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Volumn 363, Issue , 2007, Pages 21-37

Cloning, production, and purification of proteins for a medium-scale structural genomics project

Author keywords

Coexpression; Inclusion bodies; Protein expression; Structural genomics; Yeast proteins

Indexed keywords

ESCHERICHIA COLI; SACCHAROMYCES CEREVISIAE;

EID: 33847327055     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1385/1-59745-209-2:21     Document Type: Article
Times cited : (14)

References (36)
  • 1
    • 0035487690 scopus 로고    scopus 로고
    • A tour of structural genomics
    • Brenner, S. E. (2001) A tour of structural genomics. Nat. Rev. Genet. 2, 801-809.
    • (2001) Nat. Rev. Genet , vol.2 , pp. 801-809
    • Brenner, S.E.1
  • 4
    • 0031860811 scopus 로고    scopus 로고
    • Chaperone coexpression plasmids: Differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escherichia coli
    • Nishihara, K., Kitagawa, M., Yanagi, H., and Yura, T. (1998) Chaperone coexpression plasmids: differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escherichia coli. Appl. Environ. Microbiol. 64, 1694-1699.
    • (1998) Appl. Environ. Microbiol , vol.64 , pp. 1694-1699
    • Nishihara, K.1    Kitagawa, M.2    Yanagi, H.3    Yura, T.4
  • 5
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure
    • Hendrickson, W A., Horton, J. R., and LeMaster, D. M. (1990) Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure. EMBO J. 9, 1665-1672.
    • (1990) EMBO J , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    LeMaster, D.M.3
  • 6
    • 0000207681 scopus 로고
    • Tmbase: A database of membrane spanning proteins segments
    • Hofmann, K. and Stoffel, W. (1993) Tmbase: A database of membrane spanning proteins segments. Biol. Chem. Hoppe-Seyler 374, 166.
    • (1993) Biol. Chem. Hoppe-Seyler , vol.374 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 7
    • 0026656815 scopus 로고
    • Ex-haustive matching of the entire protein sequence database
    • Gonnet, G. H., Cohen, M. A., and Benner, S. A. (1992) Ex-haustive matching of the entire protein sequence database. Science 256, 1443-1445.
    • (1992) Science , vol.256 , pp. 1443-1445
    • Gonnet, G.H.1    Cohen, M.A.2    Benner, S.A.3
  • 8
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson, W. R. and Lipman, D. J. (1988) Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA 85, 2444-2448.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 10
    • 0041620432 scopus 로고    scopus 로고
    • The PredictProtein server
    • Rost B. and Liu J. (2003) The PredictProtein server. Nucleic Acids Res. 31, 3300-3304.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3300-3304
    • Rost, B.1    Liu, J.2
  • 11
    • 9144257886 scopus 로고    scopus 로고
    • The Pfam protein families database
    • Bateman A., Coin L., Durbin R., et al. (2004) The Pfam protein families database. Nucleic Acids Res. 32, 138-141.
    • (2004) Nucleic Acids Res , vol.32 , pp. 138-141
    • Bateman, A.1    Coin, L.2    Durbin, R.3
  • 12
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G., and Gibson, T. J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 13
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced Genome Annotation using Structural Profiles in the Program 3D-PSSM
    • Kelley, L. A., MacCallum, R. M., and Sternberg, M. J. E. (2000) Enhanced Genome Annotation using Structural Profiles in the Program 3D-PSSM. J. Mol. Biol. 299, 499-520.
    • (2000) J. Mol. Biol , vol.299 , pp. 499-520
    • Kelley, L.A.1    MacCallum, R.M.2    Sternberg, M.J.E.3
  • 15
    • 0030690133 scopus 로고    scopus 로고
    • Deciphering protein sequence information through hydrophobic cluster analysis (HCA): Current status and perspectives
    • Callebaut, I., Labesse, G., Durand, P., et al. (1997) Deciphering protein sequence information through hydrophobic cluster analysis (HCA): current status and perspectives. Cell. Mol. Life Sci. 53, 621-645.
    • (1997) Cell. Mol. Life Sci , vol.53 , pp. 621-645
    • Callebaut, I.1    Labesse, G.2    Durand, P.3
