메뉴 건너뛰기




Volumn 87, Issue 4, 2004, Pages 465-471

Substrate replenishment extends protein synthesis with an in vitro translation system designed to mimic the cytoplasm

Author keywords

Amino acid; Cell free protein synthesis; Combined transcription translation; Cytoplasmic mimicry; Fed batch reaction; Nucleotide

Indexed keywords

BIOMEDICAL ENGINEERING; BIOTECHNOLOGY; CONCENTRATION (PROCESS); DNA; ENERGY ABSORPTION; METABOLISM; RNA; SYNTHESIS (CHEMICAL);

EID: 4344670572     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/bit.20139     Document Type: Article
Times cited : (91)

References (35)
  • 1
    • 0026773209 scopus 로고
    • Structure and mechanism of alkaline phosphatase
    • Coleman JE. 1992. Structure and mechanism of alkaline phosphatase. Annu Rev Biophys Biomol Struct 21:441-483.
    • (1992) Annu Rev Biophys Biomol Struct , vol.21 , pp. 441-483
    • Coleman, J.E.1
  • 2
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko KA, Wanner BL. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA 97:6640-6645.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 4
    • 0014098359 scopus 로고
    • Purification and properties of two acid phosphatase fractions isolated from osmotic shock fluid of Escherichia coli
    • Dvorak HF, Brockman RW, Heppel LA. 1967. Purification and properties of two acid phosphatase fractions isolated from osmotic shock fluid of Escherichia coli. Biochem 6:1743-1751.
    • (1967) Biochem , vol.6 , pp. 1743-1751
    • Dvorak, H.F.1    Brockman, R.W.2    Heppel, L.A.3
  • 5
    • 0023840230 scopus 로고
    • ompT encodes the Escherichia coli outer membrane protease that cleaves T7 RNA polymerase during purification
    • Grodberg J, Dunn JJ. 1988. ompT encodes the Escherichia coli outer membrane protease that cleaves T7 RNA polymerase during purification. J Bacteriol 170:1245-1253.
    • (1988) J Bacteriol , vol.170 , pp. 1245-1253
    • Grodberg, J.1    Dunn, J.J.2
  • 6
    • 0014944191 scopus 로고
    • Cysteine desulfhydrase activities of Salmonella typhimurium and Escherichia coli
    • Guarneros G, Ortega MV. 1970. Cysteine desulfhydrase activities of Salmonella typhimurium and Escherichia coli. Biochim Biophys Acta 198:132-142.
    • (1970) Biochim Biophys Acta , vol.198 , pp. 132-142
    • Guarneros, G.1    Ortega, M.V.2
  • 7
    • 0037205759 scopus 로고    scopus 로고
    • NMR analysis of in vitro-synthesized proteins without purification: A high-throughput approach
    • Guignard L, Ozawa K, Pursglove SE, Otting G, Dixon NE. 2002. NMR analysis of in vitro-synthesized proteins without purification: a high-throughput approach. FEBS Lett 524:159-162.
    • (2002) FEBS Lett , vol.524 , pp. 159-162
    • Guignard, L.1    Ozawa, K.2    Pursglove, S.E.3    Otting, G.4    Dixon, N.E.5
  • 8
    • 0030974119 scopus 로고    scopus 로고
    • In vitro selection and evolution of functional proteins by using ribosome display
    • Hanes J, Pluckthun A. 1997. In vitro selection and evolution of functional proteins by using ribosome display. Proc Natl Acad Sci USA 94:4937-4942.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4937-4942
    • Hanes, J.1    Pluckthun, A.2
  • 9
    • 0032191388 scopus 로고    scopus 로고
    • Recent advances in producing and selecting functional proteins by using cell-free translation
    • Jermutus L, Ryabova LA, Pluckthun A. 1998. Recent advances in producing and selecting functional proteins by using cell-free translation. Curr Opin Biotechnol 9:534-548.
    • (1998) Curr Opin Biotechnol , vol.9 , pp. 534-548
    • Jermutus, L.1    Ryabova, L.A.2    Pluckthun, A.3
  • 10
    • 1542720448 scopus 로고    scopus 로고
    • Mimicking the Escherichia coli cytoplasmic environment activates long-lived and efficient cell-free protein synthesis
    • Jewett MC, Swartz JR. 2004a. Mimicking the Escherichia coli cytoplasmic environment activates long-lived and efficient cell-free protein synthesis. Biotechnol Bioeng 86:19-26.
    • (2004) Biotechnol Bioeng , vol.86 , pp. 19-26
    • Jewett, M.C.1    Swartz, J.R.2
  • 11
    • 1142269592 scopus 로고    scopus 로고
