메뉴 건너뛰기




Volumn 2, Issue 3, 1998, Pages 383-388

IRP-1 binding to ferritin mRNA prevents the recruitment of the small ribosomal subunit by the cap-binding complex elF4F

Author keywords

[No Author keywords available]

Indexed keywords

CAPPED RNA; FERRITIN; INITIATION FACTOR; INITIATION FACTOR 4F; IRON REGULATORY FACTOR; IRON REGULATORY PROTEIN 1; IRON SULFUR PROTEIN; MESSENGER RNA; RNA BINDING PROTEIN;

EID: 0032160381     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(00)80282-8     Document Type: Article
Times cited : (225)

References (42)
  • 1
    • 0027186325 scopus 로고
    • A Saccharomyces cerevisiae homologue of mammalian translation initiation factor 4B contributes to RNA helicase activity
    • Altmann, M., Muller, P.P., Wittmer, B., Ruchti, F., Lanker, S., and Trachsel, H. (1993). A Saccharomyces cerevisiae homologue of mammalian translation initiation factor 4B contributes to RNA helicase activity. EMBO J. 12, 3997-4003.
    • (1993) EMBO J. , vol.12 , pp. 3997-4003
    • Altmann, M.1    Muller, P.P.2    Wittmer, B.3    Ruchti, F.4    Lanker, S.5    Trachsel, H.6
  • 2
    • 0026541436 scopus 로고
    • Analysis of 40 S and 80 S complexes with mRNA as measured by sucrose density gradients and primer extension inhibition
    • Anthony, D.D., and Merrick, W.C. (1992). Analysis of 40 S and 80 S complexes with mRNA as measured by sucrose density gradients and primer extension inhibition. J. Biol. Chem. 267, 1554-1562.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1554-1562
    • Anthony, D.D.1    Merrick, W.C.2
  • 3
    • 0030827905 scopus 로고    scopus 로고
    • Structure of cDNAs encoding human eukaryotic initiation factors subunits. Possible roles in RNA binding and macromolecular assembly
    • Asano, K., Vornlocher, H.P., Richter-Cook, N.J., Merrick, W.C., Hinnebusch, A.G., and Hershey, J.W. (1997). Structure of cDNAs encoding human eukaryotic initiation factors subunits. Possible roles in RNA binding and macromolecular assembly. J. Biol. Chem. 272, 27042-27052.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27042-27052
    • Asano, K.1    Vornlocher, H.P.2    Richter-Cook, N.J.3    Merrick, W.C.4    Hinnebusch, A.G.5    Hershey, J.W.6
  • 4
    • 0028881134 scopus 로고
    • Mutation in the iron responsive element of the L ferritin mRNA in a family with dominant hyperferritinaemia and cataract
    • Beaumont, C., Leneuve, P., Devaux, I., Scoazec, J., Berthier, M., Loiseau, M., Grandchamp, B., and Bonneau, D. (1995). Mutation in the iron responsive element of the L ferritin mRNA in a family with dominant hyperferritinaemia and cataract. Nat. Genet. 11, 444-446.
    • (1995) Nat. Genet. , vol.11 , pp. 444-446
    • Beaumont, C.1    Leneuve, P.2    Devaux, I.3    Scoazec, J.4    Berthier, M.5    Loiseau, M.6    Grandchamp, B.7    Bonneau, D.8
  • 5
    • 0029053016 scopus 로고
    • Degradation of mRNA in eukaryotes
    • Beelman, C.A., and Parker, R. (1995). Degradation of mRNA in eukaryotes. Cell 81, 179-183.
    • (1995) Cell , vol.81 , pp. 179-183
    • Beelman, C.A.1    Parker, R.2
  • 6
    • 0002750772 scopus 로고
    • Mechanisms of iron toxicity
    • J.H. Brock, J.W. Halliday, M.J. Pippard, and L.W. Powell, eds. (London: W.B. Saunders)
    • Britton, R.S., Tavill, A.S., and Bacon, B.R. (1994). Mechanisms of iron toxicity. In Iron Metabolism in Health and Disease, J.H. Brock, J.W. Halliday, M.J. Pippard, and L.W. Powell, eds. (London: W.B. Saunders), 311-351.
