메뉴 건너뛰기




Volumn 89, Issue 2, 2013, Pages 241-250

Optimized protocol for expression and purification of membrane-bound PglB, a bacterial oligosaccharyl transferase

Author keywords

Asparagine linked glycosylation; Membrane protein; Oligosaccharyl transferase; PglB; Purification protocol; Recombinant expression

Indexed keywords

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

EID: 84876976018     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2013.04.001     Document Type: Article
Times cited : (13)

References (44)
  • 1
    • 33845275819 scopus 로고    scopus 로고
    • Estimation of membrane proteins in the human proteome
    • M. Ahram, Z.I. Litou, R. Fang, and G. Al-Tawallbeh Estimation of membrane proteins in the human proteome In Silico Biol. 6 2006 379 386
    • (2006) Silico Biol. , vol.6 , pp. 379-386
    • Ahram, M.1    Litou, Z.I.2    Fang, R.3    Al-Tawallbeh, G.4
  • 5
    • 54449087770 scopus 로고    scopus 로고
    • Directed evolution of a G protein-coupled receptor for expression, stability, and binding selectivity
    • C.A. Sarkar, I. Dodevski, M. Kenig, S. Dudli, and A. Mohr Directed evolution of a G protein-coupled receptor for expression, stability, and binding selectivity Proc. Natl. Acad. Sci. USA 105 2008 14808 14813
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 14808-14813
    • Sarkar, C.A.1    Dodevski, I.2    Kenig, M.3    Dudli, S.4    Mohr, A.5
  • 6
    • 77953448152 scopus 로고    scopus 로고
    • Role of N-linked glycosylation in biosynthesis, trafficking, and function of the human glucagon-like peptide 1 receptor
    • Q. Chen, L.J. Miller, and M. Dong Role of N-linked glycosylation in biosynthesis, trafficking, and function of the human glucagon-like peptide 1 receptor Am. J. Physiol. Endocrinol. Metab. 299 2010 E62 E68
    • (2010) Am. J. Physiol. Endocrinol. Metab. , vol.299
    • Chen, Q.1    Miller, L.J.2    Dong, M.3
  • 7
    • 84861100864 scopus 로고    scopus 로고
    • Serious medical complications in children with cancer and fever in chemotherapy-induced neutropenia: Results of the prospective multicenter SPOG 2003 FN study
    • F. Luthi, K. Leibundgut, F.K. Niggli, D. Nadal, and C. Aebi Serious medical complications in children with cancer and fever in chemotherapy-induced neutropenia: results of the prospective multicenter SPOG 2003 FN study Pediatr. Blood Cancer 59 2012 90 95
    • (2012) Pediatr. Blood Cancer , vol.59 , pp. 90-95
    • Luthi, F.1    Leibundgut, K.2    Niggli, F.K.3    Nadal, D.4    Aebi, C.5
  • 8
    • 77954957121 scopus 로고    scopus 로고
    • N-linked glycosylation selectively regulates autonomous precursor BCR function
    • R. Ubelhart, M.P. Bach, C. Eschbach, T. Wossning, and M. Reth N-linked glycosylation selectively regulates autonomous precursor BCR function Nat. Immunol. 11 2010 759 765
    • (2010) Nat. Immunol. , vol.11 , pp. 759-765
    • Ubelhart, R.1    Bach, M.P.2    Eschbach, C.3    Wossning, T.4    Reth, M.5
  • 9
    • 79952410920 scopus 로고    scopus 로고
    • N-linked glycosylation facilitates sialic acid-independent attachment and entry of influenza A viruses into cells expressing DC-SIGN or L-SIGN
    • S.L. Londrigan, S.G. Turville, M.D. Tate, Y.M. Deng, and A.G. Brooks N-linked glycosylation facilitates sialic acid-independent attachment and entry of influenza A viruses into cells expressing DC-SIGN or L-SIGN J. Virol. 85 2011 2990 3000
    • (2011) J. Virol. , vol.85 , pp. 2990-3000
    • Londrigan, S.L.1    Turville, S.G.2    Tate, M.D.3    Deng, Y.M.4    Brooks, A.G.5
  • 10
    • 64549099901 scopus 로고    scopus 로고
