, Bernhardt G, Sumper M. 1980. Halobacterial glycoprotein saccharides contain covalently linked sulphate. FEBS Lett. 120:110-114. http://dx.doi.org/10.1016/0014-5793(80)81058-1.
    • (1980) FEBS Lett. , vol.120 , pp. 110-114
    • Wieland, F.1    Dompert, W.2    Bernhardt, G.3    Sumper, M.4
  • 14
    • 0024346543 scopus 로고
    • Structure and biosynthesis of prokaryotic glycoproteins
    • Lechner J, Wieland F. 1989. Structure and biosynthesis of prokaryotic glycoproteins. Annu. Rev. Biochem. 58:173-194. http://dx.doi.org/10.1146/annurev.bi.58.070189.001133.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 173-194
    • Lechner, J.1    Wieland, F.2
  • 15
    • 78649546006 scopus 로고    scopus 로고
    • Distinct glycan-charged phosphodolichol carriers are required for the assembly of the pentasaccharide N-linked to the Haloferax volcanii S-layer glycoprotein
    • Guan Z, Naparstek S, Kaminski L, Konrad Z, Eichler J. 2010. Distinct glycan-charged phosphodolichol carriers are required for the assembly of the pentasaccharide N-linked to the Haloferax volcanii S-layer glycoprotein. Mol. Microbiol. 78:1294-1303. http://dx.doi.org/10.1111/j.1365-2958.2010.07405.x.
    • (2010) Mol. Microbiol. , vol.78 , pp. 1294-1303
    • Guan, Z.1    Naparstek, S.2    Kaminski, L.3    Konrad, Z.4    Eichler, J.5
  • 16
    • 33748517628 scopus 로고    scopus 로고
    • Protein N-glycosylation in Archaea: defining Haloferax volcanii genes involved in S-layer glycoprotein glycosylation
    • Abu-Qarn M, Eichler J. 2006. Protein N-glycosylation in Archaea: defining Haloferax volcanii genes involved in S-layer glycoprotein glycosylation. Mol. Microbiol. 61:511-525. http://dx.doi.org/10.1111/j.1365-2958.2006.05252.x.
    • (2006) Mol. Microbiol. , vol.61 , pp. 511-525
    • Abu-Qarn, M.1    Eichler, J.2
  • 17
    • 79953880285 scopus 로고    scopus 로고
    • Quantitative assessment of the preferences for the amino acid residues flanking archaeal N-linked glycosylation sites
    • Igura M, Kohda D. 2011. Quantitative assessment of the preferences for the amino acid residues flanking archaeal N-linked glycosylation sites. Glycobiology 21:575-583. http://dx.doi.org/10.1093/glycob/cwq196.
    • (2011) Glycobiology , vol.21 , pp. 575-583
    • Igura, M.1    Kohda, D.2
  • 18
    • 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, Eichler J. 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. http://dx.doi.org/10.1111/j.1574-6968.2009.01775.x.
    • (2009) FEMS Microbiol. Lett. , vol.300 , pp. 122-130
    • Magidovich, H.1    Eichler, J.2
  • 19
    • 84878106864 scopus 로고    scopus 로고
    • Phylogenetic- and genome-derived insight into the evolution of N-glycosylation in Archaea.
    • Kaminski L, Lurie-Weinberger MN, Allers T, Gophna U, Eichler J. 2013 Phylogenetic- and genome-derived insight into the evolution of N-glycosylation in Archaea. Mol. Phylogenet. Evol. 68:327-339. http://dx.doi.org/10.1016/j.ympev.2013.03.024.
    • (2013) Mol. Phylogenet. Evol. , vol.68 , pp. 327-339
    • Kaminski, L.1    Lurie-Weinberger, M.N.2    Allers, T.3    Gophna, U.4    Eichler, J.5
  • 20
    • 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, Yurist-Doutsch S, Giordano A, Trauner A, Morris HR, Hitchen P, Medalia O, Dell A, Eichler J. 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. http://dx.doi.org/10.1016/j.jmb.2007.10.042.
