메뉴 건너뛰기




Volumn 17, Issue 24, 1998, Pages 7480-7489

A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation

Author keywords

Eukaryotic translation initiation factor 4G; Poly(A) binding protein; Poly(A) dependent translation; Translation initiation

Indexed keywords

COMPLEMENTARY DNA; INITIATION FACTOR; POLYADENYLIC ACID; RNA BINDING PROTEIN;

EID: 0032535452     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.24.7480     Document Type: Article
Times cited : (479)

References (26)
  • 1
    • 0026457301 scopus 로고
    • Isolation and sequence of the cDNAs encoding the subunits of the isozyme form of wheat protein synthesis initiation factor 4F
    • Allen,M., Metz,A.M., Timmer,R.T, Rhoads,R.E. and Browning,K.S. (1992) Isolation and sequence of the cDNAs encoding the subunits of the isozyme form of wheat protein synthesis initiation factor 4F. J. Biol. Chem., 267, 23232-23236.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23232-23236
    • Allen, M.1    Metz, A.M.2    Timmer, R.T.3    Rhoads, R.E.4    Browning, K.S.5
  • 2
    • 0029811544 scopus 로고    scopus 로고
    • RNA-protein interactions in regulation of picornavirus RNA translation
    • Belsham,G.J. and Sonenberg,N. (1996) RNA-protein interactions in regulation of picornavirus RNA translation. Microbiol. Rev., 60, 499-511.
    • (1996) Microbiol. Rev. , vol.60 , pp. 499-511
    • Belsham, G.J.1    Sonenberg, N.2
  • 3
    • 0025762042 scopus 로고
    • The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities
    • Burd,C.G., Matunis,E.L. and Dreyfuss,G. (1991) The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities. Mol. Cell. Biol., 11, 3419-3424.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3419-3424
    • Burd, C.G.1    Matunis, E.L.2    Dreyfuss, G.3
  • 4
    • 0032473972 scopus 로고    scopus 로고
    • Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation
    • Craig,A.W.B., Haghighat, A., Yu,A.T.K. and Sonenberg,N. (1998) Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation. Nature, 392, 520-523.
    • (1998) Nature , vol.392 , pp. 520-523
    • Craig, A.W.B.1    Haghighat, A.2    Yu, A.T.K.3    Sonenberg, N.4
  • 5
    • 0023124676 scopus 로고
    • Regulated phosphorylation and low abundance of HeLa cell initiation factor eIF-4F suggest a role in translation control: Heat shock effects on eIF4F
    • Duncan,R., Milburn,S.C. and Hershey,J.W.B. (1987) Regulated phosphorylation and low abundance of HeLa cell initiation factor eIF-4F suggest a role in translation control: heat shock effects on eIF4F. J. Biol. Chem., 262, 380-388.
    • (1987) J. Biol. Chem. , vol.262 , pp. 380-388
    • Duncan, R.1    Milburn, S.C.2    Hershey, J.W.B.3
  • 6
    • 0000233999 scopus 로고
    • Eukaryotic transient expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase
    • Fuerst,T.R., Niles,E.G., Studier,F.W. and Moss,B. (1986) Eukaryotic transient expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase. Proc. Natl Acad. Sci. USA, 83, 8122-8126.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 8122-8126
    • Fuerst, T.R.1    Niles, E.G.2    Studier, F.W.3    Moss, B.4
  • 7
    • 0026038913 scopus 로고
    • The cap and poly (A) tail function synergistically to regulate mRNA translational efficiency
    • Gallie,D. (1991) The cap and poly (A) tail function synergistically to regulate mRNA translational efficiency. Genes Dev., 5, 2108-2116.
    • (1991) Genes Dev. , vol.5 , pp. 2108-2116
    • Gallie, D.1
  • 8
    • 0027219266 scopus 로고
    • TIF4631 and TIF4632: Two yeast genes encoding the high-molecular-weight subunits of the cap-binding protein complex (eukaryotic initiation factor 4F) contain an RNA recognition motif-like sequence and carry out an essential function
