메뉴 건너뛰기




Volumn 71, Issue 2, 2010, Pages 207-223

Purification of transmembrane proteins from Saccharomyces cerevisiae for X-ray crystallography

Author keywords

Crystallography; Detergents; Membrane proteins; Protein expression; Structural genomics; Yeast

Indexed keywords

MEMBRANE PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 77949488801     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2009.12.012     Document Type: Article
Times cited : (31)

References (67)
  • 2
    • 33746217557 scopus 로고    scopus 로고
    • Solution NMR of membrane proteins: practice and challenges
    • Sanders C.R., and Sonnichsen F. Solution NMR of membrane proteins: practice and challenges. Magn. Reson. Chem. 44 (2006) S24-40
    • (2006) Magn. Reson. Chem. , vol.44
    • Sanders, C.R.1    Sonnichsen, F.2
  • 3
    • 69249155615 scopus 로고    scopus 로고
    • The role of solution NMR in the structure determinations of VDAC-1 and other membrane proteins
    • Hiller S., and Wagner G. The role of solution NMR in the structure determinations of VDAC-1 and other membrane proteins. Curr. Opin. Struct. Biol. 19 (2009) 396-401
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 396-401
    • Hiller, S.1    Wagner, G.2
  • 4
    • 36148942092 scopus 로고    scopus 로고
    • Breaking the bottleneck: eukaryotic membrane protein expression for high-resolution structural studies
    • Midgett C.R., and Madden D.R. Breaking the bottleneck: eukaryotic membrane protein expression for high-resolution structural studies. J. Struct. Biol. 160 (2007) 265-274
    • (2007) J. Struct. Biol. , vol.160 , pp. 265-274
    • Midgett, C.R.1    Madden, D.R.2
  • 7
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 a resolution
    • Toyoshima C., Nakasako M., Nomura H., and Ogawa H. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 a resolution. Nature 405 (2000) 647-655
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 13
    • 33845629883 scopus 로고    scopus 로고
    • Characteristics affecting expression and solubilization of yeast membrane proteins
    • White M.A., Clark K.M., Grayhack E.J., and Dumont M.E. Characteristics affecting expression and solubilization of yeast membrane proteins. J. Mol. Biol. 365 (2007) 621-636
    • (2007) J. Mol. Biol. , vol.365 , pp. 621-636
    • White, M.A.1    Clark, K.M.2    Grayhack, E.J.3    Dumont, M.E.4
  • 14
    • 0036795285 scopus 로고    scopus 로고
    • Two proteins that form a complex is required for 7-methylguanosine modification of yeast tRNA
    • Alexandrov A., Martzen M.R., and Phizicky E.M. Two proteins that form a complex is required for 7-methylguanosine modification of yeast tRNA. RNA 8 (2002) 1253-1266
    • (2002) RNA , vol.8 , pp. 1253-1266
    • Alexandrov, A.1    Martzen, M.R.2    Phizicky, E.M.3
  • 16
    • 0036275447 scopus 로고    scopus 로고
    • Getting started with yeast
    • Sherman F. Getting started with yeast. Meth. Enzymol. 350 (2002) 3-41
    • (2002) Meth. Enzymol. , vol.350 , pp. 3-41
    • Sherman, F.1
  • 17
    • 0842288662 scopus 로고    scopus 로고
    • Membrane protein expression and production: effects of polyhistidine tag length and position
    • Mohanty A.K., and Wiener M.C. Membrane protein expression and production: effects of polyhistidine tag length and position. Protein Expr. Purif. 33 (2004) 311-325
    • (2004) Protein Expr. Purif. , vol.33 , pp. 311-325
    • Mohanty, A.K.1    Wiener, M.C.2
  • 18
    • 0034996241 scopus 로고    scopus 로고
    • MBP fusion protein with a viral protease cleavage site: one-step cleavage/purification of insoluble proteins
    • Alexandrov A., Dutta K., and Pascal S.M. MBP fusion protein with a viral protease cleavage site: one-step cleavage/purification of insoluble proteins. Biotechniques 30 (2001) 1194-1198
    • (2001) Biotechniques , vol.30 , pp. 1194-1198
    • Alexandrov, A.1    Dutta, K.2    Pascal, S.M.3
  • 19
    • 0000750473 scopus 로고
    • Metal-binding properties of human erythrocyte carbonic anhydrases
    • Lindskog S., and Nyman P.O. Metal-binding properties of human erythrocyte carbonic anhydrases. Biochim. Biophys. Acta 85 (1964) 462-474
    • (1964) Biochim. Biophys. Acta , vol.85 , pp. 462-474
    • Lindskog, S.1    Nyman, P.O.2
  • 20
    • 0008211326 scopus 로고
    • The spectrophotometric titration of the sulfhydryl and phenolic groups of aldolase
    • Donovan J.W. The spectrophotometric titration of the sulfhydryl and phenolic groups of aldolase. Biochemistry 3 (1964) 67-74
    • (1964) Biochemistry , vol.3 , pp. 67-74
    • Donovan, J.W.1
  • 21
    • 0014603264 scopus 로고
    • Yeast alcohol dehydrogenase: SH groups disulfide groups, quaternary structure, and reactivation by reductive cleavage of disulfide groups.
