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Volumn 31, Issue 23, 2011, Pages 4814-4831

Functional elements in initiation factors 1, 1A, and 2β discriminate against poor AUG context and non-AUG start codons

Author keywords

[No Author keywords available]

Indexed keywords

INITIATION FACTOR; INITIATION FACTOR 1; INITIATION FACTOR 1A; INITIATION FACTOR 2BETA; NUCLEOTIDE; UNCLASSIFIED DRUG;

EID: 83255187893     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.05819-11     Document Type: Article
Times cited : (67)

References (50)
  • 1
    • 26944435515 scopus 로고    scopus 로고
    • i release from eIF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation
    • i release from eIF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation. Mol. Cell 20:251-262.
    • (2005) Mol. Cell , vol.20 , pp. 251-262
    • Algire, M.A.1    Maag, D.2    Lorsch, J.R.3
  • 2
    • 0023988840 scopus 로고
    • mRNA structures influencing translation in the yeast Saccharomyces cerevisiae
    • Baim, S. B., and F. Sherman. 1988. mRNA structures influencing translation in the yeast Saccharomyces cerevisiae. Mol. Cell. Biol. 8:1591-1601.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 1591-1601
    • Baim, S.B.1    Sherman, F.2
  • 3
    • 0023484186 scopus 로고
    • 5-fluoroorotic acid as a selective agent in yeast molecular genetics
    • Boeke, J. D., J. Trueheart, G. Natsoulis, and G. R. Fink. 1987. 5-fluoroorotic acid as a selective agent in yeast molecular genetics. Methods Enzymol. 154:164-175.
    • (1987) Methods Enzymol. , vol.154 , pp. 164-175
    • Boeke, J.D.1    Trueheart, J.2    Natsoulis, G.3    Fink, G.R.4
  • 4
    • 0027261221 scopus 로고
    • Guanine nucleotide exchange factor for eIF-2 in yeast: genetic and biochemical analysis of interactions between essential subunits GCD2, GCD6, and GCD7 and regulatory subunit GCN3
    • Bushman, J. L., M. Foiani, A. M. Cigan, C. J. Paddon, and A. G. Hinnebusch. 1993. Guanine nucleotide exchange factor for eIF-2 in yeast: genetic and biochemical analysis of interactions between essential subunits GCD2, GCD6, and GCD7 and regulatory subunit GCN3. Mol. Cell. Biol. 13:4618-4631.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4618-4631
    • Bushman, J.L.1    Foiani, M.2    Cigan, A.M.3    Paddon, C.J.4    Hinnebusch, A.G.5
  • 5
    • 0022887593 scopus 로고
    • Escherichia coli protein synthesis initiation factor IF3 controls its own gene expression at the translational level in vivo
    • Butler, J. S., M. Springer, J. Dondon, M. Graffe, and M. Grunberg-Manago. 1986. Escherichia coli protein synthesis initiation factor IF3 controls its own gene expression at the translational level in vivo. J. Mol. Biol. 192:767-780.
    • (1986) J. Mol. Biol. , vol.192 , pp. 767-780
    • Butler, J.S.1    Springer, M.2    Dondon, J.3    Graffe, M.4    Grunberg-Manago, M.5
  • 6
    • 2542445479 scopus 로고
    • AUU-to-AUG mutation in the initiator codon of the translation initiation factor IF3 abolishes translational autocontrol of its own gene (infC) in vivo
    • Butler, J. S., M. Springer, and M. Grunberg-Manago. 1987. AUU-to-AUG mutation in the initiator codon of the translation initiation factor IF3 abolishes translational autocontrol of its own gene (infC) in vivo. Proc. Natl. Acad. Sci. U. S. A. 84:4022-4025.
