메뉴 건너뛰기




Volumn 350, Issue 3, 2006, Pages 562-567

The presence of a common downstream box enables the simultaneous expression of multiple proteins in an E. coli extract

Author keywords

Cell free protein synthesis; Co expression; Downstream box; S30 extract

Indexed keywords

BACTERIAL DNA; CHLORAMPHENICOL ACETYLTRANSFERASE; NUCLEOTIDE; RECOMBINANT PROTEIN;

EID: 33749600895     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.09.072     Document Type: Article
Times cited : (14)

References (25)
  • 1
    • 0035895435 scopus 로고    scopus 로고
    • Dissecting the interaction network of multiprotein complexes by pairwise co-expression of subunits in E. coli
    • Fribourq S., Romier C., Werten S., Gangloff Y.G., Poterszman A., and Moras D. Dissecting the interaction network of multiprotein complexes by pairwise co-expression of subunits in E. coli. J. Mol. Biol. 306 (2001) 363-373
    • (2001) J. Mol. Biol. , vol.306 , pp. 363-373
    • Fribourq, S.1    Romier, C.2    Werten, S.3    Gangloff, Y.G.4    Poterszman, A.5    Moras, D.6
  • 2
    • 0027369381 scopus 로고
    • Co-overexpression of bacterial GroESL chaperonins partly overcomes non-productive folding and tetramer assembly of E. coli-expressed human medium-chain acyl-CoA dehydrogenase (MCAD) carrying the prevalent disease-causing K304E mutation
    • Bross P., Andresen B.S., Winter V., Krautle F., Jensen T.G., Nandy A., Kolvraa S., Ghisla S., Bolund L., and Gregersen N. Co-overexpression of bacterial GroESL chaperonins partly overcomes non-productive folding and tetramer assembly of E. coli-expressed human medium-chain acyl-CoA dehydrogenase (MCAD) carrying the prevalent disease-causing K304E mutation. Biochim. Biophys. Acta 1182 (1993) 264-274
    • (1993) Biochim. Biophys. Acta , vol.1182 , pp. 264-274
    • Bross, P.1    Andresen, B.S.2    Winter, V.3    Krautle, F.4    Jensen, T.G.5    Nandy, A.6    Kolvraa, S.7    Ghisla, S.8    Bolund, L.9    Gregersen, N.10
  • 3
    • 0030938085 scopus 로고    scopus 로고
    • Co-expression of nuclear receptor partners increases their solubility and biological activities
    • Li C., Schwabe J.W., Banayo E., and Evans R.M. Co-expression of nuclear receptor partners increases their solubility and biological activities. Proc. Natl. Acad. Sci. USA 94 (1997) 2278-2283
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2278-2283
    • Li, C.1    Schwabe, J.W.2    Banayo, E.3    Evans, R.M.4
  • 4
    • 0037458018 scopus 로고    scopus 로고
    • Visualization of coupled protein folding and binding in bacteria and purification of the heterodimeric complex
    • Wang H., and Chong S. Visualization of coupled protein folding and binding in bacteria and purification of the heterodimeric complex. Proc. Natl. Acad. Sci. USA 100 (2003) 478-483
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 478-483
    • Wang, H.1    Chong, S.2
  • 5
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson H.J., and Wright P.E. Coupling of folding and binding for unstructured proteins. Curr. Opin. Struct. Biol. 12 (2002) 54-60
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 7
    • 5344225676 scopus 로고    scopus 로고
    • General co-expression vectors for the overexpression of heterodimeric protein complexes in Escherichia coli
    • Dzivenu O.K., Park H.H., and Wu H. General co-expression vectors for the overexpression of heterodimeric protein complexes in Escherichia coli. Protein Expr. Purif. 38 (2004) 1-8
    • (2004) Protein Expr. Purif. , vol.38 , pp. 1-8
    • Dzivenu, O.K.1    Park, H.H.2    Wu, H.3
  • 8
    • 27144555357 scopus 로고    scopus 로고
    • Regulation of translation via mRNA structure in prokaryotes and eukaryotes
