메뉴 건너뛰기




Volumn 150, Issue 1, 2010, Pages 44-50

Limiting factors of the translation machinery

Author keywords

Cell free protein synthesis; Escherichia coli; S30 extract; Translation factors

Indexed keywords

AMINOACYL; CELL FREE PROTEIN SYNTHESIS; CELL-FREE PRODUCTION; E. COLI; IN-VITRO; IN-VIVO; LIMITING FACTORS; PROTEIN SYNTHESIS; S30 EXTRACT; SYNTHETASES; TRANSLATION FACTORS;

EID: 77957353805     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2010.07.017     Document Type: Article
Times cited : (7)

References (28)
  • 1
    • 84965189705 scopus 로고
    • Protein turnover and incorporation of labeled amino acids into tissue proteins in vivo and in vitro
    • Borsook H. Protein turnover and incorporation of labeled amino acids into tissue proteins in vivo and in vitro. Physiol. Rev. 1950, 30:206-219.
    • (1950) Physiol. Rev. , vol.30 , pp. 206-219
    • Borsook, H.1
  • 2
    • 34547699646 scopus 로고    scopus 로고
    • Energy systems for ATP regeneration in cell-free protein synthesis reactions
    • Review
    • Calhoun K.A., Swartz J.R. Energy systems for ATP regeneration in cell-free protein synthesis reactions. Methods Mol. Biol. 2007, 375:3-17. Review.
    • (2007) Methods Mol. Biol. , vol.375 , pp. 3-17
    • Calhoun, K.A.1    Swartz, J.R.2
  • 3
    • 0025166089 scopus 로고
    • Secondary structure of the ribosome binding site determines translational efficiency: a quantitative analysis
    • De Smit M.H., van Duin J. Secondary structure of the ribosome binding site determines translational efficiency: a quantitative analysis. Proc. Natl. Acad. Sci. U.S.A. 1990, 87:7668-7672.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 7668-7672
    • De Smit, M.H.1    van Duin, J.2
  • 4
    • 0141975780 scopus 로고    scopus 로고
    • High-throughput, genome-scale protein production method based on the wheat germ cell-free expression system
    • Review
    • Endo Y., Sawasaki T. High-throughput, genome-scale protein production method based on the wheat germ cell-free expression system. Biotechnol. Adv. 2003, 21:695-713. Review.
    • (2003) Biotechnol. Adv. , vol.21 , pp. 695-713
    • Endo, Y.1    Sawasaki, T.2
  • 5
    • 0010290680 scopus 로고
    • Effect of nucleic acids on protein synthesis and amino-acid incorporation in disrupted staphylococcal cells
    • Gale E.F., Folkes J.P. Effect of nucleic acids on protein synthesis and amino-acid incorporation in disrupted staphylococcal cells. Nature 1954, 173:1223-1227.
    • (1954) Nature , vol.173 , pp. 1223-1227
    • Gale, E.F.1    Folkes, J.P.2
  • 6
    • 0021839582 scopus 로고
    • Isolation and point of action of a factor from Escherichia coli required to reconstruct translation
    • Ganoza M.C., Cunningham C., Green R.M. Isolation and point of action of a factor from Escherichia coli required to reconstruct translation. Proc. Natl. Acad. Sci. U.S.A. 1985, 82:1648-1652.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 1648-1652
    • Ganoza, M.C.1    Cunningham, C.2    Green, R.M.3
  • 7
    • 33751532962 scopus 로고    scopus 로고
    • The ribosomal stalk binds to translation factors IF2, EF-Tu, EF-G and RF3 via a conserved region of the L12 c-terminal domain
    • Helgstrand M., Mandava C.S., Mulder F.A.A., Liljas A., Sanyal S., Akke M. The ribosomal stalk binds to translation factors IF2, EF-Tu, EF-G and RF3 via a conserved region of the L12 c-terminal domain. J. Mol. Biol. 2006, 365:468-479.
    • (2006) J. Mol. Biol. , vol.365 , pp. 468-479
    • Helgstrand, M.1    Mandava, C.S.2    Mulder, F.A.A.3    Liljas, A.4    Sanyal, S.5    Akke, M.6