    • Rapid expression and purification of 100 nmol quantities of active protein using cell-free protein synthesis
    • Jewett MC, Swartz JR. 2004b. Rapid expression and purification of 100 nmol quantities of active protein using cell-free protein synthesis. Biotechnol Prog 20:102-109.
    • (2004) Biotechnol Prog , vol.20 , pp. 102-109
    • Jewett, M.C.1    Swartz, J.R.2
  • 12
    • 0442289581 scopus 로고    scopus 로고
    • Prokaryotic systems for in vitro expression
    • Weiner MP, Lu Q, editors. Westborough, MA: Eaton Publishing
    • Jewett MC, Voloshin A, Swartz JR. 2002. Prokaryotic systems for in vitro expression. In: Weiner MP, Lu Q, editors. Gene cloning and expression technologies. Westborough, MA: Eaton Publishing, p 391-411.
    • (2002) Gene Cloning and Expression Technologies , pp. 391-411
    • Jewett, M.C.1    Voloshin, A.2    Swartz, J.R.3
  • 13
    • 0036205202 scopus 로고    scopus 로고
    • Reduction of protein degradation by use of protease-deficient mutants in cell-free protein synthesis system of Escherichia coli
    • Jiang XP, Oohira K, Iwasaki Y, Nakano H, Ichihara S, Yamane T. 2002. Reduction of protein degradation by use of protease-deficient mutants in cell-free protein synthesis system of Escherichia coli. J Biosci Bioeng 93:151-156.
    • (2002) J Biosci Bioeng , vol.93 , pp. 151-156
    • Jiang, X.P.1    Oohira, K.2    Iwasaki, Y.3    Nakano, H.4    Ichihara, S.5    Yamane, T.6
  • 17
    • 0034045838 scopus 로고    scopus 로고
    • Prolonging cell free protein synthesis by selective reagent additions
    • Kim DM, Swartz JR. 2000a. Prolonging cell free protein synthesis by selective reagent additions. Biotechnol Prog 16:385-390.
    • (2000) Biotechnol Prog , vol.16 , pp. 385-390
    • Kim, D.M.1    Swartz, J.R.2
  • 18
    • 0033733369 scopus 로고    scopus 로고
    • Oxalate improves protein synthesis by enhancing ATP supply in cell-free system derived from Escherichia coli
    • Kim DM, Swartz JR. 2000b. Oxalate improves protein synthesis by enhancing ATP supply in cell-free system derived from Escherichia coli. Biotechnol Lett 22:1537-1542.
    • (2000) Biotechnol Lett , vol.22 , pp. 1537-1542
    • Kim, D.M.1    Swartz, J.R.2
  • 19
    • 0035921172 scopus 로고    scopus 로고
    • Regeneration of ATP from glycolytic intermediates for cell-free protein synthesis
    • Kim DM, Swartz JR. 2001. Regeneration of ATP from glycolytic intermediates for cell-free protein synthesis. Biotechnol Bioeng 74:309-316.
    • (2001) Biotechnol Bioeng , vol.74 , pp. 309-316
    • Kim, D.M.1    Swartz, J.R.2
  • 20
    • 0034681011 scopus 로고    scopus 로고
    • Expression-independent consumption of substrates in cell-free expression system from Escherichia coli
    • Kim RG, Choi CY. 2000. Expression-independent consumption of substrates in cell-free expression system from Escherichia coli. J Biotechnol 84:27-32.
    • (2000) J Biotechnol , vol.84 , pp. 27-32
    • Kim, R.G.1    Choi, C.Y.2
  • 21
    • 0001337698 scopus 로고
    • Purification and crystallization of the alkaline phosphatase of Escherichia coli
    • Malamy MH, Horecker BL. 1964. Purification and crystallization of the alkaline phosphatase of Escherichia coli. Biochem 3:1893-1897.
    • (1964) Biochem , vol.3 , pp. 1893-1897
    • Malamy, M.H.1    Horecker, B.L.2
  • 22
    • 3242686114 scopus 로고    scopus 로고
    • Amino acid stabilization for cell-free protein synthesis by modification of the E. coli genome
    • Michel-Reydellet N, Calhoun KA, Swartz JR. 2004. Amino acid stabilization for cell-free protein synthesis by modification of the E. coli genome. Metabol Eng (in press).
    • (2004) Metabol Eng
    • Michel-Reydellet, N.1    Calhoun, K.A.2    Swartz, J.R.3
  • 23
    • 0034302304 scopus 로고    scopus 로고
    • Single-step single-molecule PCR of DNA with a homo-priming sequence using a single primer and hot-startable DNA polymerase
    • Nakano H, Kobayashi K, Ohuchi S, Sekiguchi S, Yamane T. 2000. Single-step single-molecule PCR of DNA with a homo-priming sequence using a single primer and hot-startable DNA polymerase. J Biosci Bioeng 90:456-458.
    • (2000) J Biosci Bioeng , vol.90 , pp. 456-458