    • Buhner M., and Sund H. Yeast alcohol dehydrogenase: SH groups disulfide groups, quaternary structure, and reactivation by reductive cleavage of disulfide groups. Eur. J. Biochem. 11 (1969) 73-79
    • (1969) Eur. J. Biochem. , vol.11 , pp. 73-79
    • Buhner, M.1    Sund, H.2
  • 22
    • 33947454072 scopus 로고
    • On the mode of interaction of surface active cations with ovalbumin and bovine serum albumin
    • Foster J.F., and Yang J.T. On the mode of interaction of surface active cations with ovalbumin and bovine serum albumin. J. Am. Chem. Soc. 76 (1954) 1015-1019
    • (1954) J. Am. Chem. Soc. , vol.76 , pp. 1015-1019
    • Foster, J.F.1    Yang, J.T.2
  • 23
    • 33947438832 scopus 로고
    • Preparation and properties of serum and plasma proteins XIII. Crystallization of serum albumins from ethanol-water mixtures.
    • Cohn E.J., Hughes W.L., and Weare J.H. Preparation and properties of serum and plasma proteins XIII. Crystallization of serum albumins from ethanol-water mixtures. J. Am. Chem. Soc. 69 (1947) 1753-1761
    • (1947) J. Am. Chem. Soc. , vol.69 , pp. 1753-1761
    • Cohn, E.J.1    Hughes, W.L.2    Weare, J.H.3
  • 24
    • 0012794340 scopus 로고
    • Preparation and properties of serum and plasma proteins. XXVIII. The β1-metal-combining protein of human plasma
    • Koechlin B.A. Preparation and properties of serum and plasma proteins. XXVIII. The β1-metal-combining protein of human plasma. J. Am. Chem. Soc. 74 (1952) 2649-2653
    • (1952) J. Am. Chem. Soc. , vol.74 , pp. 2649-2653
    • Koechlin, B.A.1
  • 25
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill S.C., and von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182 (1989) 319-326
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    von Hippel, P.H.2
  • 27
    • 9944262886 scopus 로고    scopus 로고
    • A colorimetric determination for glycosidic and bile salt-based detergents: applications in membrane protein research
    • Urbani A., and Warne T. A colorimetric determination for glycosidic and bile salt-based detergents: applications in membrane protein research. Anal. Biochem. 336 (2005) 117-124
    • (2005) Anal. Biochem. , vol.336 , pp. 117-124
    • Urbani, A.1    Warne, T.2
  • 28
    • 0034814948 scopus 로고    scopus 로고
    • Expression and characterization of the anion transporter homologue YNL275w in Saccharomyces cerevisiae
    • Zhao R., and Reithmeier R.A. Expression and characterization of the anion transporter homologue YNL275w in Saccharomyces cerevisiae. Am. J. Physiol. Cell Physiol. 281 (2001) C33-45
    • (2001) Am. J. Physiol. Cell Physiol. , vol.281
    • Zhao, R.1    Reithmeier, R.A.2
  • 29
    • 0035859796 scopus 로고    scopus 로고
    • Mutational analysis of the role of N-glycosylation in alpha-factor receptor function
    • Mentesana P.E., and Konopka J.B. Mutational analysis of the role of N-glycosylation in alpha-factor receptor function. Biochemistry 40 (2001) 9685-9694
    • (2001) Biochemistry , vol.40 , pp. 9685-9694
    • Mentesana, P.E.1    Konopka, J.B.2
  • 32
    • 0034786532 scopus 로고    scopus 로고
    • The HMMTOP transmembrane topology prediction server
    • Tusnady G.E., and Simon I. The HMMTOP transmembrane topology prediction server. Bioinformatics 17 (2001) 849-850
    • (2001) Bioinformatics , vol.17 , pp. 849-850
    • Tusnady, G.E.1    Simon, I.2
  • 35
    • 0025085655 scopus 로고
    • Ligation-independent cloning of PCR products (LIC-PCR)
    • Aslanidis C., and de Jong P.J. Ligation-independent cloning of PCR products (LIC-PCR). Nucl. Acids Res. 18 (1990) 6069-6074
    • (1990) Nucl. Acids Res. , vol.18 , pp. 6069-6074
    • Aslanidis, C.1    de Jong, P.J.2
  • 37
    • 18944370824 scopus 로고    scopus 로고
    • Evaluation of the Saccharomyces cerevisiae ADH2 promoter for protein synthesis