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 4022-4025
    • Butler, J.S.1    Springer, M.2    Grunberg-Manago, M.3
  • 7
    • 41249103979 scopus 로고    scopus 로고
    • Translational efficiency of a non-AUG initiation codon is significantly affected by its sequence context in yeast
    • Chen, S. J., G. Lin, K. J. Chang, L. S. Yeh, and C. C. Wang. 2008. Translational efficiency of a non-AUG initiation codon is significantly affected by its sequence context in yeast. J. Biol. Chem. 283:3173-3180.
    • (2008) J. Biol. Chem. , vol.283 , pp. 3173-3180
    • Chen, S.J.1    Lin, G.2    Chang, K.J.3    Yeh, L.S.4    Wang, C.C.5
  • 8
    • 34249069609 scopus 로고    scopus 로고
    • Dissociation of eIF1 from the 40S ribosomal subunit is a key step in start codon selection in vivo
    • Cheung, Y. N., et al. 2007. Dissociation of eIF1 from the 40S ribosomal subunit is a key step in start codon selection in vivo. Genes Dev. 21:1217-1230.
    • (2007) Genes Dev. , vol.21 , pp. 1217-1230
    • Cheung, Y.N.1
  • 9
    • 0033830375 scopus 로고    scopus 로고
    • Physical and functional interaction between the eukaryotic orthologs of prokaryotic translation initiation factors IF1 and IF2
    • Choi, S. K., et al. 2000. Physical and functional interaction between the eukaryotic orthologs of prokaryotic translation initiation factors IF1 and IF2. Mol. Cell. Biol. 20:7183-7191.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7183-7191
    • Choi, S.K.1
  • 10
    • 0024041075 scopus 로고
    • Mutational analysis of the HIS4 translational initiator region in Saccharomyces cerevisiae
    • Cigan, A. M., E. K. Pabich, and T. F. Donahue. 1988. Mutational analysis of the HIS4 translational initiator region in Saccharomyces cerevisiae. Mol. Cell. Biol. 8:2964-2975.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2964-2975
    • Cigan, A.M.1    Pabich, E.K.2    Donahue, T.F.3
  • 11
    • 0034759978 scopus 로고    scopus 로고
    • Interaction of translation initiation factor 3 with the 30S ribosomal subunit
    • Dallas, A., and H. F. Noller. 2001. Interaction of translation initiation factor 3 with the 30S ribosomal subunit. Mol. Cell 8:855-864.
    • (2001) Mol. Cell , vol.8 , pp. 855-864
    • Dallas, A.1    Noller, H.F.2
  • 12
    • 0002538063 scopus 로고    scopus 로고
    • Genetic approaches to translation initiation in Saccharomyces cerevisiae
    • N. Sonenberg, J. W. B. Hershey, and M. B. Mathews (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Donahue, T. 2000. Genetic approaches to translation initiation in Saccharomyces cerevisiae, p. 487-502. In N. Sonenberg, J. W. B. Hershey, and M. B. Mathews (ed.), Translational control of gene expression. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2000) Translational control of gene expression , pp. 487-502
    • Donahue, T.1
  • 13
    • 0024043324 scopus 로고
    • Genetic selection for mutations that reduce or abolish ribosomal recognition of the HIS4 translational initiator region
    • Donahue, T. F., and A. M. Cigan. 1988. Genetic selection for mutations that reduce or abolish ribosomal recognition of the HIS4 translational initiator region. Mol. Cell. Biol. 8:2955-2963.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2955-2963
    • Donahue, T.F.1    Cigan, A.M.2
  • 14
    • 33947595152 scopus 로고    scopus 로고
    • N-and C-terminal residues of eIF1A have opposing effects on the fidelity of start codon selection
    • Fekete, C. A., et al. 2007. N-and C-terminal residues of eIF1A have opposing effects on the fidelity of start codon selection. EMBO 26:1602-1614.
