Cell-free translation reconstituted with purified components
10.1038/90802
Crossref journal-article
Springer Science and Business Media LLC
Nature Biotechnology (297)
Bibliography

Shimizu, Y., Inoue, A., Tomari, Y., Suzuki, T., Yokogawa, T., Nishikawa, K., & Ueda, T. (2001). Cell-free translation reconstituted with purified components. Nature Biotechnology, 19(8), 751–755.

Authors 7
  1. Yoshihiro Shimizu (first)
  2. Akio Inoue (additional)
  3. Yukihide Tomari (additional)
  4. Tsutomu Suzuki (additional)
  5. Takashi Yokogawa (additional)
  6. Kazuya Nishikawa (additional)
  7. Takuya Ueda (additional)
References 26 Referenced 1,718
  1. Stiege, W. & Erdmann, V.A. The potentials of the in vitro protein biosynthesis system. J. Biotechnol. 41, 81–90 (1995). (10.1016/0168-1656(95)00005-B) / J. Biotechnol. by W Stiege (1995)
  2. Jermutus, L., Ryabova, L.A. & Pluckthun, A. Recent advances in producing and selecting functional proteins by using cell-free translation. Curr. Opin. Biotechnol. 9, 534–548 (1998). (10.1016/S0958-1669(98)80042-6) / Curr. Opin. Biotechnol. by L Jermutus (1998)
  3. Kitaoka, Y., Nishimura, N. & Niwano, M. Cooperativity of stabilized mRNA and enhanced translation activity in the cell-free system. J. Biotechnol. 48, 1–8 (1996). (10.1016/0168-1656(96)01389-2) / J. Biotechnol. by Y Kitaoka (1996)
  4. Matveev, S.V. et al. Effect of the ATP level on the overall protein biosynthesis rate in a wheat germ cell-free system. Biochim. Biophys. Acta 1293, 207–212 (1996). (10.1016/0167-4838(95)00244-8) / Biochim. Biophys. Acta by SV Matveev (1996)
  5. 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 242, 1162–1164 (1988). (10.1126/science.3055301) / Science by AS Spirin (1988)
  6. Kim, D.M. & Choi, C.Y. A semicontinuous prokaryotic coupled transcription/translation system using a dialysis membrane. Biotechnol. Prog. 12, 645–649 (1996). (10.1021/bp960052l) / Biotechnol. Prog. by DM Kim (1996)
  7. Kung, H.F. et al. DNA-directed in vitro synthesis of beta-galactosidase. Studies with purified factors. J. Biol. Chem. 252, 6889–6894 (1977). (10.1016/S0021-9258(17)39933-7) / J. Biol. Chem. by HF Kung (1977)
  8. 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. USA 82, 1648–1652 (1985). (10.1073/pnas.82.6.1648) / Proc. Natl. Acad. Sci. USA by MC Ganoza (1985)
  9. Pavlov, M.Y. & Ehrenberg, M. Rate of translation of natural mRNAs in an optimized in vitro system. Arch. Biochem. Biophys. 328, 9–16 (1996). (10.1006/abbi.1996.0136) / Arch. Biochem. Biophys. by MY Pavlov (1996)
  10. Pavlov, M.Y., Freistroffer, D.V., Heurgue-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. 273, 389–401 (1997). (10.1006/jmbi.1997.1324) / J. Mol. Biol. by MY Pavlov (1997)
  11. Guillon, J.M., Mechulam, Y., Schmitter, J.M., Blanquet, S. & Fayat, G. Disruption of the gene for Met-tRNA(fMet) formyltransferase severely impairs growth of Escherichia coli. J. Bacteriol. 174, 4294–4301 (1992). (10.1128/JB.174.13.4294-4301.1992) / J. Bacteriol. by JM Guillon (1992)
  12. Benne, R., Arentzen, R. & Voorma, H.O. The mechanism of action of inititation factor F1 from Escherichia coli. Biochim. Biophys. Acta 269, 304–310 (1972). (10.1016/0005-2787(72)90440-6) / Biochim. Biophys. Acta by R Benne (1972)
  13. Atkinson, D.E. The energy charge of the adenylate pool as a regulatory parameter. Interaction with feedback modifiers. Biochemistry 7, 4030–4034 (1968). (10.1021/bi00851a033) / Biochemistry by DE Atkinson (1968)
  14. Noren, C.J., Anthony-Cahill, S.J., Griffith, M.C. & Schultz, P.G. A general method for site-specific incorporation of unnatural amino acids into proteins. Science 244, 182–188 (1989). (10.1126/science.2649980) / Science by CJ Noren (1989)