    • Nakano, H.1    Kobayashi, K.2    Ohuchi, S.3    Sekiguchi, S.4    Yamane, T.5
  • 24
    • 0035523362 scopus 로고    scopus 로고
    • Combined automated PCR cloning, in vitro transcription/translation and two-dimensional electrophoresis for bacterial proteome analysis
    • Norais N, Nogarotto R, Iacobini ET, Garaguso I, Grifantini R, Galli G, Grandi G. 2001. Combined automated PCR cloning, in vitro transcription/ translation and two-dimensional electrophoresis for bacterial proteome analysis. Proteomics 1:1378-1389.
    • (2001) Proteomics , vol.1 , pp. 1378-1389
    • Norais, N.1    Nogarotto, R.2    Iacobini, E.T.3    Garaguso, I.4    Grifantini, R.5    Galli, G.6    Grandi, G.7
  • 25
    • 0024968835 scopus 로고
    • A general method of site-specific incorporation of unnatural amino acids into proteins
    • Noren CJ, Anthony-Cahill SJ, Griffith MC, Schultz PG. 1989. A general method of site-specific incorporation of unnatural amino acids into proteins. Science 94:182-188.
    • (1989) Science , vol.94 , pp. 182-188
    • Noren, C.J.1    Anthony-Cahill, S.J.2    Griffith, M.C.3    Schultz, P.G.4
  • 26
    • 0001095284 scopus 로고    scopus 로고
    • Sources of nitrogen and their utilization
    • Neidhardt FC, Curtiss R III, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE, editors. Washington, DC: ASM Press
    • Reitzer LJ. 1996. Sources of nitrogen and their utilization. In: Neidhardt FC, Curtiss R III, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE, editors. Escherichia coli and Salmonella: cellular and molecular biology. 2nd edition. Washington, DC: ASM Press, p 380-390.
    • (1996) Escherichia coli and Salmonella: Cellular and Molecular Biology. 2nd Edition , pp. 380-390
    • Reitzer, L.J.1
  • 29
    • 0037069324 scopus 로고    scopus 로고
    • A cell-free protein synthesis system for high-throughput proteomics
    • Sawasaki T, Ogasawara T, Morishita R, Endo Y. 2002. A cell-free protein synthesis system for high-throughput proteomics. Proc Natl Acad Sci USA 99:14652-14657.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14652-14657
    • Sawasaki, T.1    Ogasawara, T.2    Morishita, R.3    Endo, Y.4
  • 30
    • 0027414463 scopus 로고
    • Sequencing and characterization of the sdaB gene from Escherichia coli K-12
    • Shao ZQ, Newman EB. 1993. Sequencing and characterization of the sdaB gene from Escherichia coli K-12. Eur J Biochem 212:777-784.
    • (1993) Eur J Biochem , vol.212 , pp. 777-784
    • Shao, Z.Q.1    Newman, E.B.2
  • 32
    • 0024297305 scopus 로고
    • A continuous cell-free translation system capable of producing polypeptides in high yield
    • Spirin AS, Baranov VI, Ryabova LA, Ovodov SY, Alakhov YB. 1988. A continuous cell-free translation system capable of producing polypeptides in high yield. Science 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
  • 33
    • 0024730743 scopus 로고
    • L-Serine degradation in Escherichia coli K-12: Cloning and sequencing of the sdaA gene
    • Su HS, Lang BF, Newman EB. 1989. L-Serine degradation in Escherichia coli K-12: cloning and sequencing of the sdaA gene. J Bacteriol 171:5095-5102.
    • (1989) J Bacteriol , vol.171 , pp. 5095-5102
    • Su, H.S.1    Lang, B.F.2    Newman, E.B.3
  • 34
    • 0037029135 scopus 로고    scopus 로고
    • Ribosome display for selection of active dihydrofolate reductase mutants using immobilized methotrexate on agarose beads
    • Takahashi F, Ebihara T, Mie M, Yanagida Y, Endo Y, Kobatake E, Aizawa M. 2002. Ribosome display for selection of active dihydrofolate reductase mutants using immobilized methotrexate on agarose beads. FEBS Lett 514:106-110.
    • (2002) FEBS Lett , vol.514 , pp. 106-110
    • Takahashi, F.1    Ebihara, T.2    Mie, M.3    Yanagida, Y.4    Endo, Y.5    Kobatake, E.6    Aizawa, M.7
  • 35
    • 0026729643 scopus 로고
    • 5′-Nucleotidase: Molecular structure and functional aspects
    • Zimmermann H. 1992. 5′-Nucleotidase: molecular structure and functional aspects. Biochem J 285:345-365.
    • (1992) Biochem J , vol.285 , pp. 345-365
    • Zimmermann, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.