메뉴 건너뛰기




Volumn 500, Issue , 2011, Pages 197-212

Protein production in Saccharomyces cerevisiae for systems biology studies

Author keywords

Affinity purification; expression systems; Protein production; Systems biology; Yeast tagged collections

Indexed keywords

PROTEIN;

EID: 80053056359     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/B978-0-12-385118-5.00011-6     Document Type: Chapter
Times cited : (6)

References (46)
  • 1
    • 34249041230 scopus 로고    scopus 로고
    • Exploring genetic interactions and networks with yeast
    • DOI 10.1038/nrg2085, PII NRG2085
    • C. Boone, H. Bussey, and B.J. Andrews Exploring genetic interactions and networks with yeast Nat. Rev. Genet. 8 2007 437 449 (Pubitemid 46789246)
    • (2007) Nature Reviews Genetics , vol.8 , Issue.6 , pp. 437-449
    • Boone, C.1    Bussey, H.2    Andrews, B.J.3
  • 2
    • 71549157111 scopus 로고    scopus 로고
    • Selecting an appropriate method for expressing a recombinant protein
    • W.H. Brondyk Selecting an appropriate method for expressing a recombinant protein Methods Enzymol. 463 2009 131 147
    • (2009) Methods Enzymol. , vol.463 , pp. 131-147
    • Brondyk, W.H.1
  • 3
    • 80053058108 scopus 로고    scopus 로고
    • Quantification of proteins and their modifications using QconCAT technology
    • K.M. Carroll, F. Lanucara, and C.E. Eyers Quantification of proteins and their modifications using QconCAT technology Methods Enzymol. 500 2011 113 131
    • (2011) Methods Enzymol. , vol.500 , pp. 113-131
    • Carroll, K.M.1    Lanucara, F.2    Eyers, C.E.3
  • 6
    • 0036184160 scopus 로고    scopus 로고
    • Ssf1p prevents premature processing of an early pre-60S ribosomal particle
    • DOI 10.1016/S1097-2765(02)00458-6
    • A. Fatica, A.D. Cronshaw, M. Dlakić, and D. Tollervey Ssf1p prevents premature processing of an early pre-60S ribosomal particle Mol. Cell 9 2002 341 351 (Pubitemid 34195559)
    • (2002) Molecular Cell , vol.9 , Issue.2 , pp. 341-351
    • Fatica, A.1    Cronshaw, A.D.2    Dlaki, M.3    Tollervey, D.4
  • 7
    • 77957241623 scopus 로고    scopus 로고
    • Biochemical analysis of PIFTC3, the Trypanosoma brucei orthologue of nematode DYF-13, reveals interactions with established and putative intraflagellar transport components
    • J.B. Franklin, and E. Ullu Biochemical analysis of PIFTC3, the Trypanosoma brucei orthologue of nematode DYF-13, reveals interactions with established and putative intraflagellar transport components Mol. Microbiol. 78 2010 173 186
    • (2010) Mol. Microbiol. , vol.78 , pp. 173-186
    • Franklin, J.B.1    Ullu, E.2
  • 12
    • 0025339819 scopus 로고
    • Expression of heterologous proteins in Escherichia coli
    • DOI 10.1016/0076-6879(90)85004-8
    • L. Gold Expression of heterologous proteins in Escherichia coli Methods Enzymol. 185 1990 11 14 (Pubitemid 20219807)
    • (1990) Methods in Enzymology , vol.185 , pp. 11-14
    • Gold, L.1
  • 13
    • 33744816815 scopus 로고    scopus 로고
    • Subunit architecture of multimeric complexes isolated directly from cells
    • DOI 10.1038/sj.embor.7400702, PII 7400702
    • H. Hernández, A. Dziembowski, T. Taverner, B. Séraphin, and C.V. Robinson Subunit architecture of multimeric complexes isolated directly from cells EMBO Rep. 7 2006 605 610 (Pubitemid 43827327)
    • (2006) EMBO Reports , vol.7 , Issue.6 , pp. 605-610
    • Hernandez, H.1    Dziembowski, A.2    Taverner, T.3    Seraphin, B.4    Robinson, C.V.5
  • 14
    • 34548742936 scopus 로고    scopus 로고
    • Identification and characterization of modification enzymes by biochemical analysis of the proteome
