메뉴 건너뛰기




Volumn 46, Issue 2, 2006, Pages 348-357

An efficient mammalian cell-free translation system supplemented with translation factors

Author keywords

Cell free; Eukaryotic translation initiation factor; HeLa

Indexed keywords

CAPPED RNA; INITIATION FACTOR; RECOMBINANT PROTEIN;

EID: 33645395535     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2005.09.021     Document Type: Article
Times cited : (101)

References (40)
  • 4
    • 0023878562 scopus 로고
    • The catalytic mechanism of guanine nucleotide exchange factor action and competitive inhibition by phosphorylated eukaryotic initiation factor 2
    • A.G. Rowlands, R. Panniers, and E.C. Henshaw The catalytic mechanism of guanine nucleotide exchange factor action and competitive inhibition by phosphorylated eukaryotic initiation factor 2 J. Biol. Chem. 263 1988 5526 5533
    • (1988) J. Biol. Chem. , vol.263 , pp. 5526-5533
    • Rowlands, A.G.1    Panniers, R.2    Henshaw, E.C.3
  • 5
    • 0036437307 scopus 로고    scopus 로고
    • Transcriptional and translational control in the Mammalian unfolded protein response
    • H.P. Harding, M. Calfon, F. Urano, I. Novoa, and D. Ron Transcriptional and translational control in the Mammalian unfolded protein response Annu. Rev. Cell Dev. Biol. 18 2002 575 599
    • (2002) Annu. Rev. Cell Dev. Biol. , vol.18 , pp. 575-599
    • Harding, H.P.1    Calfon, M.2    Urano, F.3    Novoa, I.4    Ron, D.5
  • 6
    • 1542316306 scopus 로고    scopus 로고
    • Regulation of mRNA translation by protein folding in the endoplasmic reticulum
    • R.J. Kaufman Regulation of mRNA translation by protein folding in the endoplasmic reticulum Trends Biochem. Sci. 29 2004 152 158
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 152-158
    • Kaufman, R.J.1
  • 7
    • 0028034493 scopus 로고
    • Cap-dependent and cap-independent translation by internal initiation of mRNAs in cell extracts prepared from Saccharomyces cerevisiae
    • N. Iizuka, L. Najita, A. Franzusoff, and P. Sarnow Cap-dependent and cap-independent translation by internal initiation of mRNAs in cell extracts prepared from Saccharomyces cerevisiae Mol. Cell Biol. 14 1994 7322 7330
    • (1994) Mol. Cell Biol. , vol.14 , pp. 7322-7330
    • Iizuka, N.1    Najita, L.2    Franzusoff, A.3    Sarnow, P.4
  • 8
    • 0034543678 scopus 로고    scopus 로고
    • Picornavirus IRESes and the poly(A) tail jointly promote cap-independent translation in a mammalian cell-free system
    • G. Bergamini, T. Preiss, and M.W. Hentze Picornavirus IRESes and the poly(A) tail jointly promote cap-independent translation in a mammalian cell-free system RNA 6 2000 1781 1790
    • (2000) RNA , vol.6 , pp. 1781-1790
    • Bergamini, G.1    Preiss, T.2    Hentze, M.W.3
  • 9
    • 0035674431 scopus 로고    scopus 로고
    • Poly(A)-binding protein interaction with elF4G stimulates picornavirus IRES-dependent translation
    • Y.V. Svitkin, H. Imataka, K. Khaleghpour, A. Kahvejian, H.D. Liebig, and N. Sonenberg Poly(A)-binding protein interaction with elF4G stimulates picornavirus IRES-dependent translation RNA 7 2001 1743 1752
    • (2001) RNA , vol.7 , pp. 1743-1752
    • Svitkin, Y.V.1    Imataka, H.2    Khaleghpour, K.3    Kahvejian, A.4    Liebig, H.D.5    Sonenberg, N.6
  • 10
    • 0033229825 scopus 로고    scopus 로고
    • Translational control of dosage compensation in Drosophila by sex-lethal: Cooperative silencing via the 5′ and 3′ UTRs of msl-2 mRNA is independent of the poly(A) tail
    • F. Gebauer, D.F. Corona, T. Preiss, P.B. Becker, and M.W. Hentze Translational control of dosage compensation in Drosophila by sex-lethal: cooperative silencing via the 5′ and 3′ UTRs of msl-2 mRNA is independent of the poly(A) tail EMBO J. 18 1999 6146 6154