  • 9
    • 0030250637 scopus 로고    scopus 로고
    • A semicontinuous prokaryotic coupled transcription/translation system using a dialysis membrane
    • Kim D.M., Choi C.Y. A semicontinuous prokaryotic coupled transcription/translation system using a dialysis membrane. Biotechnol. Prog. 1996, 12:645-649.
    • (1996) Biotechnol. Prog. , vol.12 , pp. 645-649
    • Kim, D.M.1    Choi, C.Y.2
  • 10
    • 0029956987 scopus 로고    scopus 로고
    • A highly efficient cell-free protein synthesis system from Escherichia coli
    • Kim D.M., Kigawa T., Choi C.Y., Yokoyama S. A highly efficient cell-free protein synthesis system from Escherichia coli. Eur. J. Biochem. 1996, 239:881-886.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 881-886
    • Kim, D.M.1    Kigawa, T.2    Choi, C.Y.3    Yokoyama, S.4
  • 11
    • 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., Choi C.Y. Rapid production of milligram quantities of proteins in a batch cell-free protein synthesis system. J. Biotechnol. 2006, 124:373-380.
    • (2006) J. Biotechnol. , vol.124 , pp. 373-380
    • Kim, T.W.1    Kim, D.M.2    Choi, C.Y.3
  • 12
    • 34547691508 scopus 로고    scopus 로고
    • Cell-free production of integral membrane proteins on a preparative scale
    • Review
    • Klammt C., Schwarz D., Dötsch V., Bernhard F. Cell-free production of integral membrane proteins on a preparative scale. Methods Mol. Biol. 2007, 375:57-78. Review.
    • (2007) Methods Mol. Biol. , vol.375 , pp. 57-78
    • Klammt, C.1    Schwarz, D.2    Dötsch, V.3    Bernhard, F.4
  • 13
    • 0026481261 scopus 로고
    • High efficiency cell-free synthesis of proteins: refinement of the coupled transcription/translation system
    • Kudlicki W., Kramer G., Hardesty B. High efficiency cell-free synthesis of proteins: refinement of the coupled transcription/translation system. Anal. Biochem. 1992, 206:389-393.
    • (1992) Anal. Biochem. , vol.206 , pp. 389-393
    • Kudlicki, W.1    Kramer, G.2    Hardesty, B.3
  • 15
    • 0034681174 scopus 로고    scopus 로고
    • A highly efficient and robust cell-free protein synthesis system prepared from wheat embryos: plants apparently contain a suicide system directed at ribosomes
    • Madin K., Sawasaki T., Ogasawara T., Endo Y. A highly efficient and robust cell-free protein synthesis system prepared from wheat embryos: plants apparently contain a suicide system directed at ribosomes. Proc. Natl. Acad. Sci. U.S.A. 2000, 97:559-564.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 559-564
    • Madin, K.1    Sawasaki, T.2    Ogasawara, T.3    Endo, Y.4
  • 16
    • 44049091569 scopus 로고    scopus 로고
    • SPARK: a new peptidyl transferase activity assay
    • Mankin A.S., Polacek N. SPARK: a new peptidyl transferase activity assay. Methods Mol. Med. 2008, 142:107-116.
    • (2008) Methods Mol. Med. , vol.142 , pp. 107-116
    • Mankin, A.S.1    Polacek, N.2
  • 17
    • 0035717170 scopus 로고    scopus 로고
    • Cell-free production of biologically active polypeptides: application to the synthesis of antibacterial polypeptide cecropin
    • Martemyanov K.A., Shirokov V.A., Kurnasov O.V., Gudkov A.T., Spirin A.S. Cell-free production of biologically active polypeptides: application to the synthesis of antibacterial polypeptide cecropin. Protein Expres. Purif. 2001, 21:456-461.
    • (2001) Protein Expres. Purif. , vol.21 , pp. 456-461
    • Martemyanov, K.A.1    Shirokov, V.A.2    Kurnasov, O.V.3    Gudkov, A.T.4    Spirin, A.S.5
  • 19
    • 0025989820 scopus 로고