    • Lee K.M., and DaSilva N.A. Evaluation of the Saccharomyces cerevisiae ADH2 promoter for protein synthesis. Yeast 22 (2005) 431-440
    • (2005) Yeast , vol.22 , pp. 431-440
    • Lee, K.M.1    DaSilva, N.A.2
  • 38
    • 0025291368 scopus 로고
    • Expression of heterologous proteins in Saccharomyces cerevisiae using the ADH2 promoter
    • Price V.L., Taylor W.E., Clevenger W., Worthington M., and Young E.T. Expression of heterologous proteins in Saccharomyces cerevisiae using the ADH2 promoter. Meth. Enzymol. 185 (1990) 308-318
    • (1990) Meth. Enzymol. , vol.185 , pp. 308-318
    • Price, V.L.1    Taylor, W.E.2    Clevenger, W.3    Worthington, M.4    Young, E.T.5
  • 40
    • 0030829982 scopus 로고    scopus 로고
    • Effects of medium composition and nutrient limitation on loss of the recombinant plasmid pLG669-z and beta-galactosidase expression by Saccharomyces cerevisiae
    • O'Kennedy R.D., and Patching J.W. Effects of medium composition and nutrient limitation on loss of the recombinant plasmid pLG669-z and beta-galactosidase expression by Saccharomyces cerevisiae. J. Ind. Microbiol. Biotechnol. 18 (1997) 319-325
    • (1997) J. Ind. Microbiol. Biotechnol. , vol.18 , pp. 319-325
    • O'Kennedy, R.D.1    Patching, J.W.2
  • 41
    • 0036270964 scopus 로고    scopus 로고
    • Vacuolar proteases and proteolytic artifacts in Saccharomyces cerevisiae
    • Jones E.W. Vacuolar proteases and proteolytic artifacts in Saccharomyces cerevisiae. Methods Enzymol 351 (2002) 127-150
    • (2002) Methods Enzymol , vol.351 , pp. 127-150
    • Jones, E.W.1
  • 44
    • 0013091910 scopus 로고    scopus 로고
    • Inhibition of tobacco etch virus protease activity by detergents
    • Mohanty A.K., Simmons C.R., and Wiener M.C. Inhibition of tobacco etch virus protease activity by detergents. Protein Expr. Purif. 27 (2003) 109-114
    • (2003) Protein Expr. Purif. , vol.27 , pp. 109-114
    • Mohanty, A.K.1    Simmons, C.R.2    Wiener, M.C.3
  • 46
    • 28544450037 scopus 로고    scopus 로고
    • Purification and characterization of a recombinant G-protein-coupled receptor, Saccharomyces cerevisiae Ste2p, transiently expressed in HEK293 EBNA1 cells
    • Shi C., Shin Y.O., Hanson J., Cass B., Loewen M.C., and Durocher Y. Purification and characterization of a recombinant G-protein-coupled receptor, Saccharomyces cerevisiae Ste2p, transiently expressed in HEK293 EBNA1 cells. Biochemistry 44 (2005) 15705-15714
    • (2005) Biochemistry , vol.44 , pp. 15705-15714
    • Shi, C.1    Shin, Y.O.2    Hanson, J.3    Cass, B.4    Loewen, M.C.5    Durocher, Y.6
  • 47
    • 33747754219 scopus 로고    scopus 로고
    • Crucial steps in the structure determination of the Na+/H+ antiporter NhaA in its native conformation
    • Screpanti E., Padan E., Rimon A., Michel H., and Hunte C. Crucial steps in the structure determination of the Na+/H+ antiporter NhaA in its native conformation. J. Mol. Biol. 362 (2006) 192-202
    • (2006) J. Mol. Biol. , vol.362 , pp. 192-202
    • Screpanti, E.1    Padan, E.2    Rimon, A.3    Michel, H.4    Hunte, C.5
  • 48
    • 4344579363 scopus 로고    scopus 로고
    • A pedestrian guide to membrane protein crystallization
    • Wiener M.C. A pedestrian guide to membrane protein crystallization. Methods 34 (2004) 364-372
    • (2004) Methods , vol.34 , pp. 364-372
    • Wiener, M.C.1
  • 49
    • 0033520934 scopus 로고    scopus 로고
    • Large scale purification of detergent-soluble P-glycoprotein from Pichia pastoris cells and characterization of nucleotide binding properties of wild-type Walker A, and Walker B mutant proteins
    • Lerner-Marmarosh N., Gimi K., Urbatsch I.L., Gros P., and Senior A.E. Large scale purification of detergent-soluble P-glycoprotein from Pichia pastoris cells and characterization of nucleotide binding properties of wild-type Walker A, and Walker B mutant proteins. J. Biol. Chem. 274 (1999) 34711-34718