    • (1999) EMBO J. , vol.18 , pp. 6146-6154
    • Gebauer, F.1    Corona, D.F.2    Preiss, T.3    Becker, P.B.4    Hentze, M.W.5
  • 11
  • 12
    • 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
    • K. Madin, T. Sawasaki, T. Ogasawara, and Y. Endo 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 2000 559 564
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 559-564
    • Madin, K.1    Sawasaki, T.2    Ogasawara, T.3    Endo, Y.4
  • 13
    • 23244446620 scopus 로고    scopus 로고
    • Quantitative polysome analysis identifies limitations in bacterial cell-free protein synthesis
    • K.A. Underwood, J.R. Swartz, and J.D. Puglisi Quantitative polysome analysis identifies limitations in bacterial cell-free protein synthesis Biotechnol. Bioeng. 91 2005 425 435
    • (2005) Biotechnol. Bioeng. , vol.91 , pp. 425-435
    • Underwood, K.A.1    Swartz, J.R.2    Puglisi, J.D.3
  • 15
    • 0030454053 scopus 로고    scopus 로고
    • General RNA binding proteins render translation cap dependent
    • Y.V. Svitkin, L.P. Ovchinnikov, G. Dreyfuss, and N. Sonenberg General RNA binding proteins render translation cap dependent EMBO J. 15 1996 7147 7155
    • (1996) EMBO J. , vol.15 , pp. 7147-7155
    • Svitkin, Y.V.1    Ovchinnikov, L.P.2    Dreyfuss, G.3    Sonenberg, N.4
  • 16
    • 0032535452 scopus 로고    scopus 로고
    • A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation
    • H. Imataka, A. Gradi, and N. Sonenberg A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation EMBO J. 17 1998 7480 7489
    • (1998) EMBO J. , vol.17 , pp. 7480-7489
    • Imataka, H.1    Gradi, A.2    Sonenberg, N.3
  • 17
    • 0033957406 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 4E (eIF4E) binding site and the middle one-third of eIF4GI constitute the core domain for cap-dependent translation, and the C-terminal one-third functions as a modulatory region
    • S. Morino, H. Imataka, Y.V. Svitkin, T.V. Pestova, and N. Sonenberg Eukaryotic translation initiation factor 4E (eIF4E) binding site and the middle one-third of eIF4GI constitute the core domain for cap-dependent translation, and the C-terminal one-third functions as a modulatory region Mol. Cell Biol. 20 2000 468 477
    • (2000) Mol. Cell Biol. , vol.20 , pp. 468-477
    • Morino, S.1    Imataka, H.2    Svitkin, Y.V.3    Pestova, T.V.4    Sonenberg, N.5
  • 18
    • 0031039645 scopus 로고    scopus 로고
    • A new translational regulator with homology to eukaryotic translation initiation factor 4G
    • H. Imataka, H.S. Olsen, and N. Sonenberg A new translational regulator with homology to eukaryotic translation initiation factor 4G EMBO J. 16 1997 817 825
    • (1997) EMBO J. , vol.16 , pp. 817-825
    • Imataka, H.1    Olsen, H.S.2    Sonenberg, N.3
  • 20
    • 0026680746 scopus 로고
    • Mutational analysis of a DEAD box RNA helicase: The mammalian translation initiation factor eIF-4A
    • A. Pause, and N. Sonenberg Mutational analysis of a DEAD box RNA helicase: the mammalian translation initiation factor eIF-4A EMBO J. 11 1992 2643 2654
    • (1992) EMBO J. , vol.11 , pp. 2643-2654
    • Pause, A.1    Sonenberg, N.2
  • 21
    • 0018403060 scopus 로고
    • Purification of seven protein synthesis initiation factors from Krebs II ascites cells
    • H. Trachsel, B. Erni, M.H. Schreier, L. Braun, and T. Staehelin Purification of seven protein synthesis initiation factors from Krebs II ascites cells Biochim. Biophys. Acta 561 1979 484 490
    • (1979) Biochim. Biophys. Acta , vol.561 , pp. 484-490
    • Trachsel, H.1    Erni, B.2    Schreier, M.H.3    Braun, L.4    Staehelin, T.5