    • N-linked glycosylation is an important parameter for optimal selection of cell lines producing biopharmaceutical human IgG
    • P.H. van Berkel, J. Gerritsen, G. Perdok, J. Valbjorn, and T. Vink N-linked glycosylation is an important parameter for optimal selection of cell lines producing biopharmaceutical human IgG Biotechnol. Prog. 25 2009 244 251
    • (2009) Biotechnol. Prog. , vol.25 , pp. 244-251
    • Van Berkel, P.H.1    Gerritsen, J.2    Perdok, G.3    Valbjorn, J.4    Vink, T.5
  • 11
    • 84868586999 scopus 로고    scopus 로고
    • Bacterial inactivation by a singlet oxygen bubbler: Identifying factors controlling the toxicity of (1) O2 bubbles
    • D. Bartusik, D. Aebisher, A.M. Lyons, and A. Greer Bacterial inactivation by a singlet oxygen bubbler: identifying factors controlling the toxicity of (1) O2 bubbles Environ. Sci. Technol. 46 2012 12098 12104
    • (2012) Environ. Sci. Technol. , vol.46 , pp. 12098-12104
    • Bartusik, D.1    Aebisher, D.2    Lyons, A.M.3    Greer, A.4
  • 13
    • 79952783025 scopus 로고    scopus 로고
    • N-Linked glycosylation of antibody fragments in Escherichia coli
    • C. Lizak, Y.Y. Fan, T.C. Weber, and M. Aebi N-Linked glycosylation of antibody fragments in Escherichia coli Bioconjug. Chem. 22 2011 488 496
    • (2011) Bioconjug. Chem. , vol.22 , pp. 488-496
    • Lizak, C.1    Fan, Y.Y.2    Weber, T.C.3    Aebi, M.4
  • 14
    • 84866154869 scopus 로고    scopus 로고
    • N-linked glycosylation of GP5 of porcine reproductive and respiratory syndrome virus is critically important for virus replication in vivo
    • Z. Wei, T. Lin, L. Sun, Y. Li, and X. Wang N-linked glycosylation of GP5 of porcine reproductive and respiratory syndrome virus is critically important for virus replication in vivo J. Virol. 86 2012 9941 9951
    • (2012) J. Virol. , vol.86 , pp. 9941-9951
    • Wei, Z.1    Lin, T.2    Sun, L.3    Li, Y.4    Wang, X.5
  • 15
    • 84857621778 scopus 로고    scopus 로고
    • Secretion and N-linked glycosylation are required for prostatic acid phosphatase catalytic and antinociceptive activity
    • J.K. Hurt, B.J. Fitzpatrick, J. Norris-Drouin, and M.J. Zylka Secretion and N-linked glycosylation are required for prostatic acid phosphatase catalytic and antinociceptive activity PLoS ONE 7 2012 e32741
    • (2012) PLoS ONE , vol.7 , pp. 32741
    • Hurt, J.K.1    Fitzpatrick, B.J.2    Norris-Drouin, J.3    Zylka, M.J.4
  • 16
    • 84867216481 scopus 로고    scopus 로고
    • The number and position of N-linked glycosylation sites in the hemagglutinin determine differential recognition of seasonal and 2009 pandemic H1N1 influenza virus by porcine surfactant protein D
    • M.L. Hillaire, M. van Eijk, N.J. Nieuwkoop, S.E. Vogelzang-van Trierum, and R.A. Fouchier The number and position of N-linked glycosylation sites in the hemagglutinin determine differential recognition of seasonal and 2009 pandemic H1N1 influenza virus by porcine surfactant protein D Virus Res. 169 2012 301 305
    • (2012) Virus Res. , vol.169 , pp. 301-305
    • Hillaire, M.L.1    Van Eijk, M.2    Nieuwkoop, N.J.3    Vogelzang-Van Trierum, S.E.4    Fouchier, R.A.5
  • 17
    • 79954633991 scopus 로고    scopus 로고
    • N-linked glycosylation of dengue virus NS1 protein modulates secretion, cell-surface expression, hexamer stability, and interactions with human complement
    • P. Somnuke, R.E. Hauhart, J.P. Atkinson, M.S. Diamond, and P. Avirutnan N-linked glycosylation of dengue virus NS1 protein modulates secretion, cell-surface expression, hexamer stability, and interactions with human complement Virology 413 2011 253 264
    • (2011) Virology , vol.413 , pp. 253-264