    • Kozak M. Regulation of translation via mRNA structure in prokaryotes and eukaryotes. Gene 361 (2005) 13-37
    • (2005) Gene , vol.361 , pp. 13-37
    • Kozak, M.1
  • 9
    • 31344474305 scopus 로고    scopus 로고
    • Strategies for protein co-expression in Escherichia coli
    • Tolia N.H., and Joshua-Tor L. Strategies for protein co-expression in Escherichia coli. Nat. Methods 3 (2006) 55-64
    • (2006) Nat. Methods , vol.3 , pp. 55-64
    • Tolia, N.H.1    Joshua-Tor, L.2
  • 10
    • 1842582929 scopus 로고    scopus 로고
    • Bacteria co-transformed with recombinant proteins and chaperones cloned in independent plasmids are suitable for expression tuning
    • de Marco A., and De Marco V. Bacteria co-transformed with recombinant proteins and chaperones cloned in independent plasmids are suitable for expression tuning. J. Biotechnol. 109 (2004) 45-52
    • (2004) J. Biotechnol. , vol.109 , pp. 45-52
    • de Marco, A.1    De Marco, V.2
  • 11
    • 33646095238 scopus 로고    scopus 로고
    • A set of ligation-independent expression vectors for co-expression of proteins in Escherichia coli
    • Chanda P.K., Edris W.A., and Kennedy J.D. A set of ligation-independent expression vectors for co-expression of proteins in Escherichia coli. Protein Expr. Purif. 47 (2006) 217-224
    • (2006) Protein Expr. Purif. , vol.47 , pp. 217-224
    • Chanda, P.K.1    Edris, W.A.2    Kennedy, J.D.3
  • 13
    • 4644269746 scopus 로고    scopus 로고
    • High-throughput cell-free systems for synthesis of functionally active proteins
    • Spirin A.S. High-throughput cell-free systems for synthesis of functionally active proteins. Trends Biotechnol. 22 (2004) 538-545
    • (2004) Trends Biotechnol. , vol.22 , pp. 538-545
    • Spirin, A.S.1
  • 14
    • 16544367648 scopus 로고    scopus 로고
    • Cell-free protein synthesis systems: increasing their performance and applications
    • Nakano H., Kawarasaki Y., and Yamane T. Cell-free protein synthesis systems: increasing their performance and applications. Adv. Biochem. Eng. Biotechnol. 90 (2004) 135-149
    • (2004) Adv. Biochem. Eng. Biotechnol. , vol.90 , pp. 135-149
    • Nakano, H.1    Kawarasaki, Y.2    Yamane, T.3
  • 15
    • 2142639387 scopus 로고    scopus 로고
    • Analyzing and enhancing mRNA translational efficiency in an Escherichia coli in vitro expression system
    • Voges D., Watzele M., Nemetz C., Wizemann S., and Buchberger B. Analyzing and enhancing mRNA translational efficiency in an Escherichia coli in vitro expression system. Biochem. Biophys. Res. Commun. 318 (2004) 601-614
    • (2004) Biochem. Biophys. Res. Commun. , vol.318 , pp. 601-614
    • Voges, D.1    Watzele, M.2    Nemetz, C.3    Wizemann, S.4    Buchberger, B.5
  • 16
    • 0033529890 scopus 로고    scopus 로고
    • Enhancement of translation by the downstream box does not involve base pairing of mRNA with the penultimate stem sequence of 16S rRNA
    • O'Connor M., Asai T., Squires C.L., and Dahlberg A.E. Enhancement of translation by the downstream box does not involve base pairing of mRNA with the penultimate stem sequence of 16S rRNA. Proc. Natl. Acad. Sci. USA 96 (1999) 8973-8978
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8973-8978
    • O'Connor, M.1    Asai, T.2    Squires, C.L.3    Dahlberg, A.E.4
  • 17
    • 0035941484 scopus 로고    scopus 로고
    • Codon bias at the 3′-side of the initiation codon is correlated with translation initiation efficiency in Escherichia coli
    • Stenstrom C.M., Jin H., Major L.L., Tate W.P., and Isaksson L.A. Codon bias at the 3′-side of the initiation codon is correlated with translation initiation efficiency in Escherichia coli. Gene 263 (2001) 273-284
    • (2001) Gene , vol.263 , pp. 273-284
