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Volumn 37, Issue 3, 2003, Pages 421-428

Minor Secondary-Structure Variation in the 5′-Untranslated Region of the β-Globin mRNA Changes the Concentration Requirements for eIF2

Author keywords

globin mRNA; 5 untranslated region; Initiation factor eIF2; Mammals; mRNA secondary structure; Reconstruction of the 48S initiation complex; Translation initiation

Indexed keywords

BETA GLOBIN; MESSENGER RNA; PROTEIN P50; PROTEIN SUBUNIT; RNA BINDING PROTEIN; RNA BINDING PROTEIN EIF2; RNA BINDING PROTEIN ELF4B; RNA BINDING PROTEIN ELF4F; UNCLASSIFIED DRUG;

EID: 0037786786     PISSN: 00268933     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1024243512085     Document Type: Article
Times cited : (3)

References (32)
  • 1
    • 0037154965 scopus 로고    scopus 로고
    • Gene-specific regulation by general translation factors
    • Dever T.E. 2002. Gene-specific regulation by general translation factors. Cell. 108, 545-556.
    • (2002) Cell , vol.108 , pp. 545-556
    • Dever, T.E.1
  • 3
    • 0025186664 scopus 로고
    • Selection of the 5′-proximal translation initiation site is influenced by mRNA and eIF-2 concentrations
    • Dasso M.C., Milburn S.C., Hershey J.W., Jackson R.J. 1990. Selection of the 5′-proximal translation initiation site is influenced by mRNA and eIF-2 concentrations. Eur. J. Biochem. 187, 361-371.
    • (1990) Eur. J. Biochem. , vol.187 , pp. 361-371
    • Dasso, M.C.1    Milburn, S.C.2    Hershey, J.W.3    Jackson, R.J.4
  • 4
    • 0027490295 scopus 로고
    • Gene-specific translational control of the yeast GCN4 gene by phosphorylation of eukaryotic initiation factor 2
    • Hinnebusch A.G. 1993. Gene-specific translational control of the yeast GCN4 gene by phosphorylation of eukaryotic initiation factor 2. Mol. Microbiol. 10, 215-223.
    • (1993) Mol. Microbiol. , vol.10 , pp. 215-223
    • Hinnebusch, A.G.1
  • 5
    • 0024539506 scopus 로고
    • Ribosome binding to inosine-substituted mRNAs in the absence of ATP and mRNA factors
    • Seal S.N., Schmidt A., Marcus A. 1989. Ribosome binding to inosine-substituted mRNAs in the absence of ATP and mRNA factors. J. Biol. Chem. 264, 7363-7368.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7363-7368
    • Seal, S.N.1    Schmidt, A.2    Marcus, A.3
  • 6
    • 0017381607 scopus 로고
    • Characterization of GTP-dependent Met-tRNAf binding protein
    • Barrieux A., Rosenfeld M.G. 1977. Characterization of GTP-dependent Met-tRNAf binding protein. J. Biol. Chem. 252, 3843-3847.
    • (1977) J. Biol. Chem. , vol.252 , pp. 3843-3847
    • Barrieux, A.1    Rosenfeld, M.G.2
  • 8
    • 0027254593 scopus 로고
    • Further biochemical characterization of rabbit reticulocyte eIF-4B
    • Hughes D.L., Dever T.E., Merrick W.C. 1993. Further biochemical characterization of rabbit reticulocyte eIF-4B. Arch. Biochem. Biophys. 301, 311-319.
    • (1993) Arch. Biochem. Biophys. , vol.301 , pp. 311-319
    • Hughes, D.L.1    Dever, T.E.2    Merrick, W.C.3
  • 9
    • 0016609219 scopus 로고
    • Translation in vitro of rat brain messenger RNA coding for tubulin and actin
    • Gozes I., Schmitt H., Littauer U.Z. 1975. Translation in vitro of rat brain messenger RNA coding for tubulin and actin. Proc. Natl. Acad. Sci. USA. 72, 701-705.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 701-705
    • Gozes, I.1    Schmitt, H.2    Littauer, U.Z.3
  • 10
    • 0017111458 scopus 로고
    • Inhibitory action of different RNA fractions on the translation of globin mRNA in vitro
    • Wettenhall R.E., Slobbe A. 1976. Inhibitory action of different RNA fractions on the translation of globin mRNA in vitro. Biochim. Biophys. Acta. 432, 323-328.
    • (1976) Biochim. Biophys. Acta , vol.432 , pp. 323-328
    • Wettenhall, R.E.1    Slobbe, A.2
  • 11
    • 0024792578 scopus 로고
    • Translational active mRNPs from rabbit reticulocytes are qualitatively different from free mRNA in their translatability in cell-free system