    • J.E. Jackman, L. Kotelawala, E.J. Grayhack, and E.M. Phizicky Identification and characterization of modification enzymes by biochemical analysis of the proteome Methods Enzymol. 425 2007 139 152
    • (2007) Methods Enzymol. , vol.425 , pp. 139-152
    • Jackman, J.E.1    Kotelawala, L.2    Grayhack, E.J.3    Phizicky, E.M.4
  • 15
    • 84934443276 scopus 로고    scopus 로고
    • The use of Saccharomyces cerevisiae proteomic libraries to identify RNA-modifying proteins
    • J.E. Jackman, E.J. Grayhack, and E.M. Phizicky The use of Saccharomyces cerevisiae proteomic libraries to identify RNA-modifying proteins Methods Mol. Biol. 488 2008 383 393
    • (2008) Methods Mol. Biol. , vol.488 , pp. 383-393
    • Jackman, J.E.1    Grayhack, E.J.2    Phizicky, E.M.3
  • 16
    • 71549150895 scopus 로고    scopus 로고
    • Baculovirus-insect cell expression
    • D.L. Jarvis Baculovirus-insect cell expression Methods Enzymol. 463 2009 191 222
    • (2009) Methods Enzymol. , vol.463 , pp. 191-222
    • Jarvis, D.L.1
  • 18
    • 13944274948 scopus 로고    scopus 로고
    • The past, present and future of cell-free protein synthesis
    • DOI 10.1016/j.tibtech.2005.01.003, PII S0167779905000259
    • F. Katzen, G. Chang, and W. Kudlicki The past, present and future of cell-free protein synthesis Trends Biotechnol. 23 2005 150 156 (Pubitemid 40269848)
    • (2005) Trends in Biotechnology , vol.23 , Issue.3 , pp. 150-156
    • Katzen, F.1    Chang, G.2    Kudlicki, W.3
  • 19
    • 2942676743 scopus 로고    scopus 로고
    • Metabolomics and systems biology: Making sense of the soup
    • DOI 10.1016/j.mib.2004.04.012, PII S1369527404000505
    • D.B. Kell Metabolomics and systems biology: Making sense of the soup Curr. Opin. Microbiol. 7 2004 296 307 (Pubitemid 38765114)
    • (2004) Current Opinion in Microbiology , vol.7 , Issue.3 , pp. 296-307
    • Kell, D.B.1
  • 20
    • 33644959172 scopus 로고    scopus 로고
    • Metabolomics, modelling and machine learning in systems biology - Towards an understanding of the languages of cells. The 2005 Theodor Bücher Lecture
    • D.B. Kell Metabolomics, modelling and machine learning in systems biology - Towards an understanding of the languages of cells. The 2005 Theodor Bücher Lecture FEBS J. 273 2006 873 894
    • (2006) FEBS J. , vol.273 , pp. 873-894
    • Kell, D.B.1
  • 23
    • 33748296315 scopus 로고    scopus 로고
    • Proteome chips for whole-organism assays
    • DOI 10.1038/nrm1941, PII NRM1941
    • L.A. Kung, and M. Snyder Proteome chips for whole-organism assays Nat. Rev. Mol. Cell Biol. 7 2006 617 622 (Pubitemid 44325353)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.8 , pp. 617-622
    • Kung, L.A.1    Snyder, M.2
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 47049126717 scopus 로고    scopus 로고
    • Cdc34p ubiquitin-conjugating enzyme is a component of the tombusvirus replicase complex and ubiquitinates p33 replication protein
    • DOI 10.1128/JVI.00702-08
    • Z. Li, D. Barajas, T. Panavas, D.A. Herbst, and P.D. Nagy Cdc34p ubiquitin-conjugating enzyme is a component of the tombusvirus replicase complex and ubiquitinates p33 replication protein J. Virol. 82 2008 6911 6926 (Pubitemid 351977712)
    • (2008) Journal of Virology , vol.82 , Issue.14 , pp. 6911-6926
    • Li, Z.1    Barajas, D.2    Panavas, T.3    Herbst, D.A.4    Nagy, P.D.5
  • 26
    • 35248832984 scopus 로고    scopus 로고
    • High-efficiency protein expression in plants from agroinfection- compatible tobacco mosaic virus expression vectors
    • J.A. Lindbo High-efficiency protein expression in plants from agroinfection-compatible tobacco mosaic virus expression vectors BMC Biotechnol. 7 2007 52