    • Stenstrom, C.M.1    Jin, H.2    Major, L.L.3    Tate, W.P.4    Isaksson, L.A.5
  • 18
    • 0035827918 scopus 로고    scopus 로고
    • Cooperative effects by the initiation codon and its flanking regions on translation initiation
    • Stenstrom C.M., Holmgren E., and Isaksson L.A. Cooperative effects by the initiation codon and its flanking regions on translation initiation. Gene 273 (2001) 259-265
    • (2001) Gene , vol.273 , pp. 259-265
    • Stenstrom, C.M.1    Holmgren, E.2    Isaksson, L.A.3
  • 19
    • 0037123362 scopus 로고    scopus 로고
    • Influences on translation initiation and early elongation by the messenger RNA region flanking the initiation codon at the 3′ side
    • Stenstrom C.M., and Isaksson L.A. Influences on translation initiation and early elongation by the messenger RNA region flanking the initiation codon at the 3′ side. Gene 288 (2002) 1-8
    • (2002) Gene , vol.288 , pp. 1-8
    • Stenstrom, C.M.1    Isaksson, L.A.2
  • 20
    • 4944224262 scopus 로고    scopus 로고
    • A codon window in mRNA downstream of the initiation codon where NGG codons give strongly reduced gene expression in Escherichia coli
    • Gonzalez de Valdivia E.I., and Isaksson L.A. A codon window in mRNA downstream of the initiation codon where NGG codons give strongly reduced gene expression in Escherichia coli. Nucleic Acids Res. 32 (2004) 5198-5205
    • (2004) Nucleic Acids Res. , vol.32 , pp. 5198-5205
    • Gonzalez de Valdivia, E.I.1    Isaksson, L.A.2
  • 21
    • 27144528592 scopus 로고    scopus 로고
    • Abortive translation caused by peptidyl-tRNA drop-off at NGG codons in the early coding region of mRNA
    • Gonzalez de Valdivia E.I., and Isaksson L.A. Abortive translation caused by peptidyl-tRNA drop-off at NGG codons in the early coding region of mRNA. FEBS J. 272 (2005) 5306-5316
    • (2005) FEBS J. , vol.272 , pp. 5306-5316
    • Gonzalez de Valdivia, E.I.1    Isaksson, L.A.2
  • 22
    • 0029956987 scopus 로고    scopus 로고
    • A highly efficient cell-free protein synthesis system from Escherichia coli
    • Kim D.M., Kigawa T., Choi C.Y., and Yokoyama S. A highly efficient cell-free protein synthesis system from Escherichia coli. Eur. J. Biochem. 239 (1996) 881-886
    • (1996) Eur. J. Biochem. , vol.239 , pp. 881-886
    • Kim, D.M.1    Kigawa, T.2    Choi, C.Y.3    Yokoyama, S.4
  • 23
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H., and von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166 (1987) 368-379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    von Jagow, G.2
  • 24
    • 33745196264 scopus 로고    scopus 로고
    • Rapid production of milligram quantities of proteins in a batch cell-free protein synthesis system
    • Kim T.W., Kim D.M., and Choi C.Y. Rapid production of milligram quantities of proteins in a batch cell-free protein synthesis system. J. Biotechnol. 124 (2006) 373-380
    • (2006) J. Biotechnol. , vol.124 , pp. 373-380
    • Kim, T.W.1    Kim, D.M.2    Choi, C.Y.3
  • 25
    • 33645286487 scopus 로고    scopus 로고
    • Enhancing the efficiency of cell-free protein synthesis through the polymerase-chain-reaction-based addition of a translation enhancer sequence and the in situ removal of the extra amino acid residues
    • Son J.M., Ahn J.H., Hwang M.Y., Park C.G., Choi C.Y., and Kim D.M. Enhancing the efficiency of cell-free protein synthesis through the polymerase-chain-reaction-based addition of a translation enhancer sequence and the in situ removal of the extra amino acid residues. Anal. Biochem. 351 (2006) 187-192
    • (2006) Anal. Biochem. , vol.351 , pp. 187-192
    • Son, J.M.1    Ahn, J.H.2    Hwang, M.Y.3    Park, C.G.4    Choi, C.Y.5    Kim, D.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.