    • (1994) Iron Metabolism in Health and Disease , pp. 311-351
    • Britton, R.S.1    Tavill, A.S.2    Bacon, B.R.3
  • 8
    • 0028788201 scopus 로고
    • Molecular basis for the recently described hereditary hyperferritinemia-cataract syndrome: A mutation in the iron-responsive element of ferritin L-subunit gene
    • Girelli, D., Corrocher, R., Bisceglia, L., Olivieri, O., De Franceschi, L., Zelante, L., and Gasparini, P. (1995). Molecular basis for the recently described hereditary hyperferritinemia-cataract syndrome: a mutation in the iron-responsive element of ferritin L-subunit gene. Blood 86, 4050-4053.
    • (1995) Blood , vol.86 , pp. 4050-4053
    • Girelli, D.1    Corrocher, R.2    Bisceglia, L.3    Olivieri, O.4    De Franceschi, L.5    Zelante, L.6    Gasparini, P.7
  • 9
    • 0026729483 scopus 로고
    • Position is the critical determinant for function of iron-responsive elements as translational regulators
    • Goossen, B., and Hentze, M.W. (1992). Position is the critical determinant for function of iron-responsive elements as translational regulators. Mol. Cell. Biol. 12, 1959-1966.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1959-1966
    • Goossen, B.1    Hentze, M.W.2
  • 10
    • 0028059555 scopus 로고
    • Iron regulatory protein prevents binding of the 43S translation pre-initiation complex to ferritin and eALAS mRNAs
    • Gray, N.K., and Hentze, M.W. (1994). Iron regulatory protein prevents binding of the 43S translation pre-initiation complex to ferritin and eALAS mRNAs. EMBO J. 13, 3882-3891.
    • (1994) EMBO J. , vol.13 , pp. 3882-3891
    • Gray, N.K.1    Hentze, M.W.2
  • 11
    • 0027131432 scopus 로고
    • Recombinant iron regulatory factor functions as an iron-responsive element-binding protein, a translational repressor and an aconitase. A functional assay for translational repression and direct demonstration of the iron switch
    • Gray, N.K., Quick, S., Goossen, B., Constable, A., Hirling, H., Kühn, L.C., and Hentze, M.W. (1993). Recombinant iron regulatory factor functions as an iron-responsive element-binding protein, a translational repressor and an aconitase. A functional assay for translational repression and direct demonstration of the iron switch. Eur. J. Biochem. 218, 657-667.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 657-667
    • Gray, N.K.1    Quick, S.2    Goossen, B.3    Constable, A.4    Hirling, H.5    Kühn, L.C.6    Hentze, M.W.7
  • 12
    • 0030832026 scopus 로고    scopus 로고
    • elF4G dramatically enhances the binding of elF4E to the mRNA 5′-Cap structure
    • Haghighat, A., and Sonenberg, N. (1997). elF4G dramatically enhances the binding of elF4E to the mRNA 5′-Cap structure. J. Biol. Chem. 272, 21677-21680.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21677-21680
    • Haghighat, A.1    Sonenberg, N.2
  • 13
    • 0003240658 scopus 로고
    • Cellular iron processing and storage: The role of ferritin
    • J.H. Brock, J.W. Halliday, M.J. Pippard, and L.W. Powell, eds. (London: W.B. Saunders)
    • Halliday, J.W., Ramm, G.A., and Powell, L.W. (1994). Cellular iron processing and storage: the role of ferritin. In Iron Metabolism in Health and Disease, J.H. Brock, J.W. Halliday, M.J. Pippard, and L.W. Powell, eds. (London: W.B. Saunders), 97-122.
    • (1994) Iron Metabolism in Health and Disease , pp. 97-122
    • Halliday, J.W.1    Ramm, G.A.2    Powell, L.W.3
  • 14
    • 0031024024 scopus 로고    scopus 로고
    • elF4G: A multipurpose ribosome adapter?
    • Hentze, M.W. (1997). elF4G: a multipurpose ribosome adapter? Science 275, 500-501.
