메뉴 건너뛰기




Volumn 10, Issue 10, 2014, Pages 816-822

Engineered oligosaccharyltransferases with greatly relaxed acceptor-site specificity

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; BACTERIAL PROTEIN; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE - PROTEIN GLYCOTRANSFERASE; GLYCOSYLTRANSFERASE; MEMBRANE PROTEIN; RECOMBINANT PROTEIN;

EID: 84922066686     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.1609     Document Type: Article
Times cited : (55)

References (37)
  • 1
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • Apweiler, R., Hermjakob, H., Sharon, N. On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim. Biophys. Acta 1473, 4-8 (1999).
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 2
    • 77953240454 scopus 로고    scopus 로고
    • Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints
    • Zielinska, D. F., Gnad, F., Wisniewski, J. R., Mann, M. Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints. Cell 141, 897-907 (2010).
    • (2010) Cell , vol.141 , pp. 897-907
    • Zielinska, D.F.1    Gnad, F.2    Wisniewski, J.R.3    Mann, M.4
  • 3
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • Helenius, A., Aebi, M. Intracellular functions of N-linked glycans. Science 291, 2364-2369 (2001).
    • (2001) Science , vol.291 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 4
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • Helenius, A., Aebi, M. Roles of N-linked glycans in the endoplasmic reticulum. Annu. Rev. Biochem. 73, 1019-1049 (2004).
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 5
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • Varki, A. Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 3, 97-130 (1993).
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 6
    • 33644830238 scopus 로고    scopus 로고
    • N-linked oligosaccharides as outfitters for glycoprotein folding, form and function
    • Mitra, N., Sinha, S., Ramya, T. N., Surolia, A. N-linked oligosaccharides as outfitters for glycoprotein folding, form and function. Trends Biochem. Sci. 31, 156-163 (2006).
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 156-163
    • Mitra, N.1    Sinha, S.2    Ramya, T.N.3    Surolia, A.4
  • 7
  • 8
    • 53249147141 scopus 로고    scopus 로고
    • Not just for Eukarya anymore: Protein glycosylation in Bacteria and Archaea
    • Abu-Qarn, M., Eichler, J., Sharon, N. Not just for Eukarya anymore: protein glycosylation in Bacteria and Archaea. Curr. Opin. Struct. Biol. 18, 544-550 (2008).
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 544-550
    • Abu-Qarn, M.1    Eichler, J.2    Sharon, N.3
  • 9
    • 80053469048 scopus 로고    scopus 로고
    • Mechanisms and principles of N-linked protein glycosylation
    • Schwarz, F., Aebi, M. Mechanisms and principles of N-linked protein glycosylation. Curr. Opin. Struct. Biol. 21, 576-582 (2011).
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 576-582
    • Schwarz, F.1    Aebi, M.2
  • 10
    • 14544282378 scopus 로고    scopus 로고
    • Protein glycosylation in bacterial mucosal pathogens
    • Szymanski, C. M., Wren, B. W. Protein glycosylation in bacterial mucosal pathogens. Nat. Rev. Microbiol. 3, 225-237 (2005).
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 225-237
    • Szymanski, C.M.1    Wren, B.W.2
  • 11
    • 84879126165 scopus 로고    scopus 로고
    • Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis
    • Larkin, A., Chang, M. M., Whitworth, G. E., Imperiali, B. Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis. Nat. Chem. Biol. 9, 367-373 (2013).
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 367-373
    • Larkin, A.1    Chang, M.M.2    Whitworth, G.E.3    Imperiali, B.4
  • 12
    • 0028834273 scopus 로고
    • STT3, a highly conserved protein required for yeast oligosaccharyl transferase activity in vivo
    • Zufferey, R. et al. STT3, a highly conserved protein required for yeast oligosaccharyl transferase activity in vivo. EMBO J. 14, 4949-4960 (1995).
    • (1995) EMBO J , vol.14 , pp. 4949-4960
    • Zufferey, R.1
  • 13
    • 79959191882 scopus 로고    scopus 로고
    • X-ray structure of a bacterial oligosaccharyltransferase
    • Lizak, C., Gerber, S., Numao, S., Aebi, M., Locher, K. P. X-ray structure of a bacterial oligosaccharyltransferase. Nature 474, 350-355 (2011).
    • (2011) Nature , vol.474 , pp. 350-355
    • Lizak, C.1    Gerber, S.2    Numao, S.3    Aebi, M.4    Locher, K.P.5
