메뉴 건너뛰기




Volumn 79, Issue 1, 2011, Pages 96-101

Production and crystallization of processing α-glucosidase I: Pichia pastoris expression and a two-step purification toward structural determination

Author keywords

Alpha glucosidase; Carbohydrate synthesis; Glycoside hydrolase; N Glycosylation; Pichia pastoris; Protein crystallization; Protein expression and purification

Indexed keywords

ALPHA GLUCOSIDASE; GLUCOSIDASE I;

EID: 79960121620     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2011.05.015     Document Type: Article
Times cited : (8)

References (31)
  • 1
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • DOI 10.1146/annurev.biochem.73.011303.073752
    • A. Helenius, and M. Aebi Roles of N-linked glycans in the endoplasmic reticulum Annu. Rev. Biochem. 73 2004 1019 1049 (Pubitemid 39050393)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 2
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • DOI 10.1126/science.291.5512.2364
    • A. Helenius, and M. Aebi Intracellular functions of N-linked glycans Science 291 5512 2001 2364 2369 (Pubitemid 32231791)
    • (2001) Science , vol.291 , Issue.5512 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 3
    • 70249135667 scopus 로고    scopus 로고
    • Glycosylation diseases: Quo vadis?
    • H. Schachter, and H.H. Freeze Glycosylation diseases: Quo vadis? Biochim. Biophys. Acta 1792 9 2009 925 930
    • (2009) Biochim. Biophys. Acta , vol.1792 , Issue.9 , pp. 925-930
    • Schachter, H.1    Freeze, H.H.2
  • 4
    • 25844442417 scopus 로고    scopus 로고
    • Altered glycan structures: The molecular basis of congenital disorders of glycosylation
    • DOI 10.1016/j.sbi.2005.08.010, PII S0959440X05001582, Carbohydrates and Glycoconjugates/Biophysical Methods
    • H.H. Freeze, and M. Aebi Altered glycan structures: the molecular basis of congenital disorders of glycosylation Curr. Opin. Struct. Biol. 15 5 2005 490 498 (Pubitemid 41393479)
    • (2005) Current Opinion in Structural Biology , vol.15 , Issue.5 , pp. 490-498
    • Freeze, H.H.1    Aebi, M.2
  • 5
    • 70249147686 scopus 로고    scopus 로고
    • From glycosylation disorders back to glycosylation: What have we learned?
    • T. Hennet From glycosylation disorders back to glycosylation: what have we learned? Biochim. Biophys. Acta 1792 9 2009 921 924
    • (2009) Biochim. Biophys. Acta , vol.1792 , Issue.9 , pp. 921-924
    • Hennet, T.1
  • 8
    • 0032560488 scopus 로고    scopus 로고
    • α-Glucosidase inhibitors as potential broad based anti-viral agnets
    • DOI 10.1016/S0014-5793(98)00525-0, PII S0014579398005250
    • A. Mehta, N. Zitzmann, P.M. Rudd, T.M. Block, and R.A. Dwek Alpha-glucosidase inhibitors as potential broad based anti-viral agents FEBS Lett. 430 1-2 1998 17 22 (Pubitemid 28307024)
    • (1998) FEBS Letters , vol.430 , Issue.1-2 , pp. 17-22
    • Mehta, A.1    Zitzmann, N.2    Rudd, P.M.3    Block, T.M.4    Dwek, R.A.5
  • 9
    • 58549087715 scopus 로고    scopus 로고
    • Inhibition of cellular alpha-glucosidases results in increased presentation of hepatitis B virus glycoprotein-derived peptides by MHC class i
    • E. Simsek, G. Sinnathamby, T.M. Block, Y. Liu, and R. Philip Inhibition of cellular alpha-glucosidases results in increased presentation of hepatitis B virus glycoprotein-derived peptides by MHC class I Virology 384 1 2009 12 15