    • Minich W.B., Korneyeva N.L., Ovchinnikov L.P. 1989. Translational active mRNPs from rabbit reticulocytes are qualitatively different from free mRNA in their translatability in cell-free system. FEBS Lett. 257, 257-259.
    • (1989) FEBS Lett. , vol.257 , pp. 257-259
    • Minich, W.B.1    Korneyeva, N.L.2    Ovchinnikov, L.P.3
  • 13
    • 0016244482 scopus 로고
    • Characteristics of rabbit globin mRNA purification by oligo(dT) cellulose chromatography
    • Gielen J., Aviv H., Leder P. 1974. Characteristics of rabbit globin mRNA purification by oligo(dT) cellulose chromatography. Arch. Biochem. Biophys. 163, 146-154.
    • (1974) Arch. Biochem. Biophys. , vol.163 , pp. 146-154
    • Gielen, J.1    Aviv, H.2    Leder, P.3
  • 14
    • 0035405034 scopus 로고    scopus 로고
    • In vitro reconstruction of initiation complexes to study the molecular mechanisms of translation initiation in mammals
    • Shatskii I.N. 2001. In vitro reconstruction of initiation complexes to study the molecular mechanisms of translation initiation in mammals. Mol. Biol. 35, 628-637.
    • (2001) Mol. Biol. , vol.35 , pp. 628-637
    • Shatskii, I.N.1
  • 15
    • 0034768617 scopus 로고    scopus 로고
    • Preparation and activity of synthetic unmodified mammalian tRNAi(Met) in initiation of translation in vitro
    • Pestova T.V., Hellen C.U. 2001. Preparation and activity of synthetic unmodified mammalian tRNAi(Met) in initiation of translation in vitro. RNA. 7, 1496-1505.
    • (2001) RNA , vol.7 , pp. 1496-1505
    • Pestova, T.V.1    Hellen, C.U.2
  • 16
    • 0018371457 scopus 로고
    • Purification of protein synthesis initiation factors from rabbit reticulocytes
    • Merrick W.C. 1979. Purification of protein synthesis initiation factors from rabbit reticulocytes. Methods Enzymol. 60, 101-108.
    • (1979) Methods Enzymol. , vol.60 , pp. 101-108
    • Merrick, W.C.1
  • 18
    • 0024346104 scopus 로고
    • Secondary structure analysis of adenovirus tripartite leader
    • Zhang Y., Dolph P.J., Schneider R.J. 1989. Secondary structure analysis of adenovirus tripartite leader. J. Biol. Chem. 264, 10679-10684.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10679-10684
    • Zhang, Y.1    Dolph, P.J.2    Schneider, R.J.3
  • 19
    • 0024414469 scopus 로고
    • Circumstances and mechanisms of inhibition of translation by secondary structure in eucaryotic mRNAs
    • Kozak M. 1989. Circumstances and mechanisms of inhibition of translation by secondary structure in eucaryotic mRNAs. Mol. Cell Biol. 9, 5134-5142.
    • (1989) Mol. Cell Biol. , vol.9 , pp. 5134-5142
    • Kozak, M.1
  • 20
    • 0027417253 scopus 로고
    • Inhibition of translational initiation in the yeast Saccharomyces cerevisiae as a function of the stability and position of hairpin structures in the mRNA leader
    • Vega Laso M.R., Zhu D., Sagliocco F., Brown A.J., Tuite M.F., McCarthy J.E. 1993. Inhibition of translational initiation in the yeast Saccharomyces cerevisiae as a function of the stability and position of hairpin structures in the mRNA leader. J. Biol. Chem. 268, 6453-6462.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6453-6462
    • Vega Laso, M.R.1    Zhu, D.2    Sagliocco, F.3    Brown, A.J.4    Tuite, M.F.5    McCarthy, J.E.6
  • 21
    • 0026702105 scopus 로고
    • Role of cytoplasmic mRNP proteins in translation
    • Minich W.B., Ovchinnikov L.P. 1992. Role of cytoplasmic mRNP proteins in translation. Biochimie. 74, 477-483.
    • (1992) Biochimie , vol.74 , pp. 477-483
    • Minich, W.B.1    Ovchinnikov, L.P.2
  • 22
    • 0037013235 scopus 로고    scopus 로고
    • Positive and negative effects of the major mammalian messenger ribonucleoprotein p50 on binding of 40S ribosomal subunits to the initiation codon of beta-globin mRNA
    • Pisarev A.V., Skabkin M.A., Thomas A.A., Merrick W.C., Ovchinnikov L.P., Shatsky I.N. 2002. Positive and negative effects of the major mammalian messenger ribonucleoprotein p50 on binding of 40S ribosomal subunits to the initiation codon of beta-globin mRNA. J. Biol. Chem. 277, 15445-15451.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15445-15451
