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Volumn 16, Issue 10, 1996, Pages 5328-5334

A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; ASPARTIC ACID; GLYCINE; INITIATION FACTOR; MESSENGER RNA; TYROSINE;

EID: 0039799706     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.16.10.5328     Document Type: Article
Times cited : (160)

References (46)
  • 2
    • 0027186325 scopus 로고
    • A S. cerevisiae homologue of mammalian translation initiation factor 4B contributing to RNA helicase activity
    • Altmann, M., P. P. Müller, B. Wittmer, S. Ruchti, F. Lanker, and H. Trachsel. 1993. A S. cerevisiae homologue of mammalian translation initiation factor 4B contributing to RNA helicase activity. EMBO J. 12:3997-4004.
    • (1993) EMBO J. , vol.12 , pp. 3997-4004
    • Altmann, M.1    Müller, P.P.2    Wittmer, B.3    Ruchti, S.4    Lanker, F.5    Trachsel, H.6
  • 3
    • 0029086291 scopus 로고
    • The Saccharomyces cerevisiae translation initiation factor Tif3 and its mammalian homologue, eIF-4B, have RNA annealing activity
    • Altmann, M., B. Wittmer, N. Méthot, N. Sonenberg, and H. Trachsel. 1995. The Saccharomyces cerevisiae translation initiation factor Tif3 and its mammalian homologue, eIF-4B, have RNA annealing activity. EMBO J. 14:3820-3827.
    • (1995) EMBO J. , vol.14 , pp. 3820-3827
    • Altmann, M.1    Wittmer, B.2    Méthot, N.3    Sonenberg, N.4    Trachsel, H.5
  • 4
    • 0021822441 scopus 로고
    • A mutation allowing an mRNA secondary structure diminishes translation of Saccharomyces cerevisiae iso-1-cytochrome C
    • Baim, S. B., D. F. Pietras, D. C. Eustice, and F. Sherman. 1985. A mutation allowing an mRNA secondary structure diminishes translation of Saccharomyces cerevisiae iso-1-cytochrome C. Mol. Cell. Biol. 5:1839-1846.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 1839-1846
    • Baim, S.B.1    Pietras, D.F.2    Eustice, D.C.3    Sherman, F.4
  • 5
    • 0027255909 scopus 로고
    • Elimination of false positives that arise in using the two-hybrid system
    • Bartel, P., C. T. Chien, R. Sternglanz, and S. Fields. 1993. Elimination of false positives that arise in using the two-hybrid system. BioTechniques 14:920-924.
    • (1993) BioTechniques , vol.14 , pp. 920-924
    • Bartel, P.1    Chien, C.T.2    Sternglanz, R.3    Fields, S.4
  • 7
    • 0017100264 scopus 로고
    • Purification and characterization of initiation factor IF-E3 from rabbit reticulocytes
    • Benne, R., and J. W. B. Hershey. 1976. Purification and characterization of initiation factor IF-E3 from rabbit reticulocytes. Proc. Natl. Acad. Sci. USA 73:3005-3009.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 3005-3009
    • Benne, R.1    Hershey, J.W.B.2
  • 8
    • 0018095166 scopus 로고
    • The mechanism of action of protein synthesis initiation factors from rabbit reticulocytes
    • Benne, R., and J. W. B. Hershey. 1978. The mechanism of action of protein synthesis initiation factors from rabbit reticulocytes. J. Biol. Chem. 253: 3078-3087.
    • (1978) J. Biol. Chem. , vol.253 , pp. 3078-3087
    • Benne, R.1    Hershey, J.W.B.2
  • 9
    • 0026680845 scopus 로고
    • Interaction cloning: Identification of a helix-loop-helix zipper protein that interacts with c-Fos
    • Blanar, M. A., and W. J. Rutter. 1992. Interaction cloning: identification of a helix-loop-helix zipper protein that interacts with c-Fos. Science 256:1014-1018.
    • (1992) Science , vol.256 , pp. 1014-1018
    • Blanar, M.A.1    Rutter, W.J.2
  • 10
    • 0028129989 scopus 로고
    • Conserved structures and diversity of functions of RNA-binding proteins
    • Burd, C. G., and G. Dreyfuss. 1994. Conserved structures and diversity of functions of RNA-binding proteins. Science 265:615-621.
    • (1994) Science , vol.265 , pp. 615-621
    • Burd, C.G.1    Dreyfuss, G.2
  • 11
    • 0015987426 scopus 로고
    • Prediction of protein conformation
    • Chou, P. Y., and G. D. Fasman. 1974. Prediction of protein conformation. Biochemistry 13:222-245.