    • (2009) Virology , vol.384 , Issue.1 , pp. 12-15
    • Simsek, E.1    Sinnathamby, G.2    Block, T.M.3    Liu, Y.4    Philip, R.5
  • 11
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • B. Henrissat A classification of glycosyl hydrolases based on amino acid sequence similarities Biochem. J. 280 Pt 2 1991 309 316
    • (1991) Biochem. J. , vol.280 , Issue.PART 2 , pp. 309-316
    • Henrissat, B.1
  • 12
    • 46649103223 scopus 로고    scopus 로고
    • Structural insights into the substrate specificity and function of Escherichia coli K12 YgjK, a glucosidase belonging to the glycoside hydrolase family 63
    • Y. Kurakata, A. Uechi, H. Yoshida, S. Kamitori, and Y. Sakano Structural insights into the substrate specificity and function of Escherichia coli K12 YgjK, a glucosidase belonging to the glycoside hydrolase family 63 J. Mol. Biol. 381 1 2008 116 128
    • (2008) J. Mol. Biol. , vol.381 , Issue.1 , pp. 116-128
    • Kurakata, Y.1    Uechi, A.2    Yoshida, H.3    Kamitori, S.4    Sakano, Y.5
  • 13
    • 0030032122 scopus 로고    scopus 로고
    • CWH41 encodes a novel endoplasmic reticulum membrane N-glycoprotein involved in β1,6-glucan assembly
    • B. Jiang, J. Sheraton, A.F. Ram, G.J. Dijkgraaf, and F.M. Klis CWH41 encodes a novel endoplasmic reticulum membrane N-glycoprotein involved in beta 1, 6-glucan assembly J. Bacteriol. 178 4 1996 1162 1171 (Pubitemid 26048036)
    • (1996) Journal of Bacteriology , vol.178 , Issue.4 , pp. 1162-1171
    • Jiang, B.1    Sheraton, J.2    Ram, A.F.J.3    Dijkgraaf, G.J.P.4    Klis, F.M.5    Bussey, H.6
  • 14
    • 0001042135 scopus 로고
    • Purification and characterization of trimming glucosidase I from Saccharomyces cerevisiae
    • E. Bause, R. Erkens, J. Schweden, and L. Jaenicke Purification and characterization of trimming glucosidase I from Saccharomyces cerevisiae FEBS Lett. 206 2 1986 208
    • (1986) FEBS Lett. , vol.206 , Issue.2 , pp. 208
    • Bause, E.1    Erkens, R.2    Schweden, J.3    Jaenicke, L.4
  • 15
    • 0036259187 scopus 로고    scopus 로고
    • Overexpression, purification, and partial characterization of Saccharomyces cerevisiae processing alpha glucosidase I
    • R. Dhanawansa, A. Faridmoayer, G. van der Merwe, Y.X. Li, and C.H. Scaman Overexpression, purification, and partial characterization of Saccharomyces cerevisiae processing alpha glucosidase I Glycobiology 12 3 2002 229 234 (Pubitemid 34567869)
    • (2002) Glycobiology , vol.12 , Issue.3 , pp. 229-234
    • Dhanawansa, R.1    Faridmoayer, A.2    Van Der Merwe, G.3    Li, Y.X.4    Scaman, C.H.5
  • 18
    • 0032903636 scopus 로고    scopus 로고
    • Processing glycosidases of Saccharomyces cerevisiae
    • DOI 10.1016/S0304-4165(98)00129-9, PII S0304416598001299
    • A. Herscovics Processing glycosidases of Saccharomyces cerevisiae Biochim. Biophys. Acta 1426 2 1999 275 285 (Pubitemid 29027944)
    • (1999) Biochimica et Biophysica Acta - General Subjects , vol.1426 , Issue.2 , pp. 275-285
    • Herscovics, A.1
  • 19
    • 0345832413 scopus 로고    scopus 로고
    • An improved purification procedure for soluble processing α-glucosidase I from Saccharomyces cerevisiae overexpressing CWH41
    • DOI 10.1016/j.pep.2003.09.013
