메뉴 건너뛰기




Volumn 11, Issue 3, 2010, Pages 279-284

Development of an insect cell-free system

Author keywords

5 UTR; Cell free protein synthesis; Freeze thawing; Insect cell; MALDI TOF MS; Post translational modification; Rabbit reticulocyte

Indexed keywords

CELL EXTRACT; POLYHEDRIN; SCATTER FACTOR RECEPTOR;

EID: 77950897649     PISSN: 13892010     EISSN: 18734316     Source Type: Journal    
DOI: 10.2174/138920110791111997     Document Type: Review
Times cited : (8)

References (36)
  • 2
    • 33846856245 scopus 로고    scopus 로고
    • Detection of co- and posttranslational protein N-myristoylation by metabolic labeling in an insect cell-free protein synthesis system
    • DOI 10.1016/j.ab.2006.12.030, PII S0003269706009249
    • Sakurai, N.; Moriya, K.; Suzuki, T.; Sofuku, K.; Mochiki, H.; Nishimura, O.; Utsumi, T. Detection of co- and posttranslational protein N-myristoylation by metabolic labeling in an insect cell-free protein synthesis system. Anal. Biochem., 2007, 362(2), 236-244. (Pubitemid 46227321)
    • (2007) Analytical Biochemistry , vol.362 , Issue.2 , pp. 236-244
    • Sakurai, N.1    Moriya, K.2    Suzuki, T.3    Sofuku, K.4    Mochiki, H.5    Nishimura, O.6    Utsumi, T.7
  • 3
    • 33846508661 scopus 로고    scopus 로고
    • Design of carrier tRNAs and selection of four-base codons for efficient incorporation of various nonnatural amino acids into proteins in Spodoptera frugiperda 21 (Sf21) insect cell-free translation system
    • DOI 10.1263/jbb.102.511, PII S138917230770004X
    • Taki, M.; Tokuda, Y.; Ohtsuki, T.; Sisido, M. Design of carrier tRNAs and selection of four-base codons for efficient incorporation of various nonnatural amino acids into proteins in Spodoptera frugiperda 21 (Sf21) insect cell-free translation system. J. Biosci. Bioeng., 2006, 102(6), 511-517. (Pubitemid 46164890)
    • (2006) Journal of Bioscience and Bioengineering , vol.102 , Issue.6 , pp. 511-517
    • Taki, M.1    Tokuda, Y.2    Ohtsuki, T.3    Sisido, M.4
  • 4
    • 0020645081 scopus 로고
    • Prokaryotic coupled transcription-translation
    • Chen, H.-Z.; Zubay, G. Prokaryotic coupled transcription-translation. Methods Enzymol., 1983, 101, 674-690.
    • (1983) Methods Enzymol. , vol.101 , pp. 674-690
    • Chen, H.-Z.1    Zubay, G.2
  • 5
    • 0020997221 scopus 로고
    • Cell-free translation of messenger RNA in a wheat germ system
    • Erickson, A. H.; Blobel, G. Cell-free translation of messenger RNA in a wheat germ system. Methods Enzymol., 1983, 96, 38-50.
    • (1983) Methods Enzymol. , vol.96 , pp. 38-50
    • Erickson, A.H.1    Blobel, G.2
  • 6
    • 0018422804 scopus 로고
    • The analysis of intermediary reactions involved in protein synthesis, in a cell free extract of Saccharomyces cerevisiae that translates natural messenger ribonucleic acid
    • Gaisor, E.; Herrera, F.; Sadnik, I.; McLaughlin, C. S.; Moldave, K. The preparation and characterization of a cell-free system from Saccharomyces cerevisiae that translates natural messenger ribonucleic acid. J. Biol. Chem., 1979, 254(10), 3965-3969. (Pubitemid 9178811)
    • (1979) Journal of Biological Chemistry , vol.254 , Issue.10 , pp. 3970-3976
    • Gasior, E.1    Herrera, F.2    McLaughlin, C.S.3    Moldave, K.4
  • 7
    • 0024307032 scopus 로고
    • Cell-free translation in lysates from Spodoptera frugiperda (Lepidoptera: Noctuidae) cells
    • Swerdel, M. R.; Fallon, A. M. Cell-free translation in lysates from Spodoptera frugiperda (Lepidoptera: Noctuidae) cells. Comp. Biochem. Physiol., 1989, 93(4), 803-806.