    • (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    Medalia, O.7    Dell, A.8    Eichler, J.9
  • 21
    • 77950194523 scopus 로고    scopus 로고
    • AglP is a S-adenosyl-L-methioninedependent methyltransferase that participates in the N-glycosylation pathway of Haloferax volcanii
    • Magidovich H, Yurist-Doutsch S, Konrad Z, Ventura VV, Dell A, Hitchen PG, Eichler J. 2010. AglP is a S-adenosyl-L-methioninedependent methyltransferase that participates in the N-glycosylation pathway of Haloferax volcanii. Mol. Microbiol. 76:190-199. http://dx.doi.org/10.1111/j.1365-2958.2010.07090.x.
    • (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    Eichler, J.7
  • 22
    • 80051928511 scopus 로고    scopus 로고
    • Different routes to the same ending: comparing the N-glycosylation processes of Haloferax volcanii and Haloarcula marismortui, two halophilic archaea from the Dead Sea
    • Calo D, Guan Z, Naparstek S, Eichler J. 2011. Different routes to the same ending: comparing the N-glycosylation processes of Haloferax volcanii and Haloarcula marismortui, two halophilic archaea from the Dead Sea. Mol. Microbiol. 81:1166-1177. http://dx.doi.org/10.1111/j.1365-2958.2011.07781.x.
    • (2011) Mol. Microbiol. , vol.81 , pp. 1166-1177
    • Calo, D.1    Guan, Z.2    Naparstek, S.3    Eichler, J.4
  • 23
    • 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
  • 24
    • 2342625231 scopus 로고    scopus 로고
    • Development of additional selectable markers for the halophilic archaeon Haloferax volcanii based on the leuB and trpA genes
    • Allers T, Ngo HP, Mevarech M, Lloyd RG. 2004. Development of additional selectable markers for the halophilic archaeon Haloferax volcanii based on the leuB and trpA genes. Appl. Environ. Microbiol. 70:943- 953. http://dx.doi.org/10.1128/AEM.70.2.943-953.2004.
    • (2004) Appl. Environ. Microbiol. , vol.70
    • Allers, T.1    Ngo, H.P.2    Mevarech, M.3    Lloyd, R.G.4
  • 25
    • 0022003836 scopus 로고
    • Genetic transfer in Halobacterium volcanii
    • Mevarech M, 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
  • 26
    • 0017195049 scopus 로고
    • Hydrophobic chromatography and fractionation of enzymes from extremely halophilic bacteria using decreasing concentration gradients of ammonium sulfate
    • Mevarech M, Leicht W, Werber MM. 1976. Hydrophobic chromatography and fractionation of enzymes from extremely halophilic bacteria using decreasing concentration gradients of ammonium sulfate. Biochemistry 15:2383-2387. http://dx.doi.org/10.1021/bi00656a021.
    • (1976) Biochemistry , vol.15 , pp. 2383-2387
    • Mevarech, M.1    Leicht, W.2    Werber, M.M.3
  • 27
    • 0016376428 scopus 로고
    • Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
    • Oesterhelt D, Stoeckenius W. 1974. Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane. Methods Enzymol. 31:667-678. http://dx.doi.org/10.1016/0076-6879(74)31072-5.
    • (1974) Methods Enzymol. , vol.31 , pp. 667-678
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 28
    • 0019214089 scopus 로고
    • Behaviour of mixed populations of halophilic bacteria in continuous cultures
    • Rodriguez-Valera F, Ruiz-Berraquero F, Ramos-Cormenzana A. 1980. Behaviour of mixed populations of halophilic bacteria in continuous cultures. Can. J. Microbiol. 26:1259-1263. http://dx.doi.org/10.1139/m80-210.
    • (1980) Can. J. Microbiol. , vol.26 , pp. 1259-1263
    • Rodriguez-Valera, F.1    Ruiz-Berraquero, F.2    Ramos-Cormenzana, A.3
  • 29
    • 57349184123 scopus 로고    scopus 로고
    • Defining the topology of the N-glycosylation pathway in the halophilic archaeon Haloferax volcanii
    • Plavner N, Eichler J. 2008. Defining the topology of the N-glycosylation pathway in the halophilic archaeon Haloferax volcanii. J. Bacteriol. 190: 8045-8052. http://dx.doi.org/10.1128/JB.01200-08.