    • Somnuke, P.1    Hauhart, R.E.2    Atkinson, J.P.3    Diamond, M.S.4    Avirutnan, P.5
  • 18
    • 80053469048 scopus 로고    scopus 로고
    • Mechanisms and principles of N-linked protein glycosylation
    • F. Schwarz, and M. Aebi Mechanisms and principles of N-linked protein glycosylation Curr. Opin. Struct. Biol. 21 2011 576 582
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 576-582
    • Schwarz, F.1    Aebi, M.2
  • 19
    • 79959191882 scopus 로고    scopus 로고
    • X-ray structure of a bacterial oligosaccharyltransferase
    • C. Lizak, S. Gerber, S. Numao, M. Aebi, and K.P. Locher X-ray structure of a bacterial oligosaccharyltransferase Nature 474 2011 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
  • 20
    • 80052254267 scopus 로고    scopus 로고
    • Exploiting topological constraints to reveal buried sequence motifs in the membrane-bound N-linked oligosaccharyl transferases
    • M.B. Jaffee, and B. Imperiali Exploiting topological constraints to reveal buried sequence motifs in the membrane-bound N-linked oligosaccharyl transferases Biochemistry 50 2011 7557 7567
    • (2011) Biochemistry , vol.50 , pp. 7557-7567
    • Jaffee, M.B.1    Imperiali, B.2
  • 21
    • 84859062000 scopus 로고    scopus 로고
    • A prokaryote-based cell-free translation system that efficiently synthesizes glycoproteins
    • C. Guarino, and M.P. DeLisa A prokaryote-based cell-free translation system that efficiently synthesizes glycoproteins Glycobiology 22 2012 596 601
    • (2012) Glycobiology , vol.22 , pp. 596-601
    • Guarino, C.1    Delisa, M.P.2
  • 22
    • 78651099872 scopus 로고    scopus 로고
    • Perturbing the folding energy landscape of the bacterial immunity protein Im7 by site-specific N-linked glycosylation
    • M.M. Chen, A.I. Bartlett, P.S. Nerenberg, C.T. Friel, and C.P. Hackenberger Perturbing the folding energy landscape of the bacterial immunity protein Im7 by site-specific N-linked glycosylation Proc. Natl. Acad. Sci. USA 107 2010 22528 22533
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 22528-22533
    • Chen, M.M.1    Bartlett, A.I.2    Nerenberg, P.S.3    Friel, C.T.4    Hackenberger, C.P.5
  • 23
    • 0026594004 scopus 로고
    • Genome maps of Campylobacter jejuni and Campylobacter coli
    • D.E. Taylor, M. Eaton, W. Yan, and N. Chang Genome maps of Campylobacter jejuni and Campylobacter coli J. Bacteriol. 174 1992 2332 2337
    • (1992) J. Bacteriol. , vol.174 , pp. 2332-2337
    • Taylor, D.E.1    Eaton, M.2    Yan, W.3    Chang, N.4
  • 24
    • 0031888389 scopus 로고    scopus 로고
    • An improved physical and genetic map of Campylobacter jejuni NCTC 11168 (UA580)
    • A.V. Karlyshev, J. Henderson, J.M. Ketley, and B.W. Wren An improved physical and genetic map of Campylobacter jejuni NCTC 11168 (UA580) Microbiology 144 Pt 2 1998 503 508
    • (1998) Microbiology , vol.144 , Issue.PART 2 , pp. 503-508
    • Karlyshev, A.V.1    Henderson, J.2    Ketley, J.M.3    Wren, B.W.4
  • 25
    • 33646596978 scopus 로고    scopus 로고
    • Highly efficient expression and purification system of small-size protein domains in Escherichia coli for biochemical characterization
    • W.J. Bao, Y.G. Gao, Y.G. Chang, T.Y. Zhang, and X.J. Lin Highly efficient expression and purification system of small-size protein domains in Escherichia coli for biochemical characterization Protein Expr. Purif. 47 2006 599 606
    • (2006) Protein Expr. Purif. , vol.47 , pp. 599-606
    • Bao, W.J.1    Gao, Y.G.2    Chang, Y.G.3    Zhang, T.Y.4    Lin, X.J.5
  • 26
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high-density shaking cultures