  • 22
    • 2142760951 scopus 로고    scopus 로고
    • A poly(A) tail-responsive in vitro system for cap- or IRES-driven translation from HeLa cells
    • C. Thoma, A. Ostareck-Lederer, and M.W. Hentze A poly(A) tail-responsive in vitro system for cap- or IRES-driven translation from HeLa cells Methods Mol. Biol. 257 2004 171 180
    • (2004) Methods Mol. Biol. , vol.257 , pp. 171-180
    • Thoma, C.1    Ostareck-Lederer, A.2    Hentze, M.W.3
  • 23
    • 0031026161 scopus 로고    scopus 로고
    • The poly(A) tail inhibits the assembly of a 3′-to-5′ exonuclease in an in vitro RNA stability system
    • L.P. Ford, P.S. Bagga, and J. Wilusz The poly(A) tail inhibits the assembly of a 3′-to-5′ exonuclease in an in vitro RNA stability system Mol. Cell Biol. 17 1997 398 406
    • (1997) Mol. Cell Biol. , vol.17 , pp. 398-406
    • Ford, L.P.1    Bagga, P.S.2    Wilusz, J.3
  • 24
    • 0036428702 scopus 로고    scopus 로고
    • Intracellular translation initiation factor levels in Saccharomyces cerevisiae and their role in cap-complex function
    • T. von der Haar, and J.E. McCarthy Intracellular translation initiation factor levels in Saccharomyces cerevisiae and their role in cap-complex function Mol. Microbiol. 46 2002 531 544
    • (2002) Mol. Microbiol. , vol.46 , pp. 531-544
    • Von Der Haar, T.1    McCarthy, J.E.2
  • 25
    • 0023124676 scopus 로고
    • Regulated phosphorylation and low abundance of HeLa cell initiation factor eIF-4F suggest a role in translational control. Heat shock effects on eIF-4F
    • R. Duncan, S.C. Milburn, and J.W. Hershey Regulated phosphorylation and low abundance of HeLa cell initiation factor eIF-4F suggest a role in translational control. Heat shock effects on eIF-4F J. Biol. Chem. 262 1987 380 388
    • (1987) J. Biol. Chem. , vol.262 , pp. 380-388
    • Duncan, R.1    Milburn, S.C.2    Hershey, J.W.3
  • 26
    • 0030009739 scopus 로고    scopus 로고
    • A reevaluation of the cap-binding protein, eIF4E, as a rate-limiting factor for initiation of translation in reticulocyte lysate
    • M. Rau, T. Ohlmann, S.J. Morley, and V.M. Pain A reevaluation of the cap-binding protein, eIF4E, as a rate-limiting factor for initiation of translation in reticulocyte lysate J. Biol. Chem. 271 1996 8983 8990
    • (1996) J. Biol. Chem. , vol.271 , pp. 8983-8990
    • Rau, M.1    Ohlmann, T.2    Morley, S.J.3    Pain, V.M.4
  • 27
    • 0028034233 scopus 로고
    • Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function
    • A. Pause, G.J. Belsham, A.C. Gingras, O. Donze, T.A. Lin, J.C. Lawrence Jr., and N. Sonenberg Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function Nature 371 1994 762 767
    • (1994) Nature , vol.371 , pp. 762-767
    • Pause, A.1    Belsham, G.J.2    Gingras, A.C.3    Donze, O.4    Lin, T.A.5    Lawrence Jr., J.C.6    Sonenberg, N.7
  • 28
    • 0024842214 scopus 로고
    • Gene expression in a cell-free system on the preparative scale
    • V.I. Baranov, I. Morozov, S.A. Ortlepp, and A.S. Spirin Gene expression in a cell-free system on the preparative scale Gene 84 1989 463 466
    • (1989) Gene , vol.84 , pp. 463-466
    • Baranov, V.I.1    Morozov, I.2    Ortlepp, S.A.3    Spirin, A.S.4
  • 29
    • 0032519585 scopus 로고    scopus 로고
    • EIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange
    • G.D. Pavitt, K.V. Ramaiah, S.R. Kimball, and A.G. Hinnebusch eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange Genes Dev. 12 1998 514 526
    • (1998) Genes Dev. , vol.12 , pp. 514-526
    • Pavitt, G.D.1    Ramaiah, K.V.2    Kimball, S.R.3    Hinnebusch, A.G.4
  • 30
    • 0029956389 scopus 로고    scopus 로고
