메뉴 건너뛰기




Volumn 300, Issue 1, 2009, Pages 122-130

Glycosyltransferases and oligosaccharyltransferases in Archaea: Putative components of the N-glycosylation pathway in the third domain of life

Author keywords

Archaea; Glycosyltransferase; N glycosylation; Oligosaccharyltransferase

Indexed keywords

BACTERIAL ENZYME; GLYCOSYLTRANSFERASE; OLIGOSACCHARYLTRANSFERASE; UNCLASSIFIED DRUG;

EID: 70349689931     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1111/j.1574-6968.2009.01775.x     Document Type: Article
Times cited : (62)

References (40)
  • 1
    • 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.
    • (2006) Mol Microbiol , vol.61 , pp. 511-525
    • Abu-Qarn, M.1    Eichler, J.2
  • 2
    • 34250808964 scopus 로고    scopus 로고
    • An analysis of amino acid sequences surrounding archaeal glycoprotein sequons
    • Abu-Qarn M Eichler J (2007) An analysis of amino acid sequences surrounding archaeal glycoprotein sequons. Archaea 2 : 73 81.
    • (2007) Archaea , vol.2 , pp. 73-81
    • Abu-Qarn, M.1    Eichler, J.2
  • 3
  • 4
    • 53249147141 scopus 로고    scopus 로고
    • Not just for Eukarya anymore: N-glycosylation in Bacteria and Archaea
    • Abu-Qarn M, Eichler JN Sharon N (2008a) Not just for Eukarya anymore: N-glycosylation in Bacteria and Archaea. Curr Opin Struc Biol 18 : 544 550.
    • (2008) Curr Opin Struc Biol , vol.18 , pp. 544-550
    • Abu-Qarn, M.1    Eichler, J.N.2    Sharon, N.3
  • 5
    • 42549147096 scopus 로고    scopus 로고
    • Identification of AglE, a second glycosyltransferase involved in N-glycosylation of the Haloferax volcanii S-layer glycoprotein
    • Abu-Qarn M, Giordano A, Battaglia F, Trauner A, Hitchen P, Morris HR, Dell A Eichler J (2008b) Identification of AglE, a second glycosyltransferase involved in N-glycosylation of the Haloferax volcanii S-layer glycoprotein. J Bacteriol 190 : 3140 3146.
    • (2008) J Bacteriol , vol.190 , pp. 3140-3146
    • Abu-Qarn, M.1    Giordano, A.2    Battaglia, F.3    Trauner, A.4    Hitchen, P.5    Morris, H.R.6    Dell, A.7    Eichler, J.8
  • 6
    • 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
  • 7
    • 0030843984 scopus 로고    scopus 로고
    • A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities
    • Campbell JA, Davies GJ, Bulone V Henrissat B (1997) A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem J 326 : 929 939.
    • (1997) Biochem J , vol.326 , pp. 929-939
    • Campbell, J.A.1    Davies, G.J.2    Bulone, V.3    Henrissat, B.4
  • 9
    • 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
  • 10
    • 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
  • 11
    • 0037466315 scopus 로고    scopus 로고
    • An evolving hierarchical family classification for glycosyltransferases
    • Coutinho PM, Deleury E, Davies GJ Henrissat B (2003) An evolving hierarchical family classification for glycosyltransferases. J Mol Biol 328 : 307 317.
    • (2003) J Mol Biol , vol.328 , pp. 307-317
    • Coutinho, P.M.1    Deleury, E.2    Davies, G.J.3    Henrissat, B.4
  • 12
    • 24944463449 scopus 로고    scopus 로고
    • Post-translational protein modification in Archaea
    • Eichler J Adams MWW (2005) Post-translational protein modification in Archaea. Microbiol Mol Biol R 69 : 393 425.
    • (2005) Microbiol Mol Biol R , vol.69 , pp. 393-425
    • Eichler, J.1    Adams, M.W.W.2
  • 14
    • 0037007636 scopus 로고    scopus 로고
    • A new phylum of Archaea represented by a nanosized hyperthermophilic symbiont