    • (2007) BMC Biotechnol. , vol.7 , pp. 52
    • Lindbo, J.A.1
  • 27
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • S.C. Makrides Strategies for achieving high-level expression of genes in Escherichia coli Microbiol. Rev. 60 1996 512 538 (Pubitemid 26303477)
    • (1996) Microbiological Reviews , vol.60 , Issue.3 , pp. 512-538
    • Makrides, S.C.1
  • 28
    • 71549130731 scopus 로고    scopus 로고
    • Tagging for protein expression
    • A. Malhotra Tagging for protein expression Methods Enzymol. 463 2009 239 258
    • (2009) Methods Enzymol. , vol.463 , pp. 239-258
    • Malhotra, A.1
  • 29
    • 33748939071 scopus 로고    scopus 로고
    • 7 GpppX Pyrophosphatase Activity that Locates to P Bodies
    • DOI 10.1016/j.jmb.2006.08.015, PII S0022283606010266
    • N. Malys, and J.E.G. McCarthy Dcs2, a novel stress-induced modulator of m7G pppX pyrophosphatase activity that locates to P bodies J. Mol. Biol. 363 2006 370 382 (Pubitemid 44436253)
    • (2006) Journal of Molecular Biology , vol.363 , Issue.2 , pp. 370-382
    • Malys, N.1    McCarthy, J.E.G.2
  • 30
    • 79953721157 scopus 로고    scopus 로고
    • Translation initiation: Variations in the mechanism can be anticipated
    • N. Malys, and J.E.G. McCarthy Translation initiation: Variations in the mechanism can be anticipated Cell. Mol. Life Sci. 68 2011 991 1003
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 991-1003
    • Malys, N.1    McCarthy, J.E.G.2
  • 31
    • 0036303629 scopus 로고    scopus 로고
    • A bipartite bacteriophage T4 SOC and HOC randomized peptide display library: Detection and analysis of phage T4 terminase (gp17) and late σ factor (gp55) interaction
    • DOI 10.1016/S0022-2836(02)00298-X
    • N. Malys, D.-Y. Chang, R.G. Baumann, D. Xie, and L.W. Black A bipartite bacteriophage T4 SOC and HOC randomized peptide display library: Detection and analysis of phage T4 terminase (gp17) and late σ factor (gp55) interaction J. Mol. Biol. 319 2002 289 304 (Pubitemid 34729458)
    • (2002) Journal of Molecular Biology , vol.319 , Issue.2 , pp. 289-304
    • Malys, N.1    Chang, D.-Y.2    Baumann, R.G.3    Xie, D.4    Black, L.W.5
  • 32
    • 3042761261 scopus 로고    scopus 로고
    • 7 GpppX pyrophosphatase activity of Dcs1 modulates nutrient-induced responses in yeast
    • DOI 10.1093/nar/gkh687
    • N. Malys, K. Carroll, J. Miyan, D. Tollervey, and J.E.G. McCarthy The 'scavenger' m7G pppX pyrophosphatase activity of Dcs1 modulates nutrient-induced responses in yeast Nucleic Acids Res. 32 2004 3590 3600 (Pubitemid 39157707)
    • (2004) Nucleic Acids Research , vol.32 , Issue.12 , pp. 3590-3600
    • Malys, N.1    Carroll, K.2    Miyan, J.3    Tollervey, D.4    McCarthy, J.E.G.5
  • 33
    • 71549133050 scopus 로고    scopus 로고
    • Enzyme kinetics and computational modeling for systems biology
    • P. Mendes, H. Messiha, N. Malys, and S. Hoops Enzyme kinetics and computational modeling for systems biology Methods Enzymol. 467 2009 583 599
    • (2009) Methods Enzymol. , vol.467 , pp. 583-599
    • Mendes, P.1    Messiha, H.2    Malys, N.3    Hoops, S.4
  • 34
    • 80053084213 scopus 로고    scopus 로고
    • Towards a full quantitative description of yeast metabolism: A systematic approach for estimating the kinetic parameters of isoenzymes under in-vivo like conditions
    • H.L. Messiha, N. Malys, and K.M. Carroll Towards a full quantitative description of yeast metabolism: A systematic approach for estimating the kinetic parameters of isoenzymes under in-vivo like conditions Methods Enzymol. 500 2011 215 231
