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Volumn 14, Issue 7, 2005, Pages 1729-1740

Design of improved membrane protein production experiments: Quantitation of the host response

Author keywords

Expression systems; Membrane proteins; Miniarray; Protein production; Yeast

Indexed keywords

FARNESYLPYROPHOSPHATE SYNTHETASE 1; GLUCOSE; MEMBRANE PROTEIN; MESSENGER RNA; RECOMBINANT PROTEIN; SYNTHETASE; UNCLASSIFIED DRUG;

EID: 22244478668     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.051435705     Document Type: Article
Times cited : (53)

References (45)
  • 2
    • 0037087411 scopus 로고    scopus 로고
    • Mutants defective in secretory/vacuolar pathways in the EUROFAN collection of yeast disruptants
    • Avaro, S., Belgareh-Touze, N., Sibella-Arguelles, C., Volland, C., and Haguenauer-Tsapis, R. 2002. Mutants defective in secretory/vacuolar pathways in the EUROFAN collection of yeast disruptants. Yeast 19: 351-371.
    • (2002) Yeast , vol.19 , pp. 351-371
    • Avaro, S.1    Belgareh-Touze, N.2    Sibella-Arguelles, C.3    Volland, C.4    Haguenauer-Tsapis, R.5
  • 3
    • 0035158317 scopus 로고    scopus 로고
    • Yeast - A panacea for the structure-function analysis of membrane proteins?
    • Bill, R.M. 2001. Yeast - A panacea for the structure-function analysis of membrane proteins? Curr. Genet. 40: 157-171.
    • (2001) Curr. Genet. , vol.40 , pp. 157-171
    • Bill, R.M.1
  • 4
    • 0035965254 scopus 로고    scopus 로고
    • Analysis of the pore of the unusual major intrinsic protein channel, yeast Fps1p
    • Bill, R.M., Hedfalk, K., Karlgren, S., Mullins, J.G., Rydström, J., and Hohmann, S. 2001. Analysis of the pore of the unusual major intrinsic protein channel, yeast Fps1p. J. Biol. Chem. 276: 36543-36549.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36543-36549
    • Bill, R.M.1    Hedfalk, K.2    Karlgren, S.3    Mullins, J.G.4    Rydström, J.5    Hohmann, S.6
  • 5
    • 0024421221 scopus 로고
    • hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures
    • Borkovich, K.A., Farrelly, F.W., Finkelstein, D.B., Taulien, J., and Lindquist, S. 1989. hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures. Mol. Cell. Biol. 9: 3919-3930.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3919-3930
    • Borkovich, K.A.1    Farrelly, F.W.2    Finkelstein, D.B.3    Taulien, J.4    Lindquist, S.5
  • 7
    • 0141533196 scopus 로고    scopus 로고
    • Co-expression of molecular chaperones does not improve the heterologous expression of mammalian G-protein coupled receptor expression in yeast
    • Butz, J.A., Niebauer, R.T., and Robinson, A.S. 2003. Co-expression of molecular chaperones does not improve the heterologous expression of mammalian G-protein coupled receptor expression in yeast. Biotechnol. Bioeng. 84: 292-304.
    • (2003) Biotechnol. Bioeng. , vol.84 , pp. 292-304
    • Butz, J.A.1    Niebauer, R.T.2    Robinson, A.S.3
  • 8
    • 0025924634 scopus 로고
    • Glycosylation and structure of the yeast MF α 1 α-factor precursor is important for efficient transport through the secretory pathway
    • Caplan, S., Green, R., Rocco, J., and Kurjan, J. 1991. Glycosylation and structure of the yeast MF α 1 α-factor precursor is important for efficient transport through the secretory pathway. J. Bacteriol. 173: 627-635.
    • (1991) J. Bacteriol. , vol.173 , pp. 627-635
    • Caplan, S.1    Green, R.2    Rocco, J.3    Kurjan, J.4
  • 9
    • 0037195803 scopus 로고    scopus 로고
    • Kinetic analysis of the translocation of fluorescent precursor proteins into Escherichia coli membrane vesicles
    • De Keyzer, J., Van Der Does, C., and Driessen, A.J. 2002. Kinetic analysis of the translocation of fluorescent precursor proteins into Escherichia coli membrane vesicles. J. Biol. Chem. 277: 46059-46065.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46059-46065