    • (1989) Comp. Biochem. Physiol. , vol.93 , Issue.4 , pp. 803-806
    • Swerdel, M.R.1    Fallon, A.M.2
  • 8
    • 0021004695 scopus 로고
    • Preparation and use of nuclease-treated rabbit reticulocyte lysates for translation of eukaryotic messenger RNA
    • Jackson, R. J.; Hunt T. Preparation and use of nuclease-treated rabbit reticulocyte lysates for translation of eukaryotic messenger RNA. Methods Enzymol., 1983, 96, 50-74.
    • (1983) Methods Enzymol. , vol.96 , pp. 50-74
    • Jackson, R.J.1    Hunt, T.2
  • 9
    • 0025787535 scopus 로고
    • A continuous cell-free protein synthesis system for coupled transcription-translation
    • Kigawa, T.; Yokoyama, S. A continuous cell-free protein synthesis system for coupled transcription-translation. J. Biochem., 1991, 110(2), 166-168.
    • (1991) J. Biochem. , vol.110 , Issue.2 , pp. 166-168
    • Kigawa, T.1    Yokoyama, S.2
  • 10
    • 0037029131 scopus 로고    scopus 로고
    • A bilayer cell-free protein synthesis system for high-throughput screening of gene products
    • DOI 10.1016/S0014-5793(02)02329-3, PII S0014579302023293
    • Sawasaki, T.; Hasegawa, Y.; Tsuchimochi, M.; Kamura, N.; Ogasawara, T.; Kuroita, T.; Endo, Y. A bilayer cell-free protein synthesis system for high-throughput screening of gene products. FEBS Lett., 2002, 514(1), 102-105. (Pubitemid 34251251)
    • (2002) FEBS Letters , vol.514 , Issue.1 , pp. 102-105
    • Sawasaki, T.1    Hasegawa, Y.2    Tsuchimochi, M.3    Kamura, N.4    Ogasawara, T.5    Kuroita, T.6    Endo, Y.7
  • 11
    • 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(4882), 1162-1164.
    • (1988) Science , vol.242 , Issue.4882 , pp. 1162-1164
    • Spirin, A.S.1    Baranov, V.I.2    Ryabova, L.A.3    Ovodov, S.Y.4    Alakhov, Y.B.5
  • 12
    • 0141755381 scopus 로고    scopus 로고
    • Phosphorylation of serine 13 is required for the proper function of the Hsp90 cochaperone, Cdc37
    • Shao, J.; Prince, T.; Hartson, S. D.; Matts, R. L. Phosphorylation of serine 13 is required for the proper function of the Hsp90 cochaperone, Cdc37. J. Biol. Chem., 2003, 278(40), 38117-38120.
    • (2003) J. Biol. Chem. , vol.278 , Issue.40 , pp. 38117-38120
    • Shao, J.1    Prince, T.2    Hartson, S.D.3    Matts, R.L.4
  • 13
    • 0032855355 scopus 로고    scopus 로고
    • Multi-ubiquitination of a nascent membrane protein produced in a rabbit reticulocyte lysate
    • Iwamuro, S.; Saeki, M.; Kato, S. Multi-ubiquitination of a nascent membrane protein produced in a rabbit reticulocyte lysate. J. Biochem., 1999, 126(1), 48-53. (Pubitemid 29355392)
    • (1999) Journal of Biochemistry , vol.126 , Issue.1 , pp. 48-53
    • Iwamuro, S.1    Saeki, M.2    Kato, S.3
  • 14
    • 0025944103 scopus 로고
    • Posttranslational modification of Ha-ras p21 by farnesyl versus geranylgeranyl isoprenoids is determined by the COOH-terminal amino acid
    • Kinsella, B. T.; Erdman, R. A.; Maltese, W. A. Posttranslational modification of Ha-ras p21 by farnesyl versus geranylgeranyl isoprenoids is determined by the COOH-terminal amino acid. Proc. Natl. Acad. Sci. USA, 1991, 88(20), 8934-8938.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , Issue.20 , pp. 8934-8938
    • Kinsella, B.T.1    Erdman, R.A.2    Maltese, W.A.3
  • 15
    • 0035971107 scopus 로고    scopus 로고
    • Amino Acid Residue Penultimate to the Amino-terminal Gly Residue Strongly Affects Two Cotranslational Protein Modifications, N-Myristoylation and N-Acetylation
    • DOI 10.1074/jbc.M006134200
    • Utsumi, T.; Sato, M.; Nakano, K.; Takemura, D.; Iwata, H.; Ishisaka, R. Amino acid residue penultimate to the amino-terminal gly residue strongly affects two cotranslational protein modifications, N-myristoylation and N-acetylation. J. Biol. Chem., 2001, 276(13), 10505-10513. (Pubitemid 37391966)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.13 , pp. 10505-10513
    • Utsumi, T.1    Sato, M.2    Nakano, K.3    Takemura, D.4    Iwata, H.5    Ishisaka, R.6
  • 16
    • 0031035737 scopus 로고    scopus 로고
    • Membrane insertion, glycosylation, and oligomerization of inositol trisphosphate receptors in a cell-free translation system
    • Joseph, S. K.; Boehning, D.; Pierson, S.; Nicchitta, C. V. Membrane insertion, glycosylation, and oligomerization of inositol trisphosphate receptors in a cell-free translation system. J. Biol. Chem., 1997, 272(3), 1579-1588.