    • (1974) Biochemistry , vol.13 , pp. 222-245
    • Chou, P.Y.1    Fasman, G.D.2
  • 12
    • 0027246625 scopus 로고
    • A new yeast translation initiation factor suppresses a mutation in the eIF-4A RNA helicase
    • Coppolecchia, R., P. Buser, A. Stotz, and P. Linder. 1993. A new yeast translation initiation factor suppresses a mutation in the eIF-4A RNA helicase. EMBO J. 12:4005-4011.
    • (1993) EMBO J. , vol.12 , pp. 4005-4011
    • Coppolecchia, R.1    Buser, P.2    Stotz, A.3    Linder, P.4
  • 13
    • 0021099528 scopus 로고
    • Identification and quantitation of levels of protein synthesis initiation factors in crude HeLa cell lysates by two-dimensional polyacrylamide gel electrophoresis
    • Duncan, R., and J. W. B. Hershey. 1983. Identification and quantitation of levels of protein synthesis initiation factors in crude HeLa cell lysates by two-dimensional polyacrylamide gel electrophoresis. J. Biol. Chem. 258: 7228-7235.
    • (1983) J. Biol. Chem. , vol.258 , pp. 7228-7235
    • Duncan, R.1    Hershey, J.W.B.2
  • 14
    • 0029092610 scopus 로고
    • Correlation of two-hybrid affinity data with in vitro measurements
    • Estojak, J., R. Brent, and E. A. Golemis. 1995. Correlation of two-hybrid affinity data with in vitro measurements. Mol. Cell. Biol. 15:5820-5829.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5820-5829
    • Estojak, J.1    Brent, R.2    Golemis, E.A.3
  • 15
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields, S., and O. Song. 1989. A novel genetic system to detect protein-protein interactions. Nature (London) 340:245-246.
    • (1989) Nature (London) , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 16
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz, D., A. St. Jean, R. A. Woods, and R. H. Schiestl. 1992. Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res. 20:1425.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1425
    • Gietz, D.1    St. Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 19
    • 0021270173 scopus 로고
    • RNA-stimulated ATPase activity of eukaryotic initiation factors
    • Grifo, J. A., R. D. Abramsom, C. A. Salter, and W. C. Merrick. 1984. RNA-stimulated ATPase activity of eukaryotic initiation factors. J. Biol. Chem. 259:8648-8654.
    • (1984) J. Biol. Chem. , vol.259 , pp. 8648-8654
    • Grifo, J.A.1    Abramsom, R.D.2    Salter, C.A.3    Merrick, W.C.4
  • 20
    • 85035180580 scopus 로고    scopus 로고
    • Personal communication
    • Hershey, J. W. B. Personal communication.
    • Hershey J. W., B.1
  • 21
    • 0026723117 scopus 로고
    • mRNAs containing extensive secondary structure in their 5′ non-coding region translate efficiently in cells overexpressing initiation factor eIF-4E
    • Koromilas, A. E., A. Lazaris-Karatzas, and N. Sonenberg. 1992. mRNAs containing extensive secondary structure in their 5′ non-coding region translate efficiently in cells overexpressing initiation factor eIF-4E. EMBO J. 11:4153-4158.
    • (1992) EMBO J. , vol.11 , pp. 4153-4158
    • Koromilas, A.E.1    Lazaris-Karatzas, A.2    Sonenberg, N.3
  • 22
    • 0029117427 scopus 로고
    • Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral protesses
    • Lamphear, B. J., R. Kirchweger, T. Skern, and R. E. Rhoads. 1995. Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral protesses. J. Biol. Chem. 270:21975-21983.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21975-21983
    • Lamphear, B.J.1    Kirchweger, R.2    Skern, T.3    Rhoads, R.E.4
  • 24
    • 0029166687 scopus 로고
    • The translation initiation factor eIF-4E hinds to a common motif shared by the translation factor eIF-4γ and the translational repressors, 4E-binding proteins
    • Mader, S., H. Lee, A. Pause, and N. Sonenberg. 1995. The translation initiation factor eIF-4E hinds to a common motif shared by the translation factor eIF-4γ and the translational repressors, 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
  • 25
    • 0027315727 scopus 로고
    • RNA recognition: A family matter?
    • Mattaj, I. 1993. RNA recognition: a family matter? Cell 73:837-840.
    • (1993) Cell , vol.73 , pp. 837-840
    • Mattaj, I.1
  • 26
    • 0021828470 scopus 로고
    • Eukaryotic protein synthesis initiation factor eIF-3: Determination of concentration and association with ribosomes in rabbit reticulocyte and HeLa cell lysates
    • Mengod, G., and H. Trachsel. 1985. Eukaryotic protein synthesis initiation factor eIF-3: determination of concentration and association with ribosomes in rabbit reticulocyte and HeLa cell lysates. Biochim. Biophys. Acta 825: 169-174.