    • De Keyzer, J.1    Van Der Does, C.2    Driessen, A.J.3
  • 10
    • 0024828302 scopus 로고
    • SEC62 encodes a putative membrane protein required for protein translocation into the yeast endoplasmic reticulum
    • Deshaies, R.J. and Schekman, R. 1989. SEC62 encodes a putative membrane protein required for protein translocation into the yeast endoplasmic reticulum. J. Cell. Biol. 109: 2653-2664.
    • (1989) J. Cell. Biol. , vol.109 , pp. 2653-2664
    • Deshaies, R.J.1    Schekman, R.2
  • 13
    • 0141794536 scopus 로고    scopus 로고
    • A novel yeast expression system for the overproduction of qualitycontrolled membrane proteins
    • Griffith, D.A., Delipala, C., Leadsham, J., Jarvis, S.M., and Oesterhelt, D. 2003. A novel yeast expression system for the overproduction of qualitycontrolled membrane proteins. FEBS Lett. 553: 45-50.
    • (2003) FEBS Lett. , vol.553 , pp. 45-50
    • Griffith, D.A.1    Delipala, C.2    Leadsham, J.3    Jarvis, S.M.4    Oesterhelt, D.5
  • 14
    • 0029142564 scopus 로고
    • Overexpression of integral membrane proteins for structural studies
    • Grisshammer, R. and Tate, C. 1995. Overexpression of integral membrane proteins for structural studies. Q. Rev. Biophys. 3: 315-422.
    • (1995) Q. Rev. Biophys. , vol.3 , pp. 315-422
    • Grisshammer, R.1    Tate, C.2
  • 17
    • 0025608262 scopus 로고
    • The proton extrusion of growing yeast cultures as an on-line parameter in fermentation processes: Ammonium assimilation and proton extrusion are correlated by 1:1 stoichiometry in nitrogen-limited fed-batch fermentations
    • Huth, J., Werner, S., and Muller, H.-G. 1990. The proton extrusion of growing yeast cultures as an on-line parameter in fermentation processes: Ammonium assimilation and proton extrusion are correlated by 1:1 stoichiometry in nitrogen-limited fed-batch fermentations. J. Basic Microbiol. 30: 561-567.
    • (1990) J. Basic Microbiol. , vol.30 , pp. 561-567
    • Huth, J.1    Werner, S.2    Muller, H.-G.3
  • 18
    • 0028907462 scopus 로고
    • High-level production of a human membrane protein in yeast: The peripheral-type benzodiazepine receptor
    • Joseph-Liauzun, E., Farges, R., Le Fur, G., Ferrara, P., and Loison, G. 1995. High-level production of a human membrane protein in yeast: The peripheral-type benzodiazepine receptor. Gene 155: 195-199.
    • (1995) Gene , vol.155 , pp. 195-199
    • Joseph-Liauzun, E.1    Farges, R.2    Le Fur, G.3    Ferrara, P.4    Loison, G.5
  • 19
    • 0035951647 scopus 로고    scopus 로고
    • Positive and negative regulation of squalene synthase (ERG9), an ergosterol biosynthetic gene, in Saccharomyces cerevisiae
    • Kennedy, M.A. and Bard, M. 2001. Positive and negative regulation of squalene synthase (ERG9), an ergosterol biosynthetic gene, in Saccharomyces cerevisiae. Biochim. Biophys. Acta 1517: 177-189.
    • (2001) Biochim. Biophys. Acta , vol.1517 , pp. 177-189
    • Kennedy, M.A.1    Bard, M.2
  • 20
    • 0033807177 scopus 로고    scopus 로고
    • Yeast secretory expression of insulin precursors
    • Kjeldsen, T. 2000. Yeast secretory expression of insulin precursors. Appl. Microbiol. Biotechnol. 54: 277-286.
    • (2000) Appl. Microbiol. Biotechnol. , vol.54 , pp. 277-286
    • Kjeldsen, T.1
  • 22
    • 0037450575 scopus 로고    scopus 로고
    • Lactococcus lactis as host for overproduction of functional membrane proteins
    • Kunji, E.R., Slotboom, D.J., and Poolman, B. 2003. Lactococcus lactis as host for overproduction of functional membrane proteins. Biochim. Biophys. Acta 1610: 97-108.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 97-108
    • Kunji, E.R.1    Slotboom, D.J.2    Poolman, B.3
  • 23
    • 0027200830 scopus 로고
    • The role of physiological state in osmotolerance of the salt-tolerant yeast Debaryomyces hansenii