    • (1997) J. Biol. Chem. , vol.272 , Issue.3 , pp. 1579-1588
    • Joseph, S.K.1    Boehning, D.2    Pierson, S.3    Nicchitta, C.V.4
  • 17
    • 0032818715 scopus 로고    scopus 로고
    • A part of the transmembrane domain of pro-TNF can function as a cleavable signal sequence that generates a biologically active secretory form of TNF
    • Ishisaka, R.; Sato, N.; Tanaka, K.; Takeshige, T.; Iwata, H.; Klostergaard, J.; Utsumi, T. A part of the transmembrane domain of pro-TNF can function as a cleavable signal sequence that generates a biologically active secretory form of TNF. J. Biochem., 1999, 126(2), 413-420. (Pubitemid 29408213)
    • (1999) Journal of Biochemistry , vol.126 , Issue.2 , pp. 413-420
    • Ishisaka, R.1    Sato, N.2    Tanaka, K.3    Takeshige, T.4    Iwata, H.5    Klostergaard, J.6    Utsumi, T.7
  • 20
    • 0141650681 scopus 로고    scopus 로고
    • Molecular cloning, expression, purification, and characterization of soluble full-length, human interleukin-3 with a baculovirus-insect cell expression system
    • DOI 10.1016/S1046-5928(03)00138-4
    • Ding, H.; Griesel, C.; Nimtz, M.; Conradt, H. S.; Weich, H. A.; Jager, V. Molecular cloning, expression, purification, and characterization of soluble full-length, human interleukin-3 with a baculovirus- insect cell expression system. Protein Expr. Purif., 2003, 31(1), 34-41. (Pubitemid 37207639)
    • (2003) Protein Expression and Purification , vol.31 , Issue.1 , pp. 34-41
    • Ding, H.1    Griesel, C.2    Nimtz, M.3    Conradt, H.S.4    Weich, H.A.5    Jager, V.6
  • 21
    • 0026918457 scopus 로고
    • Screening of insect cell lines for the production of recombinant proteins and infectious virus in the baculovirus expression system
    • Wickham, T. J.; Davis, T.; Granados, R. R.; Shuler, M. L.; Wood, H. A. Screening of insect cell lines for the production of recombinant proteins and infectious virus in the baculovirus expression system. Biotechnol. Prog., 1992, 8(5), 391-396.
    • (1992) Biotechnol. Prog. , vol.8 , Issue.5 , pp. 391-396
    • Wickham, T.J.1    Davis, T.2    Granados, R.R.3    Shuler, M.L.4    Wood, H.A.5
  • 22
    • 0037220797 scopus 로고    scopus 로고
    • Production of protein kinase C-delta by the baculovirus-insect cell system in serum-supplemented and serum-free media
    • DOI 10.1016/S1389-1723(03)80126-3
    • Yamaji, H.; Hirakawa, D.; Tagai, S.; Fukuda, H. Production of protein kinase C-delta by the baculovirus-insect cell system in serum-supplemented and serum-free media. J. Biosci. Bioeng., 2003, 95(2), 185-187. (Pubitemid 36313200)
    • (2003) Journal of Bioscience and Bioengineering , vol.95 , Issue.2 , pp. 185-187
    • Yamaji, H.1    Hirakawa, D.2    Tagai, S.-I.3    Fukuda, H.4
  • 23
    • 33748374698 scopus 로고    scopus 로고
    • N-terminal protein modifications in an insect cell-free protein synthesis system and their identification by mass spectrometry
    • DOI 10.1002/pmic.200600126
    • Suzuki, T.; Ito, M.; Ezure, T.; Shikata, M.; Ando, E.; Utsumi, T.; Tsunasawa, S.; Nishimura, O. N-Terminal protein modifications in an insect cell-free protein synthesis system and their identification by mass spectrometry. Proteomics, 2006, 6(16), 4486-4495. (Pubitemid 44336966)
    • (2006) Proteomics , vol.6 , Issue.16 , pp. 4486-4495
    • Suzuki, T.1    Ito, M.2    Ezure, T.3    Shikata, M.4    Ando, E.5    Utsumi, T.6    Tsunasawa, S.7    Nishimura, O.8
  • 24
    • 34347407851 scopus 로고    scopus 로고