    • Canonical eukaryotic initiation factors determine initiation of translation by internal ribosomal entry
    • T.V. Pestova, C.U. Hellen, and I.N. Shatsky Canonical eukaryotic initiation factors determine initiation of translation by internal ribosomal entry Mol. Cell Biol. 16 1996 6859 6869
    • (1996) Mol. Cell Biol. , vol.16 , pp. 6859-6869
    • Pestova, T.V.1    Hellen, C.U.2    Shatsky, I.N.3
  • 31
    • 0032572776 scopus 로고    scopus 로고
    • Eukaryotic ribosomes require initiation factors 1 and 1A to locate initiation codons
    • T.V. Pestova, S.I. Borukhov, and C.U. Hellen Eukaryotic ribosomes require initiation factors 1 and 1A to locate initiation codons Nature 394 1998 854 859
    • (1998) Nature , vol.394 , pp. 854-859
    • Pestova, T.V.1    Borukhov, S.I.2    Hellen, C.U.3
  • 33
    • 0028203337 scopus 로고
    • Use of monoclonal antibodies to study the structure and function of eukaryotic protein synthesis initiation factor eIF-2B
    • S. Oldfield, B.L. Jones, D. Tanton, and C.G. Proud Use of monoclonal antibodies to study the structure and function of eukaryotic protein synthesis initiation factor eIF-2B Eur. J. Biochem. 221 1994 399 410
    • (1994) Eur. J. Biochem. , vol.221 , pp. 399-410
    • Oldfield, S.1    Jones, B.L.2    Tanton, D.3    Proud, C.G.4
  • 34
    • 0030728936 scopus 로고    scopus 로고
    • Cocrystal structure of the messenger RNA 5′ cap-binding protein (eIF4E) bound to 7-methyl-GDP
    • J. Marcotrigiano, A.C. Gingras, N. Sonenberg, and S.K. Burley Cocrystal structure of the messenger RNA 5′ cap-binding protein (eIF4E) bound to 7-methyl-GDP Cell 89 1997 951 961
    • (1997) Cell , vol.89 , pp. 951-961
    • Marcotrigiano, J.1    Gingras, A.C.2    Sonenberg, N.3    Burley, S.K.4
  • 35
    • 0025314596 scopus 로고
    • Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5′ cap
    • A. Lazaris-Karatzas, K.S. Montine, and N. Sonenberg Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5′ cap Nature 345 1990 544 547
    • (1990) Nature , vol.345 , pp. 544-547
    • Lazaris-Karatzas, A.1    Montine, K.S.2    Sonenberg, N.3
  • 37
    • 2442648845 scopus 로고    scopus 로고
    • The translation factor eIF-4E promotes tumor formation and cooperates with c-Myc in lymphomagenesis
    • D. Ruggero, L. Montanaro, L. Ma, W. Xu, P. Londei, C. Cordon-Cardo, and P.P. Pandolfi The translation factor eIF-4E promotes tumor formation and cooperates with c-Myc in lymphomagenesis Nat. Med. 10 2004 484 486
    • (2004) Nat. Med. , vol.10 , pp. 484-486
    • Ruggero, D.1    Montanaro, L.2    Ma, L.3    Xu, W.4    Londei, P.5    Cordon-Cardo, C.6    Pandolfi, P.P.7
  • 38
    • 0030443685 scopus 로고    scopus 로고
    • The eIF4E-binding proteins 1 and 2 are negative regulators of cell growth
    • D. Rousseau, A.C. Gingras, A. Pause, and N. Sonenberg The eIF4E-binding proteins 1 and 2 are negative regulators of cell growth Oncogene 13 1996 2415 2420
    • (1996) Oncogene , vol.13 , pp. 2415-2420
    • Rousseau, D.1    Gingras, A.C.2    Pause, A.3    Sonenberg, N.4
  • 39
    • 0017351102 scopus 로고
    • 5′-Terminal structure and mRNA stability
    • Y. Furuichi, A. LaFiandra, and A.J. Shatkin 5′-Terminal structure and mRNA stability Nature 266 1977 235 239
    • (1977) Nature , vol.266 , pp. 235-239
    • Furuichi, Y.1    Lafiandra, A.2    Shatkin, A.J.3
  • 40
    • 0742288008 scopus 로고    scopus 로고
    • The enzymes and control of eukaryotic mRNA turnover
    • R. Parker, and H. Song The enzymes and control of eukaryotic mRNA turnover Nat. Struct. Mol. Biol. 11 2004 121 127
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 121-127
    • Parker, R.1    Song, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.