    • (1997) Science , vol.275 , pp. 500-501
    • Hentze, M.W.1
  • 15
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide and oxidative stress
    • Hentze, M.W., and Kühn, L.C. (1996). Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide and oxidative stress. Proc. Natl. Acad. Sci. USA 93, 8175-8182.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kühn, L.C.2
  • 16
    • 0025832056 scopus 로고
    • Translational control in mammalian cells
    • Hershey, J.W. (1991). Translational control in mammalian cells. Annu. Rev. Biochem. 60, 717-755.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 717-755
    • Hershey, J.W.1
  • 17
    • 0013916771 scopus 로고
    • A competitive inhibitor of the GTP reaction in protein synthesis
    • Hershey, J.W., and Monro, R.E. (1966). A competitive inhibitor of the GTP reaction in protein synthesis. J. Mol. Biol. 18, 68-76.
    • (1966) J. Mol. Biol. , vol.18 , pp. 68-76
    • Hershey, J.W.1    Monro, R.E.2
  • 18
    • 0030666625 scopus 로고    scopus 로고
    • Human eukaryotictranslation initiation factor 4G (elF4G) possesses two independent binding sites for elF4A
    • Imataka, H., and Sonenberg, N. (1997). Human eukaryotictranslation initiation factor 4G (elF4G) possesses two independent binding sites for elF4A. Mol. Cell. Biol. 17, 6940-6947.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6940-6947
    • Imataka, H.1    Sonenberg, N.2
  • 19
    • 0028069687 scopus 로고
    • In vitro synthesis of human protein synthesis initiation factor 4γ and its localization on 43 and 48 S initiation complexes
    • Joshi, B., Yan, R., and Rhoads, R.E. (1994). In vitro synthesis of human protein synthesis initiation factor 4γ and its localization on 43 and 48 S initiation complexes. J. Biol. Chem. 269, 2048-2055.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2048-2055
    • Joshi, B.1    Yan, R.2    Rhoads, R.E.3
  • 20
    • 0029397360 scopus 로고
    • Direct evidence that polypyrimidine tract binding protein (PTB) is essential for internal initiation of translation of encephalomyocarditis virus RNA
    • Kaminski, A., Hunt, S.L., Patton, J.G., and Jackson, R.J. (1995). Direct evidence that polypyrimidine tract binding protein (PTB) is essential for internal initiation of translation of encephalomyocarditis virus RNA. RNA 1, 924-938.
    • (1995) RNA , vol.1 , pp. 924-938
    • Kaminski, A.1    Hunt, S.L.2    Patton, J.G.3    Jackson, R.J.4
  • 21
    • 0000580062 scopus 로고
    • Isolation and characterization of ribonucleoprotein complexes
    • S.J. Higgins and B.D. Hames, eds. (Oxford: Oxford University Press)
    • Lamond, A.I., and Sproat, B. (1994). Isolation and characterization of ribonucleoprotein complexes. In RNA Processing - A Practical approach, S.J. Higgins and B.D. Hames, eds. (Oxford: Oxford University Press), pp. 103-140.
    • (1994) RNA Processing - A Practical Approach , pp. 103-140
    • Lamond, A.I.1    Sproat, B.2
  • 22
    • 0029117427 scopus 로고
    • Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (elF4G) with picornaviral proteases
    • Lamphear, B.J., Kirchweger, R., Skern, T., and Rhoads, R.E. (1995). Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (elF4G) with picornaviral proteases. 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
  • 23
    • 0029166687 scopus 로고
    • The translation initiation factor elF-4E binds to a common motif shared by the translation factor elF-4γ and the translational repressors 4E-binding proteins
    • Mader, S., Lee, H., Pause, A., and Sonenberg, N. (1995). The translation initiation factor elF-4E binds to a common motif shared by the translation factor elF-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
  • 24
    • 0026718508 scopus 로고
    • Mechanism and regulation of eukaryotic protein synthesis
    • Merrick, W.C. (1992). Mechanism and regulation of eukaryotic protein synthesis. Microbiol. Rev. 56, 291-315.