    • Protein prenylation in an insect cell-free protein synthesis system and identification of products by mass spectrometry
    • DOI 10.1002/pmic.200700237
    • Suzuki, T.; Ito, M.; Ezure, T.; Shikata, M.; Ando, E.; Utsumi, T.; Tsunasawa, S.; Nishimura, O. Protein prenylation in an insect cellfree protein synthesis system and identification of products by mass spectrometry. Proteomics, 2007, 7(12), 1942-1950. (Pubitemid 47020329)
    • (2007) Proteomics , vol.7 , Issue.12 , pp. 1942-1950
    • Suzuki, T.1    Ito, M.2    Ezure, T.3    Shikata, M.4    Ando, E.5    Utsumi, T.6    Tsunasawa, S.7    Nishimura, O.8
  • 25
    • 38049021005 scopus 로고    scopus 로고
    • Expression of proteins containing disulfide bonds in an insect cell-free system and confirmation of their arrangements by MALDI-TOF MS
    • Ezure, T.; Suzuki, T.; Shikata, M.; Ito, M.; Ando, E.; Nishimura, O.; Tsunasawa, S. Expression of proteins containing disulfide bonds in an insect cell-free system and confirmation of their arrangements by MALDI-TOF MS. Proteomics, 2007, 7(24), 4424-4434.
    • (2007) Proteomics , vol.7 , Issue.24 , pp. 4424-4434
    • Ezure, T.1    Suzuki, T.2    Shikata, M.3    Ito, M.4    Ando, E.5    Nishimura, O.6    Tsunasawa, S.7
  • 26
    • 0035014494 scopus 로고    scopus 로고
    • Establishment and characterization of cell-free translation/ glycosylation in insect cell (Spodoptera frugiperda 21) extract prepared with high pressure treatment
    • Tarui, H.; Murata, M.; Tani, I.; Imanishi, S.; Nishikawa, S.; Hara, T. Establishment and characterization of cell-free translation/ glycosylation in insect cell (Spodoptera frugiperda 21) extract prepared with high pressure treatment. Appl. Microbiol. Biotechnol., 2001, 55(4), 446-453.
    • (2001) Appl. Microbiol. Biotechnol. , vol.55 , Issue.4 , pp. 446-453
    • Tarui, H.1    Murata, M.2    Tani, I.3    Imanishi, S.4    Nishikawa, S.5    Hara, T.6
  • 27
    • 0020994721 scopus 로고
    • Preparation of microsomal membranes for cotranslational protein translocation
    • Walter, P.; Blobel, G. Preparation of microsomal membranes for cotranslational protein translocation. Methods Enzymol., 1983, 96, 84-93.
    • (1983) Methods Enzymol. , vol.96 , pp. 84-93
    • Walter, P.1    Blobel, G.2
  • 28
    • 0020981494 scopus 로고
    • Methods for the study of protein translation across the RER membrane using the reticulocyte lysate translation system and canine pancreatic microsomal membranes
    • Scheele, G. Methods for the study of protein translation across the RER membrane using the reticulocyte lysate translation system and canine pancreatic microsomal membranes. Methods Enzymol., 1983, 96, 94-111.
    • (1983) Methods Enzymol. , vol.96 , pp. 94-111
    • Scheele, G.1
  • 29
    • 0030731419 scopus 로고    scopus 로고
    • Starting at the beginning, middle, and end: Translation initiation in eukaryotes
    • Sachs, A. B.; Sarnow, P.; Hentze, M. W. Starting at the beginning, middle, and end: translation initiation in eukaryotes. Cell, 1997, 89(6), 831-838.
    • (1997) Cell , vol.89 , Issue.6 , pp. 831-838
    • Sachs, A.B.1    Sarnow, P.2    Hentze, M.W.3
  • 30
    • 0026331302 scopus 로고
    • Both the 5′ untranslated region and the sequences surrounding the start site contribute to efficient initiation of translation in vitro
    • Falcone, D.; Andrews, D. W. Both the 5′ untranslated region and the sequences surrounding the start site contribute to efficient initiation of translation in vitro. Mol. Cell. Biol., 1991, 11(5), 2656-2664.