    • F.W. Studier Protein production by auto-induction in high-density shaking cultures Protein Expr. Purif. 41 2005 207 234
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 27
    • 28844508716 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of glycopeptides with PglB, a bacterial oligosaccharyl transferase from Campylobacter jejuni
    • K.J. Glover, E. Weerapana, S. Numao, and B. Imperiali Chemoenzymatic synthesis of glycopeptides with PglB, a bacterial oligosaccharyl transferase from Campylobacter jejuni Chem. Biol. 12 2005 1311 1315
    • (2005) Chem. Biol. , vol.12 , pp. 1311-1315
    • Glover, K.J.1    Weerapana, E.2    Numao, S.3    Imperiali, B.4
  • 28
    • 34248232580 scopus 로고    scopus 로고
    • From peptide to protein: Comparative analysis of the substrate specificity of N-linked glycosylation in C. jejuni
    • M.M. Chen, K.J. Glover, and B. Imperiali From peptide to protein: comparative analysis of the substrate specificity of N-linked glycosylation in C. jejuni Biochemistry 46 2007 5579 5585
    • (2007) Biochemistry , vol.46 , pp. 5579-5585
    • Chen, M.M.1    Glover, K.J.2    Imperiali, B.3
  • 29
    • 0019570379 scopus 로고
    • N-Glycosylation of yeast proteins. Characterization of the solubilized oligosaccharyl transferase
    • C.B. Sharma, L. Lehle, and W. Tanner N-Glycosylation of yeast proteins. Characterization of the solubilized oligosaccharyl transferase Eur. J. Biochem. 116 1981 101 108
    • (1981) Eur. J. Biochem. , vol.116 , pp. 101-108
    • Sharma, C.B.1    Lehle, L.2    Tanner, W.3
  • 31
    • 39549090406 scopus 로고    scopus 로고
    • The use of systematic N- and C-terminal deletions to promote production and structural studies of recombinant proteins
    • S. Graslund, J. Sagemark, H. Berglund, L.G. Dahlgren, and A. Flores The use of systematic N- and C-terminal deletions to promote production and structural studies of recombinant proteins Protein Expr. Purif. 58 2008 210 221
    • (2008) Protein Expr. Purif. , vol.58 , pp. 210-221
    • Graslund, S.1    Sagemark, J.2    Berglund, H.3    Dahlgren, L.G.4    Flores, A.5
  • 32
    • 77950861521 scopus 로고    scopus 로고
    • Comparative structural biology of eubacterial and archaeal oligosaccharyltransferases
    • N. Maita, J. Nyirenda, M. Igura, J. Kamishikiryo, and D. Kohda Comparative structural biology of eubacterial and archaeal oligosaccharyltransferases J. Biol. Chem. 285 2010 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
  • 33
    • 69249215474 scopus 로고    scopus 로고
    • Making the most of fusion tags technology in structural characterization of membrane proteins
    • H. Xie, X.M. Guo, and H. Chen Making the most of fusion tags technology in structural characterization of membrane proteins Mol. Biotechnol. 42 2009 135 145
    • (2009) Mol. Biotechnol. , vol.42 , pp. 135-145
    • Xie, H.1    Guo, X.M.2    Chen, H.3
  • 34
    • 0027203472 scopus 로고
    • Recombinant baculovirus vectors expressing glutathione-S-transferase fusion proteins
    • A.H. Davies, J.B. Jowett, and I.M. Jones Recombinant baculovirus vectors expressing glutathione-S-transferase fusion proteins Biotechnology (NY) 11 1993 933 936
    • (1993) Biotechnology (NY) , vol.11 , pp. 933-936
    • Davies, A.H.1    Jowett, J.B.2    Jones, I.M.3
  • 35
    • 0031214792 scopus 로고    scopus 로고
    • High-level expression of soluble protein in Escherichia coli using a His6-tag and maltose-binding-protein double-affinity fusion system
    • K.D. Pryor, and B. Leiting High-level expression of soluble protein in Escherichia coli using a His6-tag and maltose-binding-protein double-affinity fusion system Protein Expr. Purif. 10 1997 309 319