    • Pisarev, A.V.1    Skabkin, M.A.2    Thomas, A.A.3    Merrick, W.C.4    Ovchinnikov, L.P.5    Shatsky, I.N.6
  • 23
    • 0018787242 scopus 로고
    • 14C]eukaryotic initiation factor 2 to measure the endogenous pool size of eukaryotic initiation factor 2 in rabbit reticulocyte lysate
    • 14C] eukaryotic initiation factor 2 to measure the endogenous pool size of eukaryotic initiation factor 2 in rabbit reticulocyte lysate. J. Biol. Chem. 254, 8091-8094.
    • (1979) J. Biol. Chem. , vol.254 , pp. 8091-8094
    • Safer, B.1    Kemper, W.2    Jagus, R.3
  • 24
    • 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., Hershey J.W. 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.2
  • 25
    • 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
    • Rau M., Ohlmann T., Morley S.J., Pain V.M. 1996. A reevaluation of the cap-binding protein, eIF4E, 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
  • 26
    • 0035231288 scopus 로고    scopus 로고
    • Initiation factor eIF2 alpha phosphorylation in stress responses and apoptosis
    • Clemens M.J. 2001. Initiation factor eIF2 alpha phosphorylation in stress responses and apoptosis. Progress Mol. Subcell. Biol. 27, 57-89.
    • (2001) Progress Mol. Subcell. Biol. , vol.27 , pp. 57-89
    • Clemens, M.J.1
  • 27
    • 0020490176 scopus 로고
    • Translational control by messenger RNA competition for eukaryotic initiation factor 2
    • Rosen H., Di Segni G., Kaempfer R. 1982. Translational control by messenger RNA competition for eukaryotic initiation factor 2. J. Biol. Chem. 257, 946-952.
    • (1982) J. Biol. Chem. , vol.257 , pp. 946-952
    • Rosen, H.1    Di Segni, G.2    Kaempfer, R.3
  • 28
    • 0018802019 scopus 로고
    • Competition between alpha- and beta-globin messenger ribonucleic acids for eukaryotic initiation factor 2
    • Di Segni G., Rosen H., Kaempfer R. 1979. Competition between alpha- and beta-globin messenger ribonucleic acids for eukaryotic initiation factor 2. Biochemistry. 18, 2847-2854.
    • (1979) Biochemistry , vol.18 , pp. 2847-2854
    • Di Segni, G.1    Rosen, H.2    Kaempfer, R.3
  • 29
    • 0018072551 scopus 로고
    • mRNA-induced dissociation of initiation factor 2
    • Barrieux A., Rosenfeld M.G. 1978. mRNA-induced dissociation of initiation factor 2. J. Biol. Chem. 253, 6311-6314.
    • (1978) J. Biol. Chem. , vol.253 , pp. 6311-6314
    • Barrieux, A.1    Rosenfeld, M.G.2
  • 30
    • 0026844798 scopus 로고
    • Hypothesis: Is eukaryotic initiation factor 2 the scanning factor?
    • Thomas A.A., Scheper G.C., Voorma H.O. 1992. Hypothesis: is eukaryotic initiation factor 2 the scanning factor? New Biol. 4, 404-407.
    • (1992) New Biol. , vol.4 , pp. 404-407
    • Thomas, A.A.1    Scheper, G.C.2    Voorma, H.O.3
  • 31
    • 0019889038 scopus 로고
    • Messenger ribonucleic acid specificity in the inhibition of eukaryotic translation by double-stranded ribonucleic acid
    • Rosen H., Knoller S., Kaempfer R. 1981. Messenger ribonucleic acid specificity in the inhibition of eukaryotic translation by double-stranded ribonucleic acid. Biochemistry. 20, 3011-3020.
    • (1981) Biochemistry , vol.20 , pp. 3011-3020
    • Rosen, H.1    Knoller, S.2    Kaempfer, R.3
  • 32
    • 0026039803 scopus 로고
    • RNA unwinding in translation: Assembly of helicase complex intermediates comprising eukaryotic initiation factors eIF-4F and eIF-4B
    • Jaramillo M., Dever T.E., Merrick W.C., Sonenberg N. 1991. RNA unwinding in translation: assembly of helicase complex intermediates comprising eukaryotic initiation factors eIF-4F and eIF-4B. Mol. Cell Biol. 11, 5992-5997.
    • (1991) Mol. Cell Biol. , vol.11 , pp. 5992-5997
    • Jaramillo, M.1    Dever, T.E.2    Merrick, W.C.3    Sonenberg, N.4


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