    • (1999) J. Biol. Chem. , vol.274 , pp. 34711-34718
    • Lerner-Marmarosh, N.1    Gimi, K.2    Urbatsch, I.L.3    Gros, P.4    Senior, A.E.5
  • 50
    • 33646029095 scopus 로고    scopus 로고
    • Effect of membrane charge on flow and protein transport during ultrafiltration
    • Mehta A., and Zydney A.L. Effect of membrane charge on flow and protein transport during ultrafiltration. Biotechnol. Prog. 22 (2006) 484-492
    • (2006) Biotechnol. Prog. , vol.22 , pp. 484-492
    • Mehta, A.1    Zydney, A.L.2
  • 51
    • 33746486656 scopus 로고    scopus 로고
    • Oligomeric states of proteins determined by size-exclusion chromatography coupled with light scattering absorbance, and refractive index detectors
    • Folta-Stogniew E. Oligomeric states of proteins determined by size-exclusion chromatography coupled with light scattering absorbance, and refractive index detectors. Meth. Mol. Biol. 328 (2006) 97-112
    • (2006) Meth. Mol. Biol. , vol.328 , pp. 97-112
    • Folta-Stogniew, E.1
  • 52
    • 0024321837 scopus 로고
    • Membrane protein molecular weight determined by low-angle laser light-scattering photometry coupled with high-performance gel chromatography
    • Hayashi Y., Matsui H., and Takagi T. Membrane protein molecular weight determined by low-angle laser light-scattering photometry coupled with high-performance gel chromatography. Meth. Enzymol. 172 (1989) 514-528
    • (1989) Meth. Enzymol. , vol.172 , pp. 514-528
    • Hayashi, Y.1    Matsui, H.2    Takagi, T.3
  • 53
    • 0030571043 scopus 로고    scopus 로고
    • Size-exclusion chromatography with on-line light-scattering absorbance, and refractive index detectors for studying proteins and their interactions.
    • Wen J., Arakawa T., and Philo J.S. Size-exclusion chromatography with on-line light-scattering absorbance, and refractive index detectors for studying proteins and their interactions. Anal. Biochem. 240 (1996) 155-166
    • (1996) Anal. Biochem. , vol.240 , pp. 155-166
    • Wen, J.1    Arakawa, T.2    Philo, J.S.3
  • 54
    • 23644444909 scopus 로고    scopus 로고
    • Refractive index-based determination of detergent concentration and its application to the study of membrane proteins
    • Strop P., and Brunger A.T. Refractive index-based determination of detergent concentration and its application to the study of membrane proteins. Protein Sci. 14 (2005) 2207-2211
    • (2005) Protein Sci. , vol.14 , pp. 2207-2211
    • Strop, P.1    Brunger, A.T.2
  • 55
    • 18844387867 scopus 로고    scopus 로고
    • Stochastic theory of size exclusion chromatography: peak shape analysis on single columns
    • Felinger A., Pasti L., Dondi F., van Hulst M., Schoenmakers P.J., and Martin M. Stochastic theory of size exclusion chromatography: peak shape analysis on single columns. Anal. Chem. 77 (2005) 3138-3148
    • (2005) Anal. Chem. , vol.77 , pp. 3138-3148
    • Felinger, A.1    Pasti, L.2    Dondi, F.3    van Hulst, M.4    Schoenmakers, P.J.5    Martin, M.6
  • 56
    • 55649088213 scopus 로고    scopus 로고
    • Static light scattering to characterize membrane proteins in detergent solution
    • Slotboom D.J., Duurkens R.H., Olieman K., and Erkens G.B. Static light scattering to characterize membrane proteins in detergent solution. Methods 46 (2008) 73-82
    • (2008) Methods , vol.46 , pp. 73-82
    • Slotboom, D.J.1    Duurkens, R.H.2    Olieman, K.3    Erkens, G.B.4
  • 58
    • 23244456428 scopus 로고    scopus 로고
    • Crystal structure of a mammalian voltage-dependent Shaker family K+ channel
    • Long S.B., Campbell E.B., and Mackinnon R. Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science 309 (2005) 897-903