    • (2008) J. Bacteriol. , vol.190 , pp. 8045-8052
    • Plavner, N.1    Eichler, J.2
  • 30
    • 0024730742 scopus 로고
    • Transformation of the archaebacterium Halobacterium volcanii with genomic DNA
    • Cline SW, Schalkwyk LC, Doolittle WF. 1989. Transformation of the archaebacterium Halobacterium volcanii with genomic DNA. J. Bacteriol. 171:4987-4991.
    • (1989) J. Bacteriol. , vol.171 , pp. 4987-4991
    • Cline, S.W.1    Schalkwyk, L.C.2    Doolittle, W.F.3
  • 31
  • 32
    • 0038305947 scopus 로고    scopus 로고
    • Post-translational secretion of fusion proteins in the halophilic archaea Haloferax volcanii
    • Irihimovitch V, Eichler J. 2003. Post-translational secretion of fusion proteins in the halophilic archaea Haloferax volcanii. J. Biol. Chem. 278: 12881-12887. http://dx.doi.org/10.1074/jbc.M210762200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12881-12887
    • Irihimovitch, V.1    Eichler, J.2
  • 33
    • 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. http://dx.doi.org/10.1074/jbc.M109.081752.
    • (2010) J. Biol. Chem. , vol.285 , pp. 4941-4950
    • Maita, N.1    Nyirenda, J.2    Igura, M.3    Kamishikiryo, J.4    Kohda, D.5
  • 34
    • 84861400022 scopus 로고    scopus 로고
    • Crystal structure of the C-terminal globular domain of oligosaccharyltransferase from Archaeoglobus fulgidus at 1.75 Å resolution
    • Matsumoto S, Igura M, Nyirenda J, Matsumoto M, Yuzawa S, Noda N, Inagaki F, Kohda D. 2012. Crystal structure of the C-terminal globular domain of oligosaccharyltransferase from Archaeoglobus fulgidus at 1.75 Å resolution. Biochemistry 51:4157- 4166. http://dx.doi.org/10.1021/bi300076u.
    • (2012) Biochemistry , vol.51
    • Matsumoto, S.1    Igura, M.2    Nyirenda, J.3    Matsumoto, M.4    Yuzawa, S.5    Noda, N.6    Inagaki, F.7    Kohda, D.8
  • 35
    • 0038309565 scopus 로고    scopus 로고
    • Three monophyletic superfamilies account for the majority of the known glycosyltransferases
    • Liu J, Mushegian A. 2003. Three monophyletic superfamilies account for the majority of the known glycosyltransferases. Protein Sci. 12:1418- 1431. http://dx.doi.org/10.1110/ps.0302103.
    • (2003) Protein Sci. , vol.12
    • Liu, J.1    Mushegian, A.2
  • 36
    • 79959191882 scopus 로고    scopus 로고
    • X-ray structure of a bacterial oligosaccharyltransferase
    • Lizak C, Gerber S, Numao S, Aebi M, Locher KP. 2011. X-ray structure of a bacterial oligosaccharyltransferase. Nature 474:350-355. http://dx.doi.org/10.1038/nature10151.
    • (2011) Nature , vol.474 , pp. 350-355
    • Lizak, C.1    Gerber, S.2    Numao, S.3    Aebi, M.4    Locher, K.P.5
  • 37
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: a case study using the Phyre server
    • Kelley LA, Sternberg MJ. 2009. Protein structure prediction on the Web: a case study using the Phyre server. Nat. Protoc. 4:363-371. http://dx.doi.org/10.1038/nprot.2009.2.
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 38
    • 84855443549 scopus 로고    scopus 로고
    • At the membrane frontier: a prospectus on the remarkable evolutionary conservation of polyprenols and polyprenyl- phosphates
    • Hartley MD, Imperiali B. 2012. At the membrane frontier: a prospectus on the remarkable evolutionary conservation of polyprenols and polyprenyl- phosphates. Arch. Biochem. Biophys. 517:83-97. http://dx.doi.org/10.1016/j.abb.2011.10.018.