    • Larsson, C. and Gustafsson, L. 1993. The role of physiological state in osmotolerance of the salt-tolerant yeast Debaryomyces hansenii. Can. J. Microbiol. 39: 603-609.
    • (1993) Can. J. Microbiol. , vol.39 , pp. 603-609
    • Larsson, C.1    Gustafsson, L.2
  • 24
    • 0037450521 scopus 로고    scopus 로고
    • Semliki Forest virus vectors for rapid and high-level expression of integral membrane proteins
    • Lundstrom, K. 2003. Semliki Forest virus vectors for rapid and high-level expression of integral membrane proteins. Biochim. Biophys. Acta 1610: 90-96.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 90-96
    • Lundstrom, K.1
  • 25
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux, B. and Walker, J.E. 1996. Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260: 289-298.
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 26
    • 0028215997 scopus 로고
    • Continued functioning of the secretory pathway is essential for ribosome synthesis
    • Mizuta, K. and Warner, J.R. 1994. Continued functioning of the secretory pathway is essential for ribosome synthesis.Mol. Cell. Biol. 14: 2493-2502.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2493-2502
    • Mizuta, K.1    Warner, J.R.2
  • 27
    • 3543088051 scopus 로고    scopus 로고
    • Decreases in yeast expression yields of the human adenosine A2a receptor are a result of translational or post-translational events
    • Niebauer, R.T., Wedekind, A., and Robinson, A.S. 2004. Decreases in yeast expression yields of the human adenosine A2a receptor are a result of translational or post-translational events. Protein Expr. Purif. 37: 134-143.
    • (2004) Protein Expr. Purif. , vol.37 , pp. 134-143
    • Niebauer, R.T.1    Wedekind, A.2    Robinson, A.S.3
  • 28
    • 0029068214 scopus 로고
    • SRP samples nascent chains for the presence of signal sequences by interacting with ribosomes at a discrete step during translation elongation
    • Ogg, S.C. and Walter, P. 1995. SRP samples nascent chains for the presence of signal sequences by interacting with ribosomes at a discrete step during translation elongation. Cell 81: 1075-1084.
    • (1995) Cell , vol.81 , pp. 1075-1084
    • Ogg, S.C.1    Walter, P.2
  • 29
    • 0033662220 scopus 로고    scopus 로고
    • DNA microarray detection of metabolic responses to protein overproduction in Escherichia coli
    • Oh, M.K. and Liao, J.C. 2000. DNA microarray detection of metabolic responses to protein overproduction in Escherichia coli. Metab. Eng. 2: 201-209.
    • (2000) Metab. Eng. , vol.2 , pp. 201-209
    • Oh, M.K.1    Liao, J.C.2
  • 30
    • 0348049833 scopus 로고    scopus 로고
    • Getting to the membrane: How is co-translational protein targeting to the endoplasmic reticulum regulated?
    • Pool, M.R. 2003. Getting to the membrane: How is co-translational protein targeting to the endoplasmic reticulum regulated? Biochem. Soc. Trans. 31: 1232-1237.
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 1232-1237
    • Pool, M.R.1
  • 31
    • 0032191422 scopus 로고    scopus 로고
    • Production of G-protein-coupled receptors in yeast
    • Reilander, H. and Weiss, H.M. 1998. Production of G-protein-coupled receptors in yeast. Curr. Opin. Biotechnol. 9: 510-517.
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 510-517
    • Reilander, H.1    Weiss, H.M.2
  • 32
    • 0024835142 scopus 로고
    • Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeast
    • Rothblatt, J.A., Deshaies, R.J., Sanders, S.L., Daum, G., and Schekman, R. 1989. Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeast. J. Cell. Biol. 109: 2641-2652.
    • (1989) J. Cell. Biol. , vol.109 , pp. 2641-2652
    • Rothblatt, J.A.1    Deshaies, R.J.2    Sanders, S.L.3    Daum, G.4    Schekman, R.5
  • 33
    • 0041876269 scopus 로고    scopus 로고