  • 16
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier, F. W. and Moffatt, B. A. (1986) Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189, 113-130.
    • (1986) J. Mol. Biol , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 17
    • 0028605713 scopus 로고
    • Novel approach to molecular cloning and polynucleotide synthesis using vaccinia DNA topoisomerase
    • Shuman, S. (1994) Novel approach to molecular cloning and polynucleotide synthesis using vaccinia DNA topoisomerase. J. Biol. Chem. 269, 32,678-32,684.
    • (1994) J. Biol. Chem , vol.269
    • Shuman, S.1
  • 18
    • 3543065278 scopus 로고    scopus 로고
    • Refolding strategies from inclusion bodies in a structural genomics project
    • Trésaugues, L., Collinet, B., Minard, P., et al. (2004) Refolding strategies from inclusion bodies in a structural genomics project. J. Struct. Funct. Genomics 5, 195-204.
    • (2004) J. Struct. Funct. Genomics , vol.5 , pp. 195-204
    • Trésaugues, L.1    Collinet, B.2    Minard, P.3
  • 19
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutants hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux B. and Walker J. (1996) Over-production of proteins in Escherichia coli: mutants 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.2
  • 20
    • 0029365773 scopus 로고
    • Cell-free synthesis and amino acidselective stable isotope labeling of proteins for NMR analysis
    • Kigawa, T., Muto, Y., and Yokoyama, S. (1995) Cell-free synthesis and amino acidselective stable isotope labeling of proteins for NMR analysis. J. Biomol. NMR 6, 129-134.
    • (1995) J. Biomol. NMR , vol.6 , pp. 129-134
    • Kigawa, T.1    Muto, Y.2    Yokoyama, S.3
  • 21
    • 0032923295 scopus 로고    scopus 로고
    • Cell-free production and stableisotope labeling of milligram quantities of proteins
    • Kigawa, T., Yabuki, T., Yoshida, Y., et al. (1999) Cell-free production and stableisotope labeling of milligram quantities of proteins. FEBS Lett. 442, 15-19.
    • (1999) FEBS Lett , vol.442 , pp. 15-19
    • Kigawa, T.1    Yabuki, T.2    Yoshida, Y.3
  • 22
    • 0036145552 scopus 로고    scopus 로고
    • Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli
    • Hammarstrom, M., Hellgren, N., van Den Berg, S., Berglund, H., and Hard, T. (2002) Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli. Protein Sci. 11, 313-321.
    • (2002) Protein Sci , vol.11 , pp. 313-321
    • Hammarstrom, M.1    Hellgren, N.2    van Den Berg, S.3    Berglund, H.4    Hard, T.5
  • 23
    • 0141888960 scopus 로고    scopus 로고
    • Improving protein folding efficiency by directed evolution using the GFP folding reporter
    • Waldo, G. S. (2003) Improving protein folding efficiency by directed evolution using the GFP folding reporter. Methods Mol. Biol. 230, 343-359.
    • (2003) Methods Mol. Biol , vol.230 , pp. 343-359
    • Waldo, G.S.1
  • 24
    • 0037048809 scopus 로고    scopus 로고
    • High-throughput screening for expression of heterologous proteins in the yeast Pichia pastoris
    • Boettner, M., Prinz, B., Holz, C., Stahl, U., and Lang, C. (2002) High-throughput screening for expression of heterologous proteins in the yeast Pichia pastoris. J. Biotechnol. 99, 51-62.
    • (2002) J. Biotechnol , vol.99 , pp. 51-62
    • Boettner, M.1    Prinz, B.2    Holz, C.3    Stahl, U.4    Lang, C.5
  • 25
    • 36549012605 scopus 로고    scopus 로고
    • Determination of optimal cultivation conditions for large scale production of yeast carboxyl methyltransferase (Ppml) in Escherichia coli
    • submitted
    • Bettache, N. A., Quevillon-Cheruel, S., Bondet, V., van Tilbeurgh, H., and Blondeau, K. Determination of optimal cultivation conditions for large scale production of yeast carboxyl methyltransferase (Ppml) in Escherichia coli, submitted.
    • Bettache, N.A.1    Quevillon-Cheruel, S.2    Bondet, V.3    van Tilbeurgh, H.4    Blondeau, K.5
  • 26
    • 0033152987 scopus 로고    scopus 로고
    • Application of fed-batch fermentation to the preparation of isotopically labeled or selenomethionyl-labeled proteins