    • (2011) Methods Enzymol. , vol.500 , pp. 215-231
    • Messiha, H.L.1    Malys, N.2    Carroll, K.M.3
  • 35
    • 79951575052 scopus 로고    scopus 로고
    • What is the true enzyme kinetics in the biological system? An investigation of macromolecular crowding effect upon enzyme kinetics of glucose-6-phosphate dehydrogenase
    • M.G. Norris, and N. Malys What is the true enzyme kinetics in the biological system? An investigation of macromolecular crowding effect upon enzyme kinetics of glucose-6-phosphate dehydrogenase Biochem. Biophys. Res. Commun. 405 2011 388 392
    • (2011) Biochem. Biophys. Res. Commun. , vol.405 , pp. 388-392
    • Norris, M.G.1    Malys, N.2
  • 36
    • 74049121769 scopus 로고    scopus 로고
    • Isolation and compositional analysis of trypanosomatid editosomes
    • A.K. Panigrahi, A. Schnaufer, and K.D. Stuart Isolation and compositional analysis of trypanosomatid editosomes Methods Enzymol. 424 2007 3 24
    • (2007) Methods Enzymol. , vol.424 , pp. 3-24
    • Panigrahi, A.K.1    Schnaufer, A.2    Stuart, K.D.3
  • 37
    • 0034841844 scopus 로고    scopus 로고
    • The tandem affinity purification (TAP) method: A general procedure of protein complex purification
    • DOI 10.1006/meth.2001.1183
    • O. Puig, F. Caspary, G. Rigaut, B. Rutz, E. Bouveret, E. Bragado-Nilsson, M. Wilm, and B. Seraphin The tandem affinity purification (TAP) method: A general procedure of protein complex purification Methods 24 2001 218 229 (Pubitemid 32846428)
    • (2001) Methods , vol.24 , Issue.3 , pp. 218-229
    • Puig, O.1    Caspary, F.2    Rigaut, G.3    Rutz, B.4    Bouveret, E.5    Bragado-Nilsson, E.6    Wilm, M.7    Seraphin, B.8
  • 38
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • DOI 10.1038/13732
    • G. Rigaut, A. Shevchenko, B. Rutz, M. Wilm, M. Mann, and B. Seraphin A generic protein purification method for protein complex characterization and proteome exploration Nat. Biotechnol. 17 1999 1030 1032 (Pubitemid 29474865)
    • (1999) Nature Biotechnology , vol.17 , Issue.10 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Seraphin, B.6
  • 41
    • 0022186670 scopus 로고
    • Measurement of protein using bicinchoninic acid
    • DOI 10.1016/0003-2697(85)90442-7
    • P.K. Smith, R.I. Krohn, G.T. Hermanson, A.K. Mallia, F.H. Gartner, M.D. Provenzano, E.K. Fujimoto, N.M. Goeke, B.J. Olson, and D.C. Klenk Measurement of protein using bicinchoninic acid Anal. Biochem. 150 1985 76 85 (Pubitemid 16258399)
    • (1985) Analytical Biochemistry , vol.150 , Issue.1 , pp. 76-85
    • Smith, P.K.1    Krohn, R.I.2    Hermanson, G.T.3
  • 44
    • 34548110776 scopus 로고    scopus 로고
    • Select what you need: A comparative evaluation of the advantages and limitations of frequently used expression systems for foreign genes
    • DOI 10.1016/j.jbiotec.2006.07.012, PII S0168165606006237
    • J. Yin, G. Li, X. Ren, and G. Herrler Select what you need: A comparative evaluation of the advantages and limitations of frequently used expression systems for foreign genes J. Biotechnol. 127 2007 335 347 (Pubitemid 44827384)
    • (2007) Journal of Biotechnology , vol.127 , Issue.3 , pp. 335-347
    • Yin, J.1    Li, G.2    Ren, X.3    Herrler, G.4
  • 45
    • 71549172205 scopus 로고    scopus 로고
    • Bacterial systems for production of heterologous proteins
    • S. Zerbs, A.M. Frank, and F.R. Collart Bacterial systems for production of heterologous proteins Methods Enzymol. 463 2009 149 168
    • (2009) Methods Enzymol. , vol.463 , pp. 149-168
    • Zerbs, S.1    Frank, A.M.2    Collart, F.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.