    • Huber H, Hohn MJ, Rachel R, Fuchs T, Wimmer VC Stetter KO (2002) A new phylum of Archaea represented by a nanosized hyperthermophilic symbiont. Nature 417 : 63 67.
    • (2002) Nature , vol.417 , pp. 63-67
    • Huber, H.1    Hohn, M.J.2    Rachel, R.3    Fuchs, T.4    Wimmer, V.C.5    Stetter, K.O.6
  • 15
    • 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.
    • (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
  • 16
    • 33645103490 scopus 로고    scopus 로고
    • An evolving view of the eukaryotic oligosaccharyltransferase
    • Kelleher DJ Gilmore R (2006) An evolving view of the eukaryotic oligosaccharyltransferase. Glycobiology 16 : 47R 62R.
    • (2006) Glycobiology , vol.16
    • Kelleher, D.J.1    Gilmore, R.2
  • 17
    • 33646564396 scopus 로고    scopus 로고
    • Definition of the bacterial N-glycosylation site consensus sequence
    • Kowarik M, Young NM, Numao S et al 2006) Definition of the bacterial N-glycosylation site consensus sequence. EMBO J 25 : 1957 1966.
    • (2006) EMBO J , vol.25 , pp. 1957-1966
    • Kowarik, M.1    Young, N.M.2    Numao, S.3    Al, E.4
  • 19
    • 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.
    • (1989) Annu Rev Biochem , vol.58 , pp. 173-194
    • Lechner, J.1    Wieland, F.2
  • 20
    • 0021925851 scopus 로고
    • Biosynthesis of sulfated saccharides N-glycosidically linked to the protein via glucose. Purification and identification of sulfated dolichyl monophosphoryl tetrasaccharides from halobacteria
    • Lechner J, Wieland F Sumper M (1985) Biosynthesis of sulfated saccharides N-glycosidically linked to the protein via glucose. Purification and identification of sulfated dolichyl monophosphoryl tetrasaccharides from halobacteria. J Biol Chem 260 : 860 866.
    • (1985) J Biol Chem , vol.260 , pp. 860-866
    • Lechner, J.1    Wieland, F.2    Sumper, M.3
  • 22
    • 0016342403 scopus 로고
    • The nature and metabolism of the carbohydrate-peptide linkages of glycoproteins
    • Marshall RD (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, R.D.1
  • 23
    • 0017278612 scopus 로고
    • Purification and characterization of a prokaryotic glycoprotein from the cell envelope of Halobacterium salinarium
    • Mescher MF Strominger JL (1976) Purification and characterization of a prokaryotic glycoprotein from the 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
  • 25
    • 0022648410 scopus 로고
    • Asparaginyl-N-acetylgalactosamine. Linkage unit of halobacterial glycosaminoglycan
    • Paul G, Lottspeich F Wieland F (1986) Asparaginyl-N-acetylgalactosamine. Linkage unit of halobacterial glycosaminoglycan. J Biol Chem 261 : 1020 1024.
    • (1986) J Biol Chem , vol.261 , pp. 1020-1024
    • Paul, G.1    Lottspeich, F.2    Wieland, F.3
  • 26
    • 40449104807 scopus 로고    scopus 로고
    • Identification of the archaeal alg7 gene homolog (N-acetylglucosamine-1- phosphate transferase) of the N-linked glycosylation system by cross-domain complementation in yeast
    • Shams-Eldin H, Chaban B, Niehus S, Schwarz RT Jarrell KF (2008) Identification of the archaeal alg7 gene homolog (N-acetylglucosamine-1- phosphate transferase) of the N-linked glycosylation system by cross-domain complementation in yeast. J Bacteriol 190 : 2217 2220.
    • (2008) J Bacteriol , vol.190 , pp. 2217-2220
    • Shams-Eldin, H.1    Chaban, B.2    Niehus, S.3    Schwarz, R.T.4    Jarrell, K.F.5
  • 27
    • 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
  • 28