    • Goyer,C., Altmann,M., Lee,H.S., Blanc,A., Deshmukh,M., Woolford,J.L.,Jr, Trachsel,H. and Sonenberg,N. (1993) TIF4631 and TIF4632: two yeast genes encoding the high-molecular-weight subunits of the cap-binding protein complex (eukaryotic initiation factor 4F) contain an RNA recognition motif-like sequence and carry out an essential function. Mol. Cell. Biol., 13, 4860-4874.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4860-4874
    • Goyer, C.1    Altmann, M.2    Lee, H.S.3    Blanc, A.4    Deshmukh, M.5    Woolford Jr., J.L.6    Trachsel, H.7    Sonenberg, N.8
  • 9
    • 0028340737 scopus 로고
    • The mRNA poly(A)-binding protein: Localization, abundance, and RNA-binding specificity
    • Görlach,M., Burd,C.G. and Dreyfuss,G. (1994) The mRNA poly(A)-binding protein: localization, abundance, and RNA-binding specificity. Exp. Cell Res., 211, 400-407.
    • (1994) Exp. Cell Res. , vol.211 , pp. 400-407
    • Görlach, M.1    Burd, C.G.2    Dreyfuss, G.3
  • 11
    • 0023238720 scopus 로고
    • Human mRNA polyadenylate binding protein: Evolutionary conservation of a nucleic acid binding motif
    • Grange,T., Martins de Sa.C., Oddos,J. and Pictet,R. (1987) Human mRNA polyadenylate binding protein: evolutionary conservation of a nucleic acid binding motif. Nucleic Acids Res., 15, 4771-4787.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 4771-4787
    • Grange, T.1    Martins De Sa, C.2    Oddos, J.3    Pictet, R.4
  • 13
    • 0029861190 scopus 로고    scopus 로고
    • The eIF4G-eIF4E complex is the target for direct cleavage by the rhinovirus 2A proteinase
    • Haghighat,A., Svitkin,Y., Novoa,I., Kuechler,E., Skem,T. and Sonenberg,N. (1996) The eIF4G-eIF4E complex is the target for direct cleavage by the rhinovirus 2A proteinase. J. Virol., 70, 8444-8450.
    • (1996) J. Virol. , vol.70 , pp. 8444-8450
    • Haghighat, A.1    Svitkin, Y.2    Novoa, I.3    Kuechler, E.4    Skem, T.5    Sonenberg, N.6
  • 14
    • 0032053542 scopus 로고    scopus 로고
    • Isolation and characterization of the cDNA and the gene for eukaryotic translation initiation factor 4G from Drosophila melanogaster
    • Hernández,G., Del Mar Castellano,M., Agudo,M. and Sierra,J.M. (1998) Isolation and characterization of the cDNA and the gene for eukaryotic translation initiation factor 4G from Drosophila melanogaster. Eur. J. Biochem., 253, 27-35.
    • (1998) Eur. J. Biochem. , vol.253 , pp. 27-35
    • Hernández, G.1    Del Mar Castellano, M.2    Agudo, M.3    Sierra, J.M.4
  • 15
    • 0030666625 scopus 로고    scopus 로고
    • Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A
    • Imataka,H. and Sonenberg,N. (1997) Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A. Mol. Cell. Biol., 17, 6940-6947.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6940-6947
    • Imataka, H.1    Sonenberg, N.2
  • 16
    • 0031039645 scopus 로고    scopus 로고
    • A new translational regulator with homology to eukaryotic translation initiation factor 4G
    • Imataka,H., Olsen,H.S. and Sonenberg,N. (1997) A new translational regulator with homology to eukaryotic translation initiation factor 4G. EMBO J., 16, 817-825.
    • (1997) EMBO J. , vol.16 , pp. 817-825
    • Imataka, H.1    Olsen, H.S.2    Sonenberg, N.3
  • 17
    • 0002799007 scopus 로고    scopus 로고
    • Poly(A) metabolism and translation: The closed-loop model
    • Hershey,J.W.B., Mathews,M.B. and Sonenberg,N. (eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Jacobson,A. (1996) Poly(A) metabolism and translation: the closed-loop model. In Hershey,J.W.B., Mathews,M.B. and Sonenberg,N. (eds), Translational Control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 451-480.
    • (1996) Translational Control , pp. 451-480
    • Jacobson, A.1
  • 18
    • 0031972645 scopus 로고    scopus 로고
    • RNA recognition motif 2 of yeast Pab1p required for its functional interaction with eukaryotic translation initiation factor 4G
    • Kessler,S.H. and Sachs,A.B. (1998) RNA recognition motif 2 of yeast Pab1p required for its functional interaction with eukaryotic translation initiation factor 4G. Mol. Cell. Biol., 18, 51-57.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 51-57