    • (1992) Microbiol. Rev. , vol.56 , pp. 291-315
    • Merrick, W.C.1
  • 25
    • 0039799706 scopus 로고    scopus 로고
    • A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation factor 4B (elF4B) self-association and interaction with elF3
    • Methot, N., Song, M.S., and Sonenberg, N. (1996). A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation factor 4B (elF4B) self-association and interaction with elF3. Mol. Cell. Biol. 16, 5328-5334.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5328-5334
    • Methot, N.1    Song, M.S.2    Sonenberg, N.3
  • 26
    • 0028902356 scopus 로고
    • Hormone-induced meiotic maturation in Xenopus oocytes occurs independently of p70s6k activation and is associated with enhanced initiation factor (elF)-4F phosphorylation and complex formation
    • Morley, S.J., and Pain, V.M. (1995). Hormone-induced meiotic maturation in Xenopus oocytes occurs independently of p70s6k activation and is associated with enhanced initiation factor (elF)-4F phosphorylation and complex formation. J. Cell Sci. 108, 1751-1760.
    • (1995) J. Cell Sci. , vol.108 , pp. 1751-1760
    • Morley, S.J.1    Pain, V.M.2
  • 27
    • 0030610901 scopus 로고    scopus 로고
    • elF4G: Translation's mystery factor begins to yield its secrets
    • Morley, S.J., Curtis, P.S., and Pain, V.M. (1997). elF4G: translation's mystery factor begins to yield its secrets. RNA 10, 1085-1104.
    • (1997) RNA , vol.10 , pp. 1085-1104
    • Morley, S.J.1    Curtis, P.S.2    Pain, V.M.3
  • 28
    • 0015216932 scopus 로고
    • The mechanism by which cycloheximide and related glutarimide antibiotics inhibit peptide synthesis on reticulocyte ribosomes
    • Obrig, T.G., Culp, W.J., McKeehan, W.L., and Hardesty, B. (1971). The mechanism by which cycloheximide and related glutarimide antibiotics inhibit peptide synthesis on reticulocyte ribosomes. J. Biol. Chem. 246, 174-181.
    • (1971) J. Biol. Chem. , vol.246 , pp. 174-181
    • Obrig, T.G.1    Culp, W.J.2    McKeehan, W.L.3    Hardesty, B.4
  • 29
    • 0028901902 scopus 로고
    • Proteolytic cleavage of initiation factor elF-4γ in the reticulocyte lysate inhibits translation of capped mRNAs but enhances that of uncapped mRNAs
    • Ohlmann, T., Rau, M., Morley, S.J., and Pain, V.M. (1995). Proteolytic cleavage of initiation factor elF-4γ in the reticulocyte lysate inhibits translation of capped mRNAs but enhances that of uncapped mRNAs. Nucleic Acids Res. 23, 334-340.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 334-340
    • Ohlmann, T.1    Rau, M.2    Morley, S.J.3    Pain, V.M.4
  • 30
    • 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
  • 32
    • 0026680746 scopus 로고
    • Mutational analysis of a DEAD box RNA helicase: The mammalian translation initiation factor elF-4A
    • Pause, A., and Sonenberg, N. (1992). Mutational analysis of a DEAD box RNA helicase: the mammalian translation initiation factor elF-4A. EMBO J. 11, 2643-2654.
    • (1992) EMBO J. , vol.11 , pp. 2643-2654
    • Pause, A.1    Sonenberg, N.2
  • 33
    • 0030009739 scopus 로고    scopus 로고
    • A reevaluation of the cap-binding protein, elF4E, as a rate-limiting factor for initiation of translation in reticulocyte lysate
    • Rau, M., Ohlmann, T., Morley, S.J., and Pain, V.M. (1996). A reevaluation of the cap-binding protein, elF4E, as a rate-limiting factor for initiation of translation in reticulocyte lysate. J. Biol. Chem. 271, 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
  • 34
    • 0028589581 scopus 로고
    • Participation of initiation factors in the recruitment of mRNA to ribosomes
    • Rhoads, R.E., Joshi, B., and Minich, W.B. (1994). Participation of initiation factors in the recruitment of mRNA to ribosomes. Biochimie 76, 831-838.