    • 14544282378 scopus 로고    scopus 로고
    • Protein glycosylation in bacterial mucosal pathogens
    • Szymanski CM Wren BW (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
  • 29
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular evolutionary genetics analysis (MEGA) software version 4.0
    • Tamura K, Dudley J, Nei M Kumar S (2007) MEGA4: Molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol Biol Evol 24 : 1596 1599.
    • (2007) Mol Biol Evol , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 30
    • 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 SI 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.I.6    Jarrell, K.F.7
  • 31
    • 0031976097 scopus 로고    scopus 로고
    • Factors controlling the glycosylation potential of the Golgi apparatus
    • Varki A (1998) Factors controlling the glycosylation potential of the Golgi apparatus. Trends Cell Biol 8 : 34 40.
    • (1998) Trends Cell Biol , vol.8 , pp. 34-40
    • Varki, A.1
  • 32
    • 0011928107 scopus 로고    scopus 로고
    • N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli
    • Wacker M, Linton D, Hitchen PG 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    Al, E.4
  • 33
    • 0242300069 scopus 로고    scopus 로고
    • The genome of Nanoarchaeum equitans: Insights into early archaeal evolution and derived parasitism
    • Waters E, Hohn MJ, Ahel I et al 2003) The genome of Nanoarchaeum equitans: insights into early archaeal evolution and derived parasitism. P Natl Acad Sci USA 100 : 12984 12988.
    • (2003) P Natl Acad Sci USA , vol.100 , pp. 12984-12988
    • Waters, E.1    Hohn, M.J.2    Ahel, I.3    Al, E.4
  • 34
    • 33646892873 scopus 로고    scopus 로고
    • Asparagine-linked protein glycosylation: From eukaryotic to prokaryotic systems
    • Weerepana E Imperiali B (2006) Asparagine-linked protein glycosylation: from eukaryotic to prokaryotic systems. Glycobiology 16 : 91R 101R.
    • (2006) Glycobiology , vol.16
    • Weerepana, E.1    Imperiali, B.2
  • 35
    • 0037033113 scopus 로고    scopus 로고
    • Studies on the function of oligosaccharyl transferase subunits. Stt3p is directly involved in the glycosylation process
    • Yan Q Lennarz WJ (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
  • 36
    • 0037044765 scopus 로고    scopus 로고
    • Structure of the N-linked glycan present on multiple glycoproteins in the Gram-negative bacterium, Campylobacter jejuni
    • Young NM, Brisson JR, Kelly J et al 2002) Structure of the N-linked glycan present on multiple glycoproteins in the Gram-negative bacterium, Campylobacter jejuni. J Biol Chem 277 : 42530 42539.
    • (2002) J Biol Chem , vol.277 , pp. 42530-42539
    • Young, N.M.1    Brisson, J.R.2    Kelly, J.3    Al, E.4
  • 37
    • 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
  • 39
    • 49249084955 scopus 로고    scopus 로고
    • AglF, aglG and aglI, novel members of a gene cluster involved in the N-glycosylation of the Haloferax volcanii S-layer glycoprotein
    • Yurist-Doutsch S, Abu-Qarn M, Battaglia F, Morris HR, Hitchen PG, Dell A Eichler J (2008b) aglF, aglG and aglI, novel members of a gene cluster involved in the N-glycosylation of the Haloferax volcanii S-layer glycoprotein. Mol Microbiol 69 : 1234 1245.
    • (2008) Mol Microbiol , vol.69 , pp. 1234-1245
    • Yurist-Doutsch, S.1    Abu-Qarn, M.2    Battaglia, F.3    Morris, H.R.4    Hitchen, P.G.5    Dell, A.6    Eichler, J.7
  • 40
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.