    • (2012) Arch. Biochem. Biophys. , vol.517 , pp. 83-97
    • Hartley, M.D.1    Imperiali, B.2
  • 39
    • 84866320274 scopus 로고    scopus 로고
    • Complete genome sequence of the metabolically versatile halophilic archaeon Haloferax mediterranei, a poly(3- hydroxybutyrate-co-3-hydroxyvalerate) producer
    • Han J, Zhang F, Hou J, Liu X, Li M, Liu H, Cai L, Zhang B, Chen Y, Zhou J, Hu S, Xiang H. 2012. Complete genome sequence of the metabolically versatile halophilic archaeon Haloferax mediterranei, a poly(3- hydroxybutyrate-co-3-hydroxyvalerate) producer. J. Bacteriol. 194:4463- 4464. http://dx.doi.org/10.1128/JB.00880-12.
    • (2012) J. Bacteriol. , vol.194
    • Han, J.1    Zhang, F.2    Hou, J.3    Liu, X.4    Li, M.5    Liu, H.6    Cai, L.7    Zhang, B.8    Chen, Y.9    Zhou, J.10    Hu, S.11    Xiang, H.12
  • 40
    • 0000549004 scopus 로고
    • Halobacterium mediterranei spec, nov., anewcarbohydrate-utilizing extreme halophile
    • Rodriguez-Valera F, Juez G, Kushner DJ. 1983. Halobacterium mediterranei spec, nov., anewcarbohydrate-utilizing extreme halophile. Syst. Appl. Microbiol. 4:369-381. http://dx.doi.org/10.1016/S0723-2020(83)80021-6.
    • (1983) Syst. Appl. Microbiol. , vol.4 , pp. 369-381
    • Rodriguez-Valera, F.1    Juez, G.2    Kushner, D.J.3
  • 41
    • 0017851894 scopus 로고
    • Glycosylation of the surface glycoprotein of Halobacterium salinarium via a cyclic pathway of lipidlinked intermediates
    • Mescher MF, Strominger JL. 1978. Glycosylation of the surface glycoprotein of Halobacterium salinarium via a cyclic pathway of lipidlinked intermediates. FEBS Lett. 89:37- 41. http://dx.doi.org/10.1016/0014-5793(78)80517-1.
    • (1978) FEBS Lett. , vol.89
    • Mescher, M.F.1    Strominger, J.L.2
  • 42
    • 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. http://dx.doi.org/10.1016/j.tim.2012.04.007.
    • (2012) Trends Microbiol. , vol.20 , pp. 307-312
    • Jarrell, K.F.1    Albers, S.V.2
  • 43
    • 0021849616 scopus 로고
    • Transient methylation of dolichyl oligosaccharides is an obligatory step in halobacterial sulfated glycoprotein biosynthesis
    • Lechner J, Wieland F, 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
  • 44
    • 77956608454 scopus 로고    scopus 로고
    • Towards glycoengineering in archaea: replacement of Haloferax volcanii AglD with homologous glycosyltransferases from other halophilic archaea
    • Calo D, Eilam Y, Lichtenstein RG, Eichler J. 2010. Towards glycoengineering in archaea: replacement of Haloferax volcanii AglD with homologous glycosyltransferases from other halophilic archaea. Appl. Environ. Microbiol. 76:5684-5692. http://dx.doi.org/10.1128/AEM.00681-10.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 5684-5692
    • Calo, D.1    Eilam, Y.2    Lichtenstein, R.G.3    Eichler, J.4
  • 45
    • 79960108098 scopus 로고    scopus 로고
    • Glyco-engineering in Archaea: differential N-glycosylation of the S-layer glycoprotein in a transformed Haloferax volcanii strain
    • Calo D, Guan Z, Eichler J. 2011. Glyco-engineering in Archaea: differential N-glycosylation of the S-layer glycoprotein in a transformed Haloferax volcanii strain. Microb. Biotechnol. 4:461-470. http://dx.doi.org/10.1111/j.1751-7915.2011.00250.x.
    • (2011) Microb. Biotechnol. , vol.4 , pp. 461-470
    • Calo, D.1    Guan, Z.2    Eichler, J.3


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