    • (1997) Protein Expr. Purif. , vol.10 , pp. 309-319
    • Pryor, K.D.1    Leiting, B.2
  • 36
    • 0032006484 scopus 로고    scopus 로고
    • Solubility of proteins isolated from inclusion bodies is enhanced by fusion to maltose-binding protein or thioredoxin
    • D. Sachdev, and J.M. Chirgwin Solubility of proteins isolated from inclusion bodies is enhanced by fusion to maltose-binding protein or thioredoxin Protein Expr. Purif. 12 1998 122 132
    • (1998) Protein Expr. Purif. , vol.12 , pp. 122-132
    • Sachdev, D.1    Chirgwin, J.M.2
  • 37
    • 59249094982 scopus 로고    scopus 로고
    • SUMO fusion technology for enhanced protein production in prokaryotic and eukaryotic expression systems
    • T. Panavas, C. Sanders, and T.R. Butt SUMO fusion technology for enhanced protein production in prokaryotic and eukaryotic expression systems Methods Mol. Biol. 497 2009 303 317
    • (2009) Methods Mol. Biol. , vol.497 , pp. 303-317
    • Panavas, T.1    Sanders, C.2    Butt, T.R.3
  • 38
    • 83755163795 scopus 로고    scopus 로고
    • Heterologous expression of membrane proteins: Choosing the appropriate host
    • F. Bernaudat, A. Frelet-Barrand, N. Pochon, S. Dementin, and P. Hivin Heterologous expression of membrane proteins: choosing the appropriate host PLoS ONE 6 2011 e29191
    • (2011) PLoS ONE , vol.6 , pp. 29191
    • Bernaudat, F.1    Frelet-Barrand, A.2    Pochon, N.3    Dementin, S.4    Hivin, P.5
  • 39
    • 0022595736 scopus 로고
    • Alkyl glycoside detergents: Synthesis and applications to the study of membrane proteins
    • T. VanAken, S. Foxall-VanAken, S. Castleman, and S. Ferguson-Miller Alkyl glycoside detergents: synthesis and applications to the study of membrane proteins Methods Enzymol. 125 1986 27 35
    • (1986) Methods Enzymol. , vol.125 , pp. 27-35
    • Vanaken, T.1    Foxall-Vanaken, S.2    Castleman, S.3    Ferguson-Miller, S.4
  • 40
    • 0019328971 scopus 로고
    • Alkyl glycoside detergents: A simpler synthesis and their effects on kinetic and physical properties of cytochrome c oxidase
    • P. Rosevear, T. VanAken, J. Baxter, and S. Ferguson-Miller Alkyl glycoside detergents: a simpler synthesis and their effects on kinetic and physical properties of cytochrome c oxidase Biochemistry 19 1980 4108 4115
    • (1980) Biochemistry , vol.19 , pp. 4108-4115
    • Rosevear, P.1    Vanaken, T.2    Baxter, J.3    Ferguson-Miller, S.4
  • 42
    • 0035783023 scopus 로고    scopus 로고
    • Stability of membrane proteins: Relevance for the selection of appropriate methods for high-resolution structure determinations
    • J.P. Rosenbusch Stability of membrane proteins: relevance for the selection of appropriate methods for high-resolution structure determinations J. Struct. Biol. 136 2001 144 157
    • (2001) J. Struct. Biol. , vol.136 , pp. 144-157
    • Rosenbusch, J.P.1
  • 43
    • 33746813576 scopus 로고    scopus 로고
    • Understanding recombinant expression of membrane proteins
    • R. Grisshammer Understanding recombinant expression of membrane proteins Curr. Opin. Biotechnol. 17 2006 337 340
    • (2006) Curr. Opin. Biotechnol. , vol.17 , pp. 337-340
    • Grisshammer, R.1
  • 44
    • 84872356936 scopus 로고    scopus 로고
    • Protein engineering methods applied to membrane protein targets
    • M.W. Lluis, J.I. Godfroy, and H. Yin Protein engineering methods applied to membrane protein targets Protein Eng. Des. Sel. 126 2012 91 100
    • (2012) Protein Eng. Des. Sel. , vol.126 , pp. 91-100
    • Lluis, M.W.1    Godfroy, J.I.2    Yin, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.