    • (1985) Biochim. Biophys. Acta , vol.825 , pp. 169-174
    • Mengod, G.1    Trachsel, H.2
  • 27
    • 85035175967 scopus 로고    scopus 로고
    • Unpublished data
    • Méthot, N. Unpublished data.
    • Méthot, N.1
  • 28
    • 0028331455 scopus 로고
    • The translation initiation factor eIF-4B contains an RNA binding region that is distinct and independent from its ribonucleoprotein consensus sequence
    • Méthot, N., a. Pause, J. W. B. Hershey, and N. Sonenberg. 1994. The translation initiation factor eIF-4B contains an RNA binding region that is distinct and independent from its ribonucleoprotein consensus sequence. Mol. Cell. Biol. 14:2307-2316.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2307-2316
    • Méthot, N.1    Pause, A.2    Hershey, J.W.B.3    Sonenberg, N.4
  • 29
    • 0029805730 scopus 로고    scopus 로고
    • In vitro RNA selection identifies RNA ligands that specifically bind to eukaryotic translation initiation factor 4B: The role of the RNA recognition motif
    • Méthot, N., G. Pickett, J. D. Keene, and N. Sonenberg. 1996. In vitro RNA selection identifies RNA ligands that specifically bind to eukaryotic translation initiation factor 4B: the role of the RNA recognition motif. RNA 2:38-50.
    • (1996) RNA , vol.2 , pp. 38-50
    • Méthot, N.1    Pickett, G.2    Keene, J.D.3    Sonenberg, N.4
  • 30
    • 0002523042 scopus 로고    scopus 로고
    • The pathway and mechanism of eukaryotic protein synthesis
    • J. W. B. Hershey, M. B. Mathews, and N. Sonenberg (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Merrick, W. C., and J. W. B. Hershey. 1996. The pathway and mechanism of eukaryotic protein synthesis, p. 1-29. In J. W. B. Hershey, M. B. Mathews, and N. Sonenberg (ed.), Translational control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1996) Translational Control , pp. 1-29
    • Merrick, W.C.1    Hershey, J.W.B.2
  • 31
    • 0020494554 scopus 로고
    • Immunological characterization of mammalian protein synthesis initiation factors
    • Meyer, L. J., S. C. Milburn, and J. W. B. Hershey. 1982. Immunological characterization of mammalian protein synthesis initiation factors. Biochemistry 21:4206-4212.
    • (1982) Biochemistry , vol.21 , pp. 4206-4212
    • Meyer, L.J.1    Milburn, S.C.2    Hershey, J.W.B.3
  • 32
    • 0024998982 scopus 로고
    • Cloning and expression of eukaryotic initiation factor 4B: Sequence determination identifies a common RNA recognition motif
    • Milburn, S. C., J. W. B. Hershey, M. V. Davies, K. Kelleher, and R. J. Kaufman. 1990. Cloning and expression of eukaryotic initiation factor 4B: sequence determination identifies a common RNA recognition motif. EMBO J. 9:2783-2790.
    • (1990) EMBO J. , vol.9 , pp. 2783-2790
    • Milburn, S.C.1    Hershey, J.W.B.2    Davies, M.V.3    Kelleher, K.4    Kaufman, R.J.5
  • 33
    • 0028990057 scopus 로고
    • The RNP domain: A sequence-specific RNA binding domain involved in processing and transport of RNA
    • Nagai, K., C. Oubridge, N. Ito, J. Avis, and P. Evans. 1995. The RNP domain: a sequence-specific RNA binding domain involved in processing and transport of RNA. Trends Biochem. Sci. 20:235-240.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 235-240
    • Nagai, K.1    Oubridge, C.2    Ito, N.3    Avis, J.4    Evans, P.5
  • 34
    • 0016200293 scopus 로고
    • Dissociation of skeletal muscle ribosomes from normal and diabetic animals by initiation factors eIF-3
    • Nakaya, K., R. S. Ranu, and I. G. Wool. 1974. Dissociation of skeletal muscle ribosomes from normal and diabetic animals by initiation factors eIF-3. Biochem. Biophys. Res. Commun. 59:237-242.
    • (1974) Biochem. Biophys. Res. Commun. , vol.59 , pp. 237-242
    • Nakaya, K.1    Ranu, R.S.2    Wool, I.G.3
  • 35
    • 0028285942 scopus 로고
    • Two structural domains of initiation factor eIF-4B arc involved in binding to RNA
    • Naranda, T., W. B. Strong, J. Menaya, B. J. Fabbri, and J. W. B. Hershey. 1994. Two structural domains of initiation factor eIF-4B arc involved in binding to RNA. J. Biol. Chem. 269:14465-14472.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14465-14472
    • Naranda, T.1    Strong, W.B.2    Menaya, J.3    Fabbri, B.J.4    Hershey, J.W.B.5
  • 36
    • 0026680746 scopus 로고
    • Mutational analysis of a DEAD box RNA helicase: The mammalian translation initiation factor eIF-4A
    • Pause, A., and N. Sonenberg. 1992. Mutational analysis of a DEAD box RNA helicase: the mammalian translation initiation factor eIF-4A. EMBOJ. 11:2643-2654.