    • Heterologous expression of G-protein-coupled receptors: Comparison of expression systems from the standpoint of large-scale production and purification
    • Sarramegna, V., Talmont, F., Demange, P., and Milon, A. 2003. Heterologous expression of G-protein-coupled receptors: Comparison of expression systems from the standpoint of large-scale production and purification. Cell. Mol. Life Sci. 60: 1529-1546.
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 1529-1546
    • Sarramegna, V.1    Talmont, F.2    Demange, P.3    Milon, A.4
  • 34
    • 0021799817 scopus 로고
    • The induction of ribosome biosynthesis in a nonmitotic secretory tissue
    • Schmidt, T., Chen, P.S., and Pellegrini, M. 1985. The induction of ribosome biosynthesis in a nonmitotic secretory tissue. J. Biol. Chem. 260: 7645-7650.
    • (1985) J. Biol. Chem. , vol.260 , pp. 7645-7650
    • Schmidt, T.1    Chen, P.S.2    Pellegrini, M.3
  • 35
    • 0037459447 scopus 로고    scopus 로고
    • Structural basis for the function of the β subunit of the eukaryotic signal recognition particle receptor
    • Schwartz, T. and Blobel, G. 2003. Structural basis for the function of the β subunit of the eukaryotic signal recognition particle receptor. Cell 112: 793-803.
    • (2003) Cell , vol.112 , pp. 793-803
    • Schwartz, T.1    Blobel, G.2
  • 36
    • 0030839345 scopus 로고    scopus 로고
    • Characterization of two new genes down-regulated by α-factor
    • Seidel, J. and Tanner, W. 1997. Characterization of two new genes down-regulated by α-factor. Yeast 13: 809-817.
    • (1997) Yeast , vol.13 , pp. 809-817
    • Seidel, J.1    Tanner, W.2
  • 37
    • 0036886546 scopus 로고    scopus 로고
    • The transcriptional response to alkaline pH in Saccharomyces cerevisiae: Evidence for calcium-mediated signalling
    • Serrano, R., Ruiz, A., Bernal, D., Chambers, J.R., and Arino, J. 2002. The transcriptional response to alkaline pH in Saccharomyces cerevisiae: Evidence for calcium-mediated signalling. Mol. Microbiol. 46: 1319-1333.
    • (2002) Mol. Microbiol. , vol.46 , pp. 1319-1333
    • Serrano, R.1    Ruiz, A.2    Bernal, D.3    Chambers, J.R.4    Arino, J.5
  • 38
    • 4544341015 scopus 로고    scopus 로고
    • Linear models and empirical Bayes methods for assessing differential expression in microarray experiments
    • Article 3
    • Smyth, G.K. 2004. Linear models and empirical Bayes methods for assessing differential expression in microarray experiments. Stat. Appl. Genet. Mol. Biol. 3: Article 3.
    • (2004) Stat. Appl. Genet. Mol. Biol. , vol.3
    • Smyth, G.K.1
  • 39
    • 0027058051 scopus 로고
    • Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum
    • Stirling, C.J., Rothblatt, J., Hosobuchi, M., Deshaies, R., and Schekman, R. 1992. Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum. Mol. Biol. Cell 3: 129-142.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 129-142
    • Stirling, C.J.1    Rothblatt, J.2    Hosobuchi, M.3    Deshaies, R.4    Schekman, R.5
  • 44
    • 0031551576 scopus 로고    scopus 로고
    • Mdj2p, a novel DnaJ homolog in the mitochondrial inner membrane of the yeast Saccharomyces cerevisiae
    • Westermann, B. and Neupert, W. 1997. Mdj2p, a novel DnaJ homolog in the mitochondrial inner membrane of the yeast Saccharomyces cerevisiae. J. Mol. Biol. 272: 477-483.
    • (1997) J. Mol. Biol. , vol.272 , pp. 477-483
    • Westermann, B.1    Neupert, W.2
  • 45
    • 6344275303 scopus 로고    scopus 로고
    • Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast
    • Youker, R.T., Walsh, P., Beilharz, T., Lithgow, T., and Brodsky, J.L. 2004. Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast. Mol. Biol. Cell 15: 4787-4797.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4787-4797
    • Youker, R.T.1    Walsh, P.2    Beilharz, T.3    Lithgow, T.4    Brodsky, J.L.5


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