    • Kessler, S.H.1    Sachs, A.B.2
  • 19
    • 0029117427 scopus 로고
    • Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral proteases: Implications for capdependent and cap-independent translational initiation
    • Lamphear,B., Kirchweger,R., Skem,T. and Rhoads,R. (1995) Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral proteases: implications for capdependent and cap-independent translational initiation. J. Biol. Chem., 270, 21975-21983.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21975-21983
    • Lamphear, B.1    Kirchweger, R.2    Skem, T.3    Rhoads, R.4
  • 20
    • 0030952218 scopus 로고    scopus 로고
    • Translation initiation factors eIF-iso4G and eIF-4B interact with the poly(A)-binding protein and increase its RNA binding activity
    • Le,H., Tanguay,R.L., Balasta,M.L., Wei,C., Browing,K.S., Metz,A.M., Goss,D.J. and Gallie,D.R. (1997) Translation initiation factors eIF-iso4G and eIF-4B interact with the poly(A)-binding protein and increase its RNA binding activity. J. Biol. Chem., 272, 16247-16255.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16247-16255
    • Le, H.1    Tanguay, R.L.2    Balasta, M.L.3    Wei, C.4    Browing, K.S.5    Metz, A.M.6    Goss, D.J.7    Gallie, D.R.8
  • 21
    • 0029166687 scopus 로고
    • The translation initiation factor eIF4E binds to a common motif shared by the translation factor eIF-4γ and the translational repressers 4E-binding proteins
    • Mader,S., Lee,H., Pause,A. and Sonenberg,N. (1995) The translation initiation factor eIF4E binds to a common motif shared by the translation factor eIF-4γ and the translational repressers 4E-binding proteins. Mol. Cell. Biol., 15, 4990-4997.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4990-4997
    • Mader, S.1    Lee, H.2    Pause, A.3    Sonenberg, N.4
  • 22
    • 0002523042 scopus 로고    scopus 로고
    • The pathway and mechanism of eukaryotic protein synthesis
    • Hershey,J.W.B., Mathews,M.B. and Sonenberg,N. (eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Merrick,W.C. and Hershey,J.W.B. (1996) The pathway and mechanism of eukaryotic protein synthesis. In Hershey,J.W.B., Mathews,M.B. and Sonenberg,N. (eds), Translational Control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 31-70.
    • (1996) Translational Control , pp. 31-70
    • Merrick, W.C.1    Hershey, J.W.B.2
  • 23
    • 0030610901 scopus 로고    scopus 로고
    • eIF4G: Translation's mystery factor begins to yield its secrets
    • Morley,S.J., Curtis,P.S. and Pain,V.M. (1997) eIF4G: translation's mystery factor begins to yield its secrets. RNA, 3, 1085-1104.
    • (1997) RNA , vol.3 , pp. 1085-1104
    • Morley, S.J.1    Curtis, P.S.2    Pain, V.M.3
  • 24
    • 0025310854 scopus 로고
    • mRNA poly(A) tail, a 3′ enhancer of translational initiation
    • Munroe,D. and Jacobson,A. (1990) mRNA poly(A) tail, a 3′ enhancer of translational initiation. Mol. Cell. Biol., 10, 3441-3455.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 3441-3455
    • Munroe, D.1    Jacobson, A.2
  • 25
    • 0031054338 scopus 로고    scopus 로고
    • The proteolytic cleavage of eukaryotic initiation factor (eIF) 4G is prevented by eIF4E binding protein (PHAS-I; 4E-BP1) in the reticulocyte lysate
    • Ohlmann,T., Pain,V.M., Wood,W., Rau,M. and Morley,S.J. (1997) The proteolytic cleavage of eukaryotic initiation factor (eIF) 4G is prevented by eIF4E binding protein (PHAS-I; 4E-BP1) in the reticulocyte lysate. EMBO J., 16, 844-855.
    • (1997) EMBO J. , vol.16 , pp. 844-855
    • Ohlmann, T.1    Pain, V.M.2    Wood, W.3    Rau, M.4    Morley, S.J.5
  • 26
    • 0029968705 scopus 로고    scopus 로고
    • Initiation of protein synthesis in eukaryotic cells
    • Pain,V.M. (1996) Initiation of protein synthesis in eukaryotic cells. Eur. J. Biochem., 236, 747-771.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 747-771
    • Pain, V.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.