  • 14
    • 84887060511 scopus 로고    scopus 로고
    • Crystal structures of an archaeal oligosaccharyltransferase provide insights into the catalytic cycle of N-linked protein glycosylation
    • Matsumoto, S. et al. Crystal structures of an archaeal oligosaccharyltransferase provide insights into the catalytic cycle of N-linked protein glycosylation. Proc. Natl. Acad. Sci. USA 110, 17868-17873 (2013).
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 17868-17873
    • Matsumoto, S.1
  • 15
    • 33646564396 scopus 로고    scopus 로고
    • Definition of the bacterial N-glycosylation site consensus sequence
    • Kowarik, M. et al. Definition of the bacterial N-glycosylation site consensus sequence. EMBO J. 25, 1957-1966 (2006).
    • (2006) EMBO J , vol.25 , pp. 1957-1966
    • Kowarik, M.1
  • 16
    • 84880799462 scopus 로고    scopus 로고
    • Inverse metabolic engineering to improve Escherichia coli as an N-glycosylation host
    • Pandhal, J. et al. Inverse metabolic engineering to improve Escherichia coli as an N-glycosylation host. Biotechnol. Bioeng. 110, 2482-2493 (2013).
    • (2013) Biotechnol. Bioeng. , vol.110 , pp. 2482-2493
    • Pandhal, J.1
  • 17
    • 84866514981 scopus 로고    scopus 로고
    • Structural insights from random mutagenesis of Campylobacter jejuni oligosaccharyltransferase PglB
    • Ihssen, J. et al. Structural insights from random mutagenesis of Campylobacter jejuni oligosaccharyltransferase PglB. BMC Biotechnol. 12, 67 (2012).
    • (2012) BMC Biotechnol , vol.12 , pp. 67
    • Ihssen, J.1
  • 18
    • 77957304985 scopus 로고    scopus 로고
    • A filamentous phage display system for N-linked glycoproteins
    • Çelik, E., Fisher, A. C., Guarino, C., Mansell, T. J., DeLisa, M. P. A filamentous phage display system for N-linked glycoproteins. Protein Sci. 19, 2006-2013 (2010).
    • (2010) Protein Sci , vol.19 , pp. 2006-2013
    • Çelik, E.1    Fisher, A.C.2    Guarino, C.3    Mansell, T.J.4    Delisa, M.P.5
  • 20
    • 84859813803 scopus 로고    scopus 로고
    • An engineered eukaryotic protein glycosylation pathway in Escherichia coli
    • Valderrama-Rincon, J. D. et al. An engineered eukaryotic protein glycosylation pathway in Escherichia coli. Nat. Chem. Biol. 8, 434-436 (2012).
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 434-436
    • Valderrama-Rincon, J.D.1
  • 21
    • 84871455762 scopus 로고    scopus 로고
    • Glycoengineering of host mimicking type-2 LacNAc polymers and Lewis X antigens on bacterial cell surfaces
    • Mally, M. et al. Glycoengineering of host mimicking type-2 LacNAc polymers and Lewis X antigens on bacterial cell surfaces. Mol. Microbiol. 87, 112-131 (2013).
    • (2013) Mol. Microbiol. , vol.87 , pp. 112-131
    • Mally, M.1
  • 22
    • 79551485538 scopus 로고    scopus 로고
    • Production of secretory and extracellular N-linked glycoproteins in Escherichia coli
    • Fisher, A. C. et al. Production of secretory and extracellular N-linked glycoproteins in Escherichia coli. Appl. Environ. Microbiol. 77, 871-881 (2011).
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 871-881
    • Fisher, A.C.1
  • 23
    • 0011928107 scopus 로고    scopus 로고
    • N-linked glycosylation in Campylobacter jejuni and its functional transfer into E coli
    • Wacker, M. et al. N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli. Science 298, 1790-1793 (2002).
    • (2002) Science , vol.298 , pp. 1790-1793
    • Wacker, M.1
  • 24
    • 30544435865 scopus 로고    scopus 로고
    • Extracellular accumulation of recombinant proteins fused to the carrier protein YebF in Escherichia coli
    • Zhang, G., Brokx, S., Weiner, J. H. Extracellular accumulation of recombinant proteins fused to the carrier protein YebF in Escherichia coli. Nat. Biotechnol. 24, 100-104 (2006).
    • (2006) Nat. Biotechnol. , vol.24 , pp. 100-104
    • Zhang, G.1    Brokx, S.2    Weiner, J.H.3
  • 25
    • 20044393802 scopus 로고    scopus 로고
    • Engineering N-linked protein glycosylation with diverse O antigen lipopolysaccharide structures in Escherichia coli
    • Feldman, M. F. et al. Engineering N-linked protein glycosylation with diverse O antigen lipopolysaccharide structures in Escherichia coli. Proc. Natl. Acad. Sci. USA 102, 3016-3021 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 3016-3021
    • Feldman, M.F.1
  • 26
    • 0036173114 scopus 로고    scopus 로고