    • A coupled in vitro transcription-translation system for the exclusive synthesis of polypeptides expressed from the T7 promotor
    • Nevin D.E., Pratt J.M. A coupled in vitro transcription-translation system for the exclusive synthesis of polypeptides expressed from the T7 promotor. FEBS Lett. 1991, 291:259-263.
    • (1991) FEBS Lett. , vol.291 , pp. 259-263
    • Nevin, D.E.1    Pratt, J.M.2
  • 20
    • 0030779476 scopus 로고    scopus 로고
    • Release factor RF3 abolishes competition between release factor RF1 and ribosome recycling factor (RRF) for a ribosome binding site
    • Pavlov M.Y., Freistroffer D.V., Heurgué-Hamard V., Buckingham R.H., Ehrenberg M. Release factor RF3 abolishes competition between release factor RF1 and ribosome recycling factor (RRF) for a ribosome binding site. J. Mol. Biol. 1997, 273:389-401.
    • (1997) J. Mol. Biol. , vol.273 , pp. 389-401
    • Pavlov, M.Y.1    Freistroffer, D.V.2    Heurgué-Hamard, V.3    Buckingham, R.H.4    Ehrenberg, M.5
  • 21
    • 0001951544 scopus 로고
    • IRL Press, Oxford, UK and Washington, DC, B.D. Hames, S.J. Higgins (Eds.)
    • Pratt J.M. In Transcription and Translation 1984, 179-209. IRL Press, Oxford, UK and Washington, DC. B.D. Hames, S.J. Higgins (Eds.).
    • (1984) In Transcription and Translation , pp. 179-209
    • Pratt, J.M.1
  • 22
    • 0016415604 scopus 로고
    • Chloramphenicol acetyltransferase from chloramphenicol-resistant bacteria
    • Shaw W.V. Chloramphenicol acetyltransferase from chloramphenicol-resistant bacteria. Methods Enzymol. 1975, 43:737-755.
    • (1975) Methods Enzymol. , vol.43 , pp. 737-755
    • Shaw, W.V.1
  • 24
    • 23044504786 scopus 로고    scopus 로고
    • Protein synthesis by pure translation systems
    • Shimizu Y., Kanamori T., Ueda T. Protein synthesis by pure translation systems. Methods 2005, 36:299-304.
    • (2005) Methods , vol.36 , pp. 299-304
    • Shimizu, Y.1    Kanamori, T.2    Ueda, T.3
  • 25
    • 4644269746 scopus 로고    scopus 로고
    • High-throughput cell-free systems for synthesis of functionally active proteins
    • Review
    • Spirin A.S. High-throughput cell-free systems for synthesis of functionally active proteins. Trends Biotechnol. 2004, 22:538-545. Review.
    • (2004) Trends Biotechnol. , vol.22 , pp. 538-545
    • Spirin, A.S.1
  • 26
    • 0024297305 scopus 로고
    • A continuous cell-free translation system capable of producing polypeptides in high yield
    • Spirin A.S., Baranov V.I., Ryabova L.A., Ovodov S.Y., Alakhov Y.B. A continuous cell-free translation system capable of producing polypeptides in high yield. Science 1988, 242:1162-1164.
    • (1988) Science , vol.242 , pp. 1162-1164
    • Spirin, A.S.1    Baranov, V.I.2    Ryabova, L.A.3    Ovodov, S.Y.4    Alakhov, Y.B.5
  • 27
    • 23244446620 scopus 로고    scopus 로고
    • Quantitative polysome analysis identifies limitations in bacterial cell-free protein synthesis
    • Underwood K.A., Swartz J.R., Puglisi J.D. Quantitative polysome analysis identifies limitations in bacterial cell-free protein synthesis. Biotechnol. Bioeng. 2005, 91:425-435.
    • (2005) Biotechnol. Bioeng. , vol.91 , pp. 425-435
    • Underwood, K.A.1    Swartz, J.R.2    Puglisi, J.D.3
  • 28
    • 0019426060 scopus 로고
    • Attenuation in the control of expression of bacterial operons
    • Yanofsky C. Attenuation in the control of expression of bacterial operons. Nature 1981, 289:751-758.
    • (1981) Nature , vol.289 , pp. 751-758
    • Yanofsky, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.