    • (2007) EMBO , vol.26 , pp. 1602-1614
    • Fekete, C.A.1
  • 15
    • 0033522507 scopus 로고    scopus 로고
    • Structure and interactions of the translation initiation factor eIF1
    • Fletcher, C. M., T. V. Pestova, C. U. T. Hellen, and G. Wagner. 1999. Structure and interactions of the translation initiation factor eIF1. EMBO J. 18:2631-2639.
    • (1999) EMBO J. , vol.18 , pp. 2631-2639
    • Fletcher, C.M.1    Pestova, T.V.2    Hellen, C.U.T.3    Wagner, G.4
  • 16
    • 0024266139 scopus 로고
    • New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • Gietz, R. D., and A. Sugino. 1988. New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene 74:527-534.
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2
  • 17
    • 0025018043 scopus 로고
    • Domains of initiator tRNA and initiation codon crucial for initiator tRNA selection by Escherichia coli IF3
    • Hartz, D., J. Binkley, T. Hollingsworth, and L. Gold. 1990. Domains of initiator tRNA and initiation codon crucial for initiator tRNA selection by Escherichia coli IF3. Genes Dev. 4:1790-1800.
    • (1990) Genes Dev. , vol.4 , pp. 1790-1800
    • Hartz, D.1    Binkley, J.2    Hollingsworth, T.3    Gold, L.4
  • 18
    • 0347416978 scopus 로고    scopus 로고
    • Genome-wide analysis of mRNAs regulated by the nonsense-mediated and 5to 3mRNA decay pathways in yeast
    • He, F., et al. 2003. Genome-wide analysis of mRNAs regulated by the nonsense-mediated and 5to 3mRNA decay pathways in yeast. Molecular Cell 12:1439-1452.
    • (2003) Molecular Cell , vol.12 , pp. 1439-1452
    • He, F.1
  • 19
    • 0021846299 scopus 로고
    • A hierarchy of trans-acting factors modulate translation of an activator of amino acid biosynthetic genes in Saccharomyces cerevisiae
    • Hinnebusch, A. G. 1985. A hierarchy of trans-acting factors modulate translation of an activator of amino acid biosynthetic genes in Saccharomyces cerevisiae. Mol. Cell. Biol. 5:2349-2360.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 2349-2360
    • Hinnebusch, A.G.1
  • 20
    • 34249665243 scopus 로고    scopus 로고
    • Mechanism of translation initiation in the yeast Saccharomyces cerevisiae
    • M. Mathews, N. Sonenberg, and J. W. B. Hershey (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Hinnebusch, A. G., T. E. Dever, and K. Asano. 2007. Mechanism of translation initiation in the yeast Saccharomyces cerevisiae, p. 225-268. In M. Mathews, N. Sonenberg, and J. W. B. Hershey (ed.), Translational control in biology and medicine. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2007) Translational control in biology and medicine , pp. 225-268
    • Hinnebusch, A.G.1    Dever, T.E.2    Asano, K.3
  • 21
    • 0030886675 scopus 로고    scopus 로고
    • GTP hydrolysis controls stringent selection of the AUG start codon during translation initiation in Saccharomyces cerevisiae
    • Huang, H., H. Yoon, E. M. Hannig, and T. F. Donahue. 1997. GTP hydrolysis controls stringent selection of the AUG start codon during translation initiation in Saccharomyces cerevisiae. Genes Dev. 11:2396-2413.
    • (1997) Genes Dev. , vol.11 , pp. 2396-2413
    • Huang, H.1    Yoon, H.2    Hannig, E.M.3    Donahue, T.F.4
  • 22
    • 78149277351 scopus 로고    scopus 로고
    • Initiation context modulates autoregulation of eukaryotic translation initiation factor 1 (eIF1)
    • Ivanov, I. P., G. Loughran, M. S. Sachs, and J. F. Atkins. 2010. Initiation context modulates autoregulation of eukaryotic translation initiation factor 1 (eIF1). Proc. Natl. Acad. Sci. U. S. A. 107:18056-18060.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 18056-18060
    • Ivanov, I.P.1    Loughran, G.2    Sachs, M.S.3    Atkins, J.F.4
  • 23
    • 0022552131 scopus 로고
    • Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes
    • Kozak, M. 1986. Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell 44:283-292.