    • Identification of N-acetylgalactosamine-containing glycoproteins PEB3 and CgpA in Campylobacter jejuni
    • Linton, D., Allan, E., Karlyshev, A. V., Cronshaw, A. D., Wren, B. W. Identification of N-acetylgalactosamine-containing glycoproteins PEB3 and CgpA in Campylobacter jejuni. Mol. Microbiol. 43, 497-508 (2002).
    • (2002) Mol. Microbiol. , vol.43 , pp. 497-508
    • Linton, D.1    Allan, E.2    Karlyshev, A.V.3    Cronshaw, A.D.4    Wren, B.W.5
  • 27
    • 33751215862 scopus 로고    scopus 로고
    • N-linked glycosylation of folded proteins by the bacterial oligosaccharyltransferase
    • Kowarik, M. et al. N-linked glycosylation of folded proteins by the bacterial oligosaccharyltransferase. Science 314, 1148-1150 (2006).
    • (2006) Science , vol.314 , pp. 1148-1150
    • Kowarik, M.1
  • 28
    • 0025367812 scopus 로고
    • Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: Implications for protein engineering
    • Gavel, Y., von Heijne, G. Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineering. Protein Eng. 3, 433-442 (1990).
    • (1990) Protein Eng , vol.3 , pp. 433-442
    • Gavel, Y.1    Von Heijne, G.2
  • 29
    • 79952000705 scopus 로고    scopus 로고
    • Relaxed acceptor site specificity of bacterial oligosaccharyltransferase in vivo
    • Schwarz, F. et al. Relaxed acceptor site specificity of bacterial oligosaccharyltransferase in vivo. Glycobiology 21, 45-54 (2011).
    • (2011) Glycobiology , vol.21 , pp. 45-54
    • Schwarz, F.1
  • 30
    • 79956083561 scopus 로고    scopus 로고
    • Desulfovibrio desulfuricans PglB homolog possesses oligosaccharyltransferase activity with relaxed glycan specificity and distinct protein acceptor sequence requirements
    • Ielmini, M. V., Feldman, M. F. Desulfovibrio desulfuricans PglB homolog possesses oligosaccharyltransferase activity with relaxed glycan specificity and distinct protein acceptor sequence requirements. Glycobiology 21, 734-742 (2011).
    • (2011) Glycobiology , vol.21 , pp. 734-742
    • Ielmini, M.V.1    Feldman, M.F.2
  • 31
    • 84875970481 scopus 로고    scopus 로고
    • Mechanism of bacterial oligosaccharyltransferase: In vitro quantification of sequon binding and catalysis
    • Gerber, S. et al. Mechanism of bacterial oligosaccharyltransferase: in vitro quantification of sequon binding and catalysis. J. Biol. Chem. 288, 8849-8861 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 8849-8861
    • Gerber, S.1
  • 32
    • 84896884825 scopus 로고    scopus 로고
    • Universal Genetic Assay for Engineering Extracellular Protein Expression
    • Haitjema, C. H. et al. Universal Genetic Assay for Engineering Extracellular Protein Expression. ACS Synth. Biol. 3, 74-82 (2013)
    • (2013) ACS Synth. Biol. , vol.3 , pp. 74-82
    • Haitjema, C.H.1
  • 33
    • 33746045692 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae-based molecular tool kit for manipulation of genes from gram-negative bacteria
    • Shanks, R. M., Caiazza, N. C., Hinsa, S. M., Toutain, C. M., O'Toole, G. A. Saccharomyces cerevisiae-based molecular tool kit for manipulation of genes from gram-negative bacteria. Appl. Environ. Microbiol. 72, 5027-5036 (2006).
    • (2006) Appl. Environ. Microbiol , vol.72 , pp. 5027-5036
    • Shanks, R.M.1    Caiazza, N.C.2    Hinsa, S.M.3    Toutain, C.M.4    O'Toole, G.A.5
  • 34
    • 0030861452 scopus 로고    scopus 로고
    • Independent and tight regulation of transcriptional units in Escherichia coli via the LacR/O, the TetR/O and AraC/I1-I2 regulatory elements
    • Lutz, R., Bujard, H. Independent and tight regulation of transcriptional units in Escherichia coli via the LacR/O, the TetR/O and AraC/I1-I2 regulatory elements. Nucleic Acids Res. 25, 1203-1210 (1997).
    • (1997) Nucleic Acids Res , vol.25 , pp. 1203-1210
    • Lutz, R.1    Bujard, H.2
  • 35
    • 84860872726 scopus 로고    scopus 로고
    • Comparative characterization of the glycosylation profiles of an influenza hemagglutinin produced in plant and insect hosts
    • Zhang, S. et al. Comparative characterization of the glycosylation profiles of an influenza hemagglutinin produced in plant and insect hosts. Proteomics 12, 1269-1288 (2012).
    • (2012) Proteomics , vol.12 , pp. 1269-1288
    • Zhang, S.1
  • 36
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • Arnold, K., Bordoli, L., Kopp, J., Schwede, T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22, 195-201 (2006).
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.