  15. Kim, D.M., Kigawa, T., Choi, C.Y. & Yokoyama, S. A highly efficient cell-free protein synthesis system from Escherichia coli. Eur. J. Biochem. 239, 881–886 (1996). (10.1111/j.1432-1033.1996.0881u.x) / Eur. J. Biochem. by DM Kim (1996)
  16. Glick, B.R. & Ganoza, M.C. Identification of a soluble protein that stimulates peptide bond synthesis. Proc. Natl. Acad. Sci. USA 72, 4257–4260 (1975). (10.1073/pnas.72.11.4257) / Proc. Natl. Acad. Sci. USA by BR Glick (1975)
  17. Kossel, H. Purification and properties of peptidyl-tRNA hydrolase from Escherichia coli. Biochim. Biophys. Acta 204, 191–202 (1970). (10.1016/0005-2787(70)90502-2) / Biochim. Biophys. Acta by H Kossel (1970)
  18. Lu, J., Aoki, H. & Ganoza, M.C. Molecular characterization of a prokaryotic translation factor homologous to the eukaryotic initiation factor eIF4A. Int. J. Biochem. Cell. Biol. 31, 215–229 (1999). (10.1016/S1357-2725(98)00142-3) / Int. J. Biochem. Cell. Biol. by J Lu (1999)
  19. Spedding, G. Isolation and analysis of ribosomes from prokaryotes, eukaryotes and organelles. In Ribosomes and protein synthesis: a practical approach. (ed. Spedding, G.) 1–29 (IRL Press at Oxford University Press, New York, NY; 1990).
  20. Olins, P.O. & Rangwala, S.H. A novel sequence element derived from bacteriophage T7 mRNA acts as an enhancer of translation of the lacZ gene in Escherichia coli. J. Biol. Chem. 264, 16973–16976 (1989). (10.1016/S0021-9258(18)71444-0) / J. Biol. Chem. by PO Olins (1989)
  21. Sampson, J.R. & Uhlenbeck, O.C. Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro. Proc. Natl. Acad. Sci. USA 85, 1033–1037 (1988). (10.1073/pnas.85.4.1033) / Proc. Natl. Acad. Sci. USA by JR Sampson (1988)
  22. Jelenc, P.C. & Kurland, C.G. Nucleoside triphosphate regeneration decreases the frequency of translation errors. Proc. Natl. Acad. Sci. USA 76, 3174–3178 (1979). (10.1073/pnas.76.7.3174) / Proc. Natl. Acad. Sci. USA by PC Jelenc (1979)
  23. Wagner, E.G., Jelenc, P.C., Ehrenberg, M. & Kurland, C.G. Rate of elongation of polyphenylalanine in vitro. Eur. J. Biochem. 122, 193–197 (1982). (10.1111/j.1432-1033.1982.tb05866.x) / Eur. J. Biochem. by EG Wagner (1982)
  24. Poe, M., Greenfield, N.J., Hirshfield, J.M., Williams, M.N. & Hoogsteen, K. Dihydrofolate reductase. Purification and characterization of the enzyme from an amethopterin-resistant mutant of Escherichia coli. Biochemistry 11, 1023–1030 (1972). (10.1021/bi00756a012) / Biochemistry by M Poe (1972)
  25. Schleif, R.F. l-arabinose operon messenger of Escherichia coli. Its inducibility and translation efficiency relative to lactose operon messenger. J. Mol. Biol. 61, 275–279 (1971). (10.1016/0022-2836(71)90226-9) / J. Mol. Biol. by RF Schleif (1971)
  26. Short, G.F., Golovine, S.Y. & Hecht, S.M. Effect of release factor 1 on in vitro protein translation and the elaboration of protein containing unnatural amino acids. Biochemistry 38, 8808–8819 (1999). (10.1021/bi990281r) / Biochemistry by GF Short (1999)
Dates
Type When
Created 23 years, 1 month ago (July 26, 2002, 4:32 a.m.)
Deposited 2 years, 3 months ago (May 18, 2023, 3:17 p.m.)
Indexed 20 minutes ago (Aug. 27, 2025, 5:19 a.m.)
Issued 24 years ago (Aug. 1, 2001)
Published 24 years ago (Aug. 1, 2001)
Published Online 24 years ago (Aug. 1, 2001)
Published Print 24 years ago (Aug. 1, 2001)
Funders 0

None

@article{Shimizu_2001, title={Cell-free translation reconstituted with purified components}, volume={19}, ISSN={1546-1696}, url={http://dx.doi.org/10.1038/90802}, DOI={10.1038/90802}, number={8}, journal={Nature Biotechnology}, publisher={Springer Science and Business Media LLC}, author={Shimizu, Yoshihiro and Inoue, Akio and Tomari, Yukihide and Suzuki, Tsutomu and Yokogawa, Takashi and Nishikawa, Kazuya and Ueda, Takuya}, year={2001}, month=aug, pages={751–755} }