    • (1986) Cell , vol.44 , pp. 283-292
    • Kozak, M.1
  • 24
    • 0024546509 scopus 로고
    • The scanning model for translation: an update
    • Kozak, M. 1989. The scanning model for translation: an update. J. Cell Biol. 108:229-241.
    • (1989) J. Cell Biol. , vol.108 , pp. 229-241
    • Kozak, M.1
  • 25
    • 0033055772 scopus 로고    scopus 로고
    • The cis-acting sequences responsible for the differential decay of the unstable MFA2 and stable PGK1 transcripts in yeast include the context of the translational start codon
    • LaGrandeur, T., and R. Parker. 1999. The cis-acting sequences responsible for the differential decay of the unstable MFA2 and stable PGK1 transcripts in yeast include the context of the translational start codon. RNA 5:420-433.
    • (1999) RNA , vol.5 , pp. 420-433
    • LaGrandeur, T.1    Parker, R.2
  • 26
    • 0027151981 scopus 로고
    • Translation of mRNAs with degenerate initiation triplet AUU displays high initiation factor 2 dependence and is subject to initiation factor 3 repression
    • La Teana, A., C. L. Pon, and C. O. Gualerzi. 1993. Translation of mRNAs with degenerate initiation triplet AUU displays high initiation factor 2 dependence and is subject to initiation factor 3 repression. Proc. Natl. Acad. Sci. U. S. A. 90:4161-4165.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 4161-4165
    • La Teana, A.1    Pon, C.L.2    Gualerzi, C.O.3
  • 27
    • 0345305759 scopus 로고    scopus 로고
    • Position of eukaryotic initiation factor eIF1 on the 40S ribosomal subunit determined by directed hydroxyl radical probing
    • Lomakin, I. B., V. G. Kolupaeva, A. Marintchev, G. Wagner, and T. V. Pestova. 2003. Position of eukaryotic initiation factor eIF1 on the 40S ribosomal subunit determined by directed hydroxyl radical probing. Genes Dev. 17:2786-2797.
    • (2003) Genes Dev. , vol.17 , pp. 2786-2797
    • Lomakin, I.B.1    Kolupaeva, V.G.2    Marintchev, A.3    Wagner, G.4    Pestova, T.V.5
  • 28
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine, M. S., et al. 1998. Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14:953-961.
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1
  • 29
    • 31344481752 scopus 로고    scopus 로고
    • Communication between eukaryotic translation initiation factors 5 and 1A within the ribosomal preinitiation complex plays a role in start site selection
    • Maag, D., M. A. Algire, and J. R. Lorsch. 2006. Communication between eukaryotic translation initiation factors 5 and 1A within the ribosomal preinitiation complex plays a role in start site selection. J. Mol. Biol. 356:724-737.
    • (2006) J. Mol. Biol. , vol.356 , pp. 724-737
    • Maag, D.1    Algire, M.A.2    Lorsch, J.R.3
  • 30
    • 12344314307 scopus 로고    scopus 로고
    • A conformational change in the eukaryotic translation preinitiation complex and release of eIF1 signal recognition of the start codon
    • Maag, D., C. A. Fekete, Z. Gryczynski, and J. R. Lorsch. 2005. A conformational change in the eukaryotic translation preinitiation complex and release of eIF1 signal recognition of the start codon. Mol. Cell 17:265-275.
    • (2005) Mol. Cell , vol.17 , pp. 265-275
    • Maag, D.1    Fekete, C.A.2    Gryczynski, Z.3    Lorsch, J.R.4
  • 31
    • 77952110724 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 1 (eIF1), the inspector of good AUG context for translation initiation, has an extremely bad AUG context
    • Miyasaka, H., S. Endo, and H. Shimizu. 2010. Eukaryotic translation initiation factor 1 (eIF1), the inspector of good AUG context for translation initiation, has an extremely bad AUG context. J. Biosci. Bioeng. 109:635-637.