    • Studts, J. M. and Fox, B. G. (1999) Application of fed-batch fermentation to the preparation of isotopically labeled or selenomethionyl-labeled proteins. Protein Expr. Purif. 16, 109-119.
    • (1999) Protein Expr. Purif , vol.16 , pp. 109-119
    • Studts, J.M.1    Fox, B.G.2
  • 27
    • 0027439390 scopus 로고
    • Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin
    • Van Duyne, G. D., Standaert, R. F., Karplus, P. A., Schreiber, S. L., and Clardy, J. (1993) Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. J. Mol. Biol. 229, 105-124.
    • (1993) J. Mol. Biol , vol.229 , pp. 105-124
    • Van Duyne, G.D.1    Standaert, R.F.2    Karplus, P.A.3    Schreiber, S.L.4    Clardy, J.5
  • 28
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • Doublie, S. (1997) Preparation of selenomethionyl proteins for phase determination. Meth. Enzymol. 276, 523-530.
    • (1997) Meth. Enzymol , vol.276 , pp. 523-530
    • Doublie, S.1
  • 29
    • 36549059064 scopus 로고    scopus 로고
    • Sambrook, J., Frits, E. F., and Maniatis, T. (eds.) (1989) Preparation and transformation of competent E.coli. In: Molecular Cloning, 2nd ed., CSH Laboratory Press, Cold Spring Harbor, NY, pp. I.74-I.84.
    • Sambrook, J., Frits, E. F., and Maniatis, T. (eds.) (1989) Preparation and transformation of competent E.coli. In: Molecular Cloning, 2nd ed., CSH Laboratory Press, Cold Spring Harbor, NY, pp. I.74-I.84.
  • 31
    • 0037015054 scopus 로고    scopus 로고
    • Lesley, S. A., Kuhn, P., Godzik, A., et al. (2002) Structural genomics of the Thermotoga maritima proteome implemented in a high-throughput structure determination pipeline. Proc. Natl. Acad. Sci. USA 99, 11, 664-11, 669.
    • Lesley, S. A., Kuhn, P., Godzik, A., et al. (2002) Structural genomics of the Thermotoga maritima proteome implemented in a high-throughput structure determination pipeline. Proc. Natl. Acad. Sci. USA 99, 11, 664-11, 669.
  • 32
    • 0037351701 scopus 로고    scopus 로고
    • Medium-scale structural genomics: Strategies for protein expression and crystallization
    • Vincentelli, R., Bignon, C., Gruez, A., et al. (2003) Medium-scale structural genomics: strategies for protein expression and crystallization. Acc. Chem. Res. 36, 165-172.
    • (2003) Acc. Chem. Res , vol.36 , pp. 165-172
    • Vincentelli, R.1    Bignon, C.2    Gruez, A.3
  • 33
    • 0037349370 scopus 로고    scopus 로고
    • Facilities and methods for the high-throughput crystal structural analysis of human proteins
    • Heinemann, U., Bussow, K., Mueller, U., and Umbach, P. (2003) Facilities and methods for the high-throughput crystal structural analysis of human proteins. Acc. Chem. Res. 36, 157-163.
    • (2003) Acc. Chem. Res , vol.36 , pp. 157-163
    • Heinemann, U.1    Bussow, K.2    Mueller, U.3    Umbach, P.4
  • 34
    • 0037478890 scopus 로고    scopus 로고
    • Contribution of structural genomics to understanding the biology of Escherichia coli
    • Matte, A., Sivaraman, J., Ekiel, I., Gehring, K., Jia, Z., and Cygler, M. (2003) Contribution of structural genomics to understanding the biology of Escherichia coli. J. Bacteriol. 185, 3994-4002.
    • (2003) J. Bacteriol , vol.185 , pp. 3994-4002
    • Matte, A.1    Sivaraman, J.2    Ekiel, I.3    Gehring, K.4    Jia, Z.5    Cygler, M.6
  • 35
    • 0038648648 scopus 로고    scopus 로고
    • Crystal structures of fusion proteins with large-affinity tags
    • Smyth, D. R., Mrozkiewicz, M. K., McGrath, W. J., Listwan, P., and Kobe, B. (2003) Crystal structures of fusion proteins with large-affinity tags. Protein Sci. 12, 1313-1322.
    • (2003) Protein Sci , vol.12 , pp. 1313-1322
    • Smyth, D.R.1    Mrozkiewicz, M.K.2    McGrath, W.J.3    Listwan, P.4    Kobe, B.5
  • 36
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky, V. N. (2002) Natively unfolded proteins: a point where biology waits for physics. Protein Sci. 11, 739-756.
    • (2002) Protein Sci , vol.11 , pp. 739-756
    • Uversky, V.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.