Abstract
The development of a system capable of synthesizing any desired protein on a preparative scale is one of the most important endeavors in biotechnology today. Three strategies are currently being used: chemical synthesis, in vivo expression, and cell-free protein synthesis. The first two methods have severe limitations: chemical synthesis is not feasible for the synthesis of long peptides because of low yield, and in vivo expression can produce only those proteins that do not affect the physiology of the host cell [1–3]. Cell-free translation systems, in contrast, can synthesize proteins with high speed and accuracy, approaching in vivo rates [4–5], and they can express proteins that would interfere with cell physiology. However, they are relatively inefficient because of their instability[6].
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Golf SA, Goldberg A L (1987) An increased content of protease La, the Ion gene product, increases protein degradation and blocks growth in E. coli. J Biol Chem 262: 4508–4515
Chrunyk BA, Evans J, Lillquist J, Young P, Wetzel R (1993) Inclusion body formation and protein stability in sequence variants of interleukin-1β. J Biol Chem 268: 18053–18061
Henrich B, Lubitz W, Plapp R (1982) Lysis of E. coli by induction of cloned φX174 gene. Mol Gen Genet 185: 493–497
Kurland C G (1982) Translational accuracy in vitro. Cell 28: 201–202
Pavlov MY, Ehrenberg M (1996) Rate of translation of natural mRNA in an optimized in vitro system. Arch Biochem Biophys 328: 9–16
Roberts BE, Paterson BM (1973) Efficient translation of tobacco mosaic virus RNA and rabbit globin 9S RNA in a cell-free system from commercial wheat germ. Proc Natl Acad Sci USA 70: 2330–2334
Spirin AS, Baranov VI, Ryabova LA, Ovodov Syu, Alakhov YuB (1988) A continuous cell- free translation system capable of producing polypeptides in high yield. Science 242: 1162–1164
Baranov VI, Morozov IYu, Ortlepp SA, Spirin AS (1989) Gene expression in a cell-free system on the preparative scale. Gene 84: 463–466
Endo Y, Otsuzuki S, Ito K, Miura K (1992) Production of an enzymatic active protein using a continuous flow cell-free translation system. J Biotechnol 25: 221–230
Kigawa T, Yokoyama S (1991) A continuous cell-free protein synthesis system for coupled transcription-translation. J Biochem 110: 166–168
Kim DM., Kigawa T, Choi CY, Yokoyama S (1996) A highly efficient cell-free protein synthesis system from E. coli. Eur J Biochem 239: 881–886
Kigawa T, Yabuki T, Yoshida Y, Tsutsui M, Ito Y, Shibata T, Yokoyama S (1999) Cell-free production and stable-isotope labeling of milligram quantities of protein. FEBS Lett 442: 15–19
Kawarasaki Y, Kawai T, Nakano H, Yamane T (1995) A long-lived batch reaction system of cell-free protein synthesis. Anal Biochem 226: 320–324
Endo Y, Mitsui K, Motizuki M, Tsurugi K (1987) The mechanism of action of ricin and related toxic lectins on eukaryotic ribosomes. J Biol Chem 262: 5908–5912
Endo Y, Tsurugi K (1987) RNA N-glycosidase activity of ricin A-chain. J Biol Chem 262: 8128–8130
Wool IG, Glück A, Endo Y (1992) Ribotoxin recognition of ribosomal RNA and a proposal for the mechanism of translation. Trends Biochem Sci 17: 266–269
Barbieri L, Battelli MG, Stirpe F (1993) Ribosome-inactivating proteins from plants. Biochim Biophys Acta 1154: 237–282
Taylor S, Massiah A, Lomonossoff G, Robert LM, Lord JM, Hartely MR (1994) Correlation between the activities of five ribosome-inactivating proteins in depurination of tobacco ribosomes and inhibition of tobacco mosaic virus infection. Plant J 5: 827–853
Ready MP, Brown DT, Robertus JD (1986) Extracellular localization of pokeweed antiviral protein. Proc Natl Acad Sci USA 83: 5053–5056
Massiah AJ, Hartely MR (1995) Wheat ribosome-inactivating proteins: Seed and leaf forms with different specificities and cofactor requirements. Planta 197: 633–640
Ogasawara T, Sawasaki T, Morishita R, Ozawa A, Madin K, Endo Y (1999) A new class of enzyme acting on damaged ribosomes: ribosomal RNA apurinic site specific lyase found in wheat germ. The EMBO J 18: 6522–6531
Madin K, Sawasaki T, Ogasawara T, Endo Y (2000) 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 USA 97: 559–564
Johnston FB, Stern H (1957) Mass-isolation of viable wheat embryos. Nature 179: 160–161
Erickson AH, Blobel G (1983) Cell-free translation of messenger RNA in a wheat germ system. Meths Enzymol 96: 38–50
Hirao I, Yoshinari S, Yokoyama S, Endo Y, Ellington AD (1997) RNA aptamers that bind to and inhibit the ribosome-inactivating protein, pepocin. Nucleic Acids Symp Ser 37: 283–284
Lodish HF, Housman D, Jacobsen M (1971) Initiation of haemoglobin synthesis. Specific inhibition by antibiotics and bacteriophage ribonucleic acid. Biochemistry 10: 2348–2356
Bohlmann H (1994) The role of thionins in plant protection. Critical Rev in Plant Sciences. 13: 1–16
Colilla FJ, Rocher A, Mendez E (1990) Gamma-purothionins: amino acid sequence of two polypeptides of a new family of thionins from wheat endosperm. FEBS Lett 270: 191–194
Brummer J, Thole H, Kloppstech K (1994) Hordothionins inhibit protein synthesis at the level of initiation in the wheat germ system. Eur J Biochem 219: 425–433
Matsushita S (1959) On the protein formation and changes of the amounts of the ribonucleic acid and ribonuclease activity in the grains during the ripening process of wheat. Memoirs of the Res. Inst, for Food Science, Kyoto Univ. No. 19: 1–4
Chiu WL, Niwa Y, Zeng W, Hirano T, Kobayashi H, Sheet J (1996) Engineered GFP as a vital reporter in plants. Current Biology 6: 325–330
Hamamoto H, Sugiyama K, Nakagawa N, Hashida E, Matsunaga Y, Takemoto S, Watanabe Y, Okada Y (1999) A new tobacco mosaic virus vector and its use for the systemic production of angiotensin-1-covering enzyme inhibitor in transgenic tobacco and tomato. Biotechnology 11: 930–932
Dawson WO (1992) Tobamovirus-plant interaction. Virology 186: 359–367
Sachs AB, Sarnow P, Hentze M W (1997) Starting at the beginning, middle, and end: translation initiation in eukaryotes. Cell 89: 831–838
Wells SE, Hillner PE, Vale RD, Sachs AB (1998) Circularization of mRNA by eukaryotic translation initiation factors. Molecular Cell 2: 135–140
Netzer WJ, Hartl FU (1997) Recombination of protein domains facilitated by co-translational folding in eukaryotes. Nature 388: 343–349
Mattheakis LC, Bhatt RR, Dower WJ (1994) An in vitro polysome display system for identifying ligands from very large peptide libraries. Proc Natl Acad Sci USA 91: 9022–9026
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2002 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Madin, K., Sawasaki, T., Endo, Y. (2002). Highly Productive Plant Continuous Cell-Free System. In: Spirin, A.S. (eds) Cell-Free Translation Systems. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-59379-6_9
Download citation
DOI: https://doi.org/10.1007/978-3-642-59379-6_9
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-63956-2
Online ISBN: 978-3-642-59379-6
eBook Packages: Springer Book Archive