    • (1992) EMBOJ. , vol.11 , pp. 2643-2654
    • Pause, A.1    Sonenberg, N.2
  • 37
    • 0021799353 scopus 로고
    • Insertion mutagenesis to increase the secondary structure within the 5′ noncoding region of a eukaryotic mRNA reduces translational efficiency
    • Pelletier, J., and N. Sonenberg. 1985. Insertion mutagenesis to increase the secondary structure within the 5′ noncoding region of a eukaryotic mRNA reduces translational efficiency. Cell 40:515-526.
    • (1985) Cell , vol.40 , pp. 515-526
    • Pelletier, J.1    Sonenberg, N.2
  • 38
    • 0018786531 scopus 로고
    • Binding and release of radiolabeled eukaryotic initiation factors 2 and 3 during 80S initiation complex formation
    • Peterson, D. T., W. C. Merrick, and B. Safer. 1979. Binding and release of radiolabeled eukaryotic initiation factors 2 and 3 during 80S initiation complex formation. J. Biol. Chem. 254:2509-2510.
    • (1979) J. Biol. Chem. , vol.254 , pp. 2509-2510
    • Peterson, D.T.1    Merrick, W.C.2    Safer, B.3
  • 40
    • 0020645053 scopus 로고
    • Construction and use of gene fusions lacZ (β-galaclosidase) which are expressed in yeast
    • Rose, M., and D. Botstein. 1983. Construction and use of gene fusions lacZ (β-galaclosidase) which are expressed in yeast. Methods Enzymol. 101:167-180.
    • (1983) Methods Enzymol. , vol.101 , pp. 167-180
    • Rose, M.1    Botstein, D.2
  • 41
    • 0025176473 scopus 로고
    • Bidirectional RNA helicase activity of eucaryotic translation initiation factors 4A and 4F
    • Rozen, F., I. Edery, K. Meerovitch, T. E. Dever, W. C. Merrick, and N. Sonenberg. 1990. Bidirectional RNA helicase activity of eucaryotic translation initiation factors 4A and 4F. Mol. Cell. Biol. 10:1134-1144.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1134-1144
    • Rozen, F.1    Edery, I.2    Meerovitch, K.3    Dever, T.E.4    Merrick, W.C.5    Sonenberg, N.6
  • 42
    • 0000831271 scopus 로고    scopus 로고
    • mRNA 5′ cap-binding protein eIF4E and control of cell growth
    • J. W. B. Hershey, M. B. Mathews, and N. Sonenberg (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Sonenberg, N. 1996. mRNA 5′ cap-binding protein eIF4E and control of cell growth, p. 245-269. In J. W. B. Hershey, M. B. Mathews, and N. Sonenberg (ed.), Translational control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1996) Translational Control , pp. 245-269
    • Sonenberg, N.1
  • 43
    • 0018143765 scopus 로고
    • A polypeptide in eukaryotic initiation factors that crosslinks specifically to the 5′-terminal cap in mRNA
    • Sonenberg, N., M. A. Morgan, W. C. Merrick, and A. J. Shatkin. 1978. A polypeptide in eukaryotic initiation factors that crosslinks specifically to the 5′-terminal cap in mRNA. Proc. Natl. Acad. Sci. USA 75:4843-4847.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4843-4847
    • Sonenberg, N.1    Morgan, M.A.2    Merrick, W.C.3    Shatkin, A.J.4
  • 45
    • 0017707116 scopus 로고
    • Initiation of mammalian protein synthesis: The assembly of the initiation complex with purified initiation factors
    • Trachsel, H., B. Erni, M. H. Schreier, and T. Staehelin. 1977. Initiation of mammalian protein synthesis: the assembly of the initiation complex with purified initiation factors. J. Mol. Biol. 116:755-767.
    • (1977) J. Mol. Biol. , vol.116 , pp. 755-767
    • Trachsel, H.1    Erni, B.2    Schreier, M.H.3    Staehelin, T.4
  • 46
    • 0023894655 scopus 로고
    • Characterization of glutathione S-transferases in rat kidney. Alteration of composition by cis-platinum
    • Trakshel, G. M., and M. D. Maines. 1988. Characterization of glutathione S-transferases in rat kidney. Alteration of composition by cis-platinum. Biochem. J. 252:127-136.
    • (1988) Biochem. J. , vol.252 , pp. 127-136
    • Trakshel, G.M.1    Maines, M.D.2


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