    • (2005) Science , vol.309 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3
  • 59
    • 0038303147 scopus 로고    scopus 로고
    • A defined protein-detergent-lipid complex for crystallization of integral membrane proteins: the cytochrome b6f complex of oxygenic photosynthesis
    • Zhang H., Kurisu G., Smith J.L., and Cramer W.A. A defined protein-detergent-lipid complex for crystallization of integral membrane proteins: the cytochrome b6f complex of oxygenic photosynthesis. Proc. Natl. Acad. Sci. USA 100 (2003) 5160-5163
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5160-5163
    • Zhang, H.1    Kurisu, G.2    Smith, J.L.3    Cramer, W.A.4
  • 60
    • 43649107013 scopus 로고    scopus 로고
    • Binding of alkyl polyglucoside surfactants to bacteriorhodopsin and its relation to protein stability
    • Santonicola M.G., Lenhoff A.M., and Kaler E.W. Binding of alkyl polyglucoside surfactants to bacteriorhodopsin and its relation to protein stability. Biophys. J. 94 (2008) 3647-3658
    • (2008) Biophys. J. , vol.94 , pp. 3647-3658
    • Santonicola, M.G.1    Lenhoff, A.M.2    Kaler, E.W.3
  • 61
    • 0026210859 scopus 로고
    • Efficient production of recombinant DNA proteins in Saccharomyces cerevisiae by controlled high-cell-density fermentation
    • Alberghina L., Porro D., Martegani E., and Ranzi B.M. Efficient production of recombinant DNA proteins in Saccharomyces cerevisiae by controlled high-cell-density fermentation. Biotechnol. Appl. Biochem. 14 (1991) 82-92
    • (1991) Biotechnol. Appl. Biochem. , vol.14 , pp. 82-92
    • Alberghina, L.1    Porro, D.2    Martegani, E.3    Ranzi, B.M.4
  • 62
    • 0030019291 scopus 로고    scopus 로고
    • An integrating vector for tunable High copy, stable integration into the dispersed Ty delta sites of Saccharomyces cerevisiae
    • Parekh R.N., Shaw M.R., and Wittrup K.D. An integrating vector for tunable High copy, stable integration into the dispersed Ty delta sites of Saccharomyces cerevisiae. Biotechnol. Prog. 12 (1996) 16-21
    • (1996) Biotechnol. Prog. , vol.12 , pp. 16-21
    • Parekh, R.N.1    Shaw, M.R.2    Wittrup, K.D.3
  • 63
    • 0025333081 scopus 로고
    • Regulated GAL4 expression cassette providing controllable and high-level output from high-copy galactose promoters in yeast
    • Mylin L.M., Hofmann K.J., Schultz L.D., and Hopper J.E. Regulated GAL4 expression cassette providing controllable and high-level output from high-copy galactose promoters in yeast. Meth. Enzymol. 185 (1990) 297-308
    • (1990) Meth. Enzymol. , vol.185 , pp. 297-308
    • Mylin, L.M.1    Hofmann, K.J.2    Schultz, L.D.3    Hopper, J.E.4
  • 64
    • 0021343526 scopus 로고
    • Insertion of apocytochrome c into lipid vesicles
    • Dumont M.E., and Richards F.M. Insertion of apocytochrome c into lipid vesicles. J. Biol. Chem. 259 (1984) 4147-4156
    • (1984) J. Biol. Chem. , vol.259 , pp. 4147-4156
    • Dumont, M.E.1    Richards, F.M.2
  • 65
    • 0025938224 scopus 로고
    • Analysis of the oligomeric state of Band 3, the anion transport protein of the human erythrocyte membrane by size exclusion high performance liquid chromatography Oligomeric stability and origin of heterogeneity
    • Casey J.R., and Reithmeier R.A. Analysis of the oligomeric state of Band 3, the anion transport protein of the human erythrocyte membrane by size exclusion high performance liquid chromatography Oligomeric stability and origin of heterogeneity. J. Biol. Chem. 266 (1991) 15726-15737
    • (1991) J. Biol. Chem. , vol.266 , pp. 15726-15737
    • Casey, J.R.1    Reithmeier, R.A.2
  • 67
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes
    • Krogh A., Larsson B., von Heijne G., and Sonnhammer E.L. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 305 (2001) 567-580
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.