    • A. Faridmoayer, and C.H. Scaman An improved purification procedure for soluble processing alpha-glucosidase I from Saccharomyces cerevisiae overexpressing CWH41 Protein Expr. Purif. 33 1 2004 11 18 (Pubitemid 38078067)
    • (2004) Protein Expression and Purification , vol.33 , Issue.1 , pp. 11-18
    • Faridmoayer, A.1    Scaman, C.H.2
  • 20
    • 28444473450 scopus 로고    scopus 로고
    • Binding residues and catalytic domain of soluble Saccharomyces cerevisiae processing alpha-glucosidase I
    • DOI 10.1093/glycob/cwj009
    • A. Faridmoayer, and C.H. Scaman Binding residues and catalytic domain of soluble Saccharomyces cerevisiae processing alpha-glucosidase I Glycobiology 15 12 2005 1341 1348 (Pubitemid 41724338)
    • (2005) Glycobiology , vol.15 , Issue.12 , pp. 1341-1348
    • Faridmoayer, A.1    Scaman, C.H.2
  • 21
    • 34848890673 scopus 로고    scopus 로고
    • Truncations and functional carboxylic acid residues of yeast processing α-glucosidase I
    • DOI 10.1007/s10719-007-9035-2
    • A. Faridmoayer, and C.H. Scaman Truncations and functional carboxylic acid residues of yeast processing alpha-glucosidase I Glycoconj. J. 24 8 2007 429 437 (Pubitemid 47512575)
    • (2007) Glycoconjugate Journal , vol.24 , Issue.8 , pp. 429-437
    • Faridmoayer, A.1    Scaman, C.H.2
  • 22
    • 14744285206 scopus 로고    scopus 로고
    • Expression of heterologous proteins in Pichia pastoris: A useful experimental tool in protein engineenring and production
    • DOI 10.1002/jmr.687
    • R. Daly, and M.T. Hearn Expression of heterologous proteins in Pichia pastoris: a useful experimental tool in protein engineering and production J. Mol. Recognit. 18 2 2005 119 138 (Pubitemid 40328574)
    • (2005) Journal of Molecular Recognition , vol.18 , Issue.2 , pp. 119-138
    • Daly, R.1    Hearn, M.T.W.2
  • 24
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 26
    • 33646920982 scopus 로고    scopus 로고
    • 3Man N-glycan tetrasaccharide by iterative allyl IAD
    • DOI 10.1016/j.carres.2006.02.022, PII S0008621506000838
    • 3Man N-glycan tetrasaccharide by iterative allyl IAD Carbohydr. Res. 341 10 2006 1609 1618 (Pubitemid 43795416)
    • (2006) Carbohydrate Research , vol.341 , Issue.10 , pp. 1609-1618
    • Attolino, E.1    Cumpstey, I.2    Fairbanks, A.J.3
  • 27
    • 33847801270 scopus 로고
    • Halide ion catalyzed glycosylation reactions syntheses of alpha-linked disaccharides
    • R.U. Lemieux, K.B. Hendriks, and R.V. Stick Halide ion catalyzed glycosylation reactions syntheses of alpha-linked disaccharides J. Am. Chem. Soc. 97 14 1975 4056 4062
    • (1975) J. Am. Chem. Soc. , vol.97 , Issue.14 , pp. 4056-4062
    • Lemieux, R.U.1    Hendriks, K.B.2    Stick, R.V.3
  • 29
    • 0000557576 scopus 로고    scopus 로고
    • 1-antitrypsin in Saccharomyces cerevisiae and methylotrophic yeasts
    • DOI 10.1002/(SICI)1097-0061(19980315)14:4<371::AID-YEA231>3.0.CO;2- 1
    • H.A. Kang, J.H. Sohn, E.S. Choi, B.H. Chung, M.H. Yu, and S.K. Rhee Glycosylation of human alpha 1-antitrypsin in Saccharomyces cerevisiae and methylotrophic yeasts Yeast 14 4 1998 371 381 (Pubitemid 28138987)
    • (1998) Yeast , vol.14 , Issue.4 , pp. 371-381
    • Kang, H.A.1    Sohn, J.-H.2    Choi, E.-S.3    Chung, B.H.4    Yu, M.-H.5    Rhee, S.-K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.