    • (1991) Mol. Cell. Biol. , vol.11 , Issue.5 , pp. 2656-2664
    • Falcone, D.1    Andrews, D.W.2
  • 31
    • 0023651443 scopus 로고
    • A comparison of eukaryotic viral 5'-leader sequences as enhancers of mRNA expression in vivo
    • Gallie, D. R.; Sleat, D. E.; Watts, J. W.; Turner, P. C.; Wilson, T. M. A comparison of eukaryotic viral 5'-leader sequences as enhancers of mRNA expression in vivo. Nucleic Acids Res., 1987, 15(21), 3257-3273.
    • (1987) Nucleic Acids Res. , vol.15 , Issue.21 , pp. 3257-3273
    • Gallie, D.R.1    Sleat, D.E.2    Watts, J.W.3    Turner, P.C.4    Wilson, T.M.5
  • 32
    • 0025813516 scopus 로고
    • A strategy for efficient in vitro translation of cDNAs using the rabbit beta-globin leader sequence
    • Annweiler, A.; Hipskind, R. A.; Wirth, T. A strategy for efficient in vitro translation of cDNAs using the rabbit beta-globin leader sequence. Nucleic Acids Res., 1991, 19(13), 3750.
    • (1991) Nucleic Acids Res. , vol.19 , Issue.13 , pp. 3750
    • Annweiler, A.1    Hipskind, R.A.2    Wirth, T.3
  • 33
    • 35448945259 scopus 로고    scopus 로고
    • Construction of homo- And heteropolymers of plant ferritin subunits using an in vitro protein expression system
    • DOI 10.1016/j.pep.2007.07.011, PII S1046592807001908
    • Masuda, T.; Goto, F.; Yoshihara, T.; Ezure, T.; Suzuki, T.; Kobayashi, S.; Shikata, M.; Utsumi, S. Construction of homo- and heteropolymers of plant ferritin subunits using an in vitro protein expression system. Protein Expr. Purif., 2007, 56(2), 237-246. (Pubitemid 47633224)
    • (2007) Protein Expression and Purification , vol.56 , Issue.2 , pp. 237-246
    • Masuda, T.1    Goto, F.2    Yoshihara, T.3    Ezure, T.4    Suzuki, T.5    Kobayashi, S.6    Shikata, M.7    Utsumi, S.8
  • 34
    • 77950904005 scopus 로고    scopus 로고
    • Co-synthesis of human delta-aminolevulinate dehydratase (ALAD) mutants with the wild-type enzyme in cellfree system-critical importance of conformation on enzyme activity
    • Inoue, R.; Akagi, R. Co-synthesis of human delta-aminolevulinate dehydratase (ALAD) mutants with the wild-type enzyme in cellfree system-critical importance of conformation on enzyme activity-. J. Clin. Biochem. Nutr., 2008, 43(3), 143-153.
    • (2008) J. Clin. Biochem. Nutr. , vol.43 , Issue.3 , pp. 143-153
    • Inoue, R.1    Akagi, R.2
  • 35
    • 47949123686 scopus 로고    scopus 로고
    • Expression and chain assembly of human laminin-332 in an insect cell-free translation system
    • Phan, H. P.; Ezure, T.; Ito, M.; Kadowaki, T.; Kitagawa, Y.; Niimi, T. Expression and chain assembly of human laminin-332 in an insect cell-free translation system. Biosci. Biotechnol. Biochem., 2008, 72(7), 1847-1852.
    • (2008) Biosci. Biotechnol. Biochem. , vol.72 , Issue.7 , pp. 1847-1852
    • Phan, H.P.1    Ezure, T.2    Ito, M.3    Kadowaki, T.4    Kitagawa, Y.5    Niimi, T.6
  • 36
    • 56049095074 scopus 로고    scopus 로고
    • Exploration of human ORFeome: High-throughput preparation of ORF clones and efficient characterization of their protein products
    • Nagase, T.; Yamakawa, H.; Tadokoro, S.; Nakajima, D.; Inoue, S.; Yamaguchi, K.; Itokawa, Y.; Kikuno, R. F.; Koga, H.; Ohara, O. Exploration of human ORFeome: high-throughput preparation of ORF clones and efficient characterization of their protein products. DNA Res., 2008, 15(3), 137-149.
    • (2008) DNA Res. , vol.15 , Issue.3 , pp. 137-149
    • Nagase, T.1    Yamakawa, H.2    Tadokoro, S.3    Nakajima, D.4    Inoue, S.5    Yamaguchi, K.6    Itokawa, Y.7    Kikuno, R.F.8    Koga, H.9    Ohara, O.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.