    • (1994) Biochimie , vol.76 , pp. 831-838
    • Rhoads, R.E.1    Joshi, B.2    Minich, W.B.3
  • 35
    • 0023713448 scopus 로고
    • Binding of a cytosolic protein to the iron-responsive element of human ferritin messenger RNA
    • Rouault, T.A., Hentze, M.W., Caughman, S.W., Harford, J.B., and Klausner, R.D. (1988). Binding of a cytosolic protein to the iron-responsive element of human ferritin messenger RNA. Science 241, 1207-1210.
    • (1988) Science , vol.241 , pp. 1207-1210
    • Rouault, T.A.1    Hentze, M.W.2    Caughman, S.W.3    Harford, J.B.4    Klausner, R.D.5
  • 36
    • 0002146863 scopus 로고    scopus 로고
    • Translational control of ferritin
    • J.W.B. Hershey, M.B. Mathews, and N. Sonenberg, eds. (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press)
    • Rouault, T., Klausner, R.D., and Harford, J.B. (1996). Translational control of ferritin. In Translational Control, J.W.B. Hershey, M.B. Mathews, and N. Sonenberg, eds. (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press), pp. 335-362.
    • (1996) Translational Control , pp. 335-362
    • Rouault, T.1    Klausner, R.D.2    Harford, J.B.3
  • 37
    • 0025176473 scopus 로고
    • Bidirectional RNA helicase activity of eucaryotic translation initiation factors 4A and 4F
    • Rozen, F., Edery, I., Meerovitch, K., Dever, T.E., Merrick, W.C., and Sonenberg, N. (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
  • 38
    • 0030731419 scopus 로고    scopus 로고
    • Starting at the beginning, middle, and end: Translation initiation in eukaryotes
    • Sachs, A.B., Sarnow, P., and Hentze, M.W. (1997). Starting at the beginning, middle, and end: translation initiation in eukaryotes. Cell 89, 831-838.
    • (1997) Cell , vol.89 , pp. 831-838
    • Sachs, A.B.1    Sarnow, P.2    Hentze, M.W.3
  • 39
    • 0025856617 scopus 로고
    • Modulation of the mitogenic activity of eukaryotic translation initiation factor-4E by protein kinase C
    • Smith, M.R., Jaramillo, M., Tuazon, P.T., Traugh, J.A., Liu, Y.L., Sonenberg, N., and Kung, H.F. (1991). Modulation of the mitogenic activity of eukaryotic translation initiation factor-4E by protein kinase C. New Biol. 3, 601-607.
    • (1991) New Biol. , vol.3 , pp. 601-607
    • Smith, M.R.1    Jaramillo, M.2    Tuazon, P.T.3    Traugh, J.A.4    Liu, Y.L.5    Sonenberg, N.6    Kung, H.F.7
  • 40
    • 0026494918 scopus 로고
    • Bacteriophage and spliceosomal proteins function as position-dependent cis/trans repressors of mRNA translation in vitro
    • Stripecke, R., and Hentze, M.W. (1992). Bacteriophage and spliceosomal proteins function as position-dependent cis/trans repressors of mRNA translation in vitro. Nucleic Acids Res. 20, 5555-5564.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 5555-5564
    • Stripecke, R.1    Hentze, M.W.2
  • 41
    • 0028070676 scopus 로고
    • Proteins binding to 5′ untranslated region sites: A general mechanism for translational regulation of mRNAs in human and yeast cells
    • Stripecke, R., Oliveira, C.C., McCarthy, J.E., and Hentze, M.W. (1994). Proteins binding to 5′ untranslated region sites: a general mechanism for translational regulation of mRNAs in human and yeast cells. Mol. Cell. Biol. 14, 5898-5909.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5898-5909
    • Stripecke, R.1    Oliveira, C.C.2    McCarthy, J.E.3    Hentze, M.W.4
  • 42
    • 0030454053 scopus 로고    scopus 로고
    • General RNA binding proteins render translation cap dependent
    • Svitkin, Y.V., Ovchinnikov, L.P., Dreyfuss, G., and Sonenberg, N. (1996). General RNA binding proteins render translation cap dependent. EMBO J. 15, 7147-7155.
    • (1996) EMBO J. , vol.15 , pp. 7147-7155
    • Svitkin, Y.V.1    Ovchinnikov, L.P.2    Dreyfuss, G.3    Sonenberg, N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.