    • (2010) J. Biosci. Bioeng. , vol.109 , pp. 635-637
    • Miyasaka, H.1    Endo, S.2    Shimizu, H.3
  • 32
    • 0026320245 scopus 로고
    • Association of RAP1 binding sites with stringent control of ribosomal protein gene transcription in Saccharomyces cerevisiae
    • Moehle, C. M., and A. G. Hinnebusch. 1991. Association of RAP1 binding sites with stringent control of ribosomal protein gene transcription in Saccharomyces cerevisiae. Mol. Cell. Biol. 11:2723-2735.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2723-2735
    • Moehle, C.M.1    Hinnebusch, A.G.2
  • 33
    • 70350557033 scopus 로고    scopus 로고
    • eIF1 controls multiple steps in start codon recognition during eukaryotic translation initiation
    • Nanda, J. S., et al. 2009. eIF1 controls multiple steps in start codon recognition during eukaryotic translation initiation. J. Mol. Biol. 394:268-285.
    • (2009) J. Mol. Biol. , vol.394 , pp. 268-285
    • Nanda, J.S.1
  • 34
    • 34047263278 scopus 로고    scopus 로고
    • The eukaryotic translation initiation factors eIF1 and eIF1A induce an open conformation of the 40S ribosome
    • Passmore, L. A., et al. 2007. The eukaryotic translation initiation factors eIF1 and eIF1A induce an open conformation of the 40S ribosome. Mol. Cell 26:41-50.
    • (2007) Mol. Cell , vol.26 , pp. 41-50
    • Passmore, L.A.1
  • 35
    • 0037112055 scopus 로고    scopus 로고
    • The roles of individual eukaryotic translation initiation factors in ribosomal scanning and initiation codon selection
    • Pestova, T. V., and V. G. Kolupaeva. 2002. The roles of individual eukaryotic translation initiation factors in ribosomal scanning and initiation codon selection. Genes Dev. 16:2906-2922.
    • (2002) Genes Dev. , vol.16 , pp. 2906-2922
    • Pestova, T.V.1    Kolupaeva, V.G.2
  • 36
    • 33846991130 scopus 로고    scopus 로고
    • The mechanism of translation initiation in eukaryotes
    • M. Mathews, N. Sonenberg, and J. W. B. Hershey (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Pestova, T. V., J. R. Lorsch, and C. U. T. Hellen. 2007. The mechanism of translation initiation in eukaryotes, p. 87-128. In M. Mathews, N. Sonenberg, and J. W. B. Hershey (ed.), Translational control in biology and medicine. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2007) Translational control in biology and medicine , pp. 87-128
    • Pestova, T.V.1    Lorsch, J.R.2    Hellen, C.U.T.3
  • 37
    • 33644779804 scopus 로고    scopus 로고
    • Specific functional interactions of nucleotides at key -3 and +4 positions flanking the initiation codon with components of the mammalian 48S translation initiation complex
    • Pisarev, A. V., et al. 2006. Specific functional interactions of nucleotides at key -3 and +4 positions flanking the initiation codon with components of the mammalian 48S translation initiation complex. Genes Dev. 20:624-636.
    • (2006) Genes Dev. , vol.20 , pp. 624-636
    • Pisarev, A.V.1
  • 38
    • 79951510534 scopus 로고    scopus 로고
    • Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1
    • Rabl, J., M. Leibundgut, S. F. Ataide, A. Haag, and N. Ban. 2011. Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1. Science 331:730-736.
    • (2011) Science , vol.331 , pp. 730-736
    • Rabl, J.1    Leibundgut, M.2    Ataide, S.F.3    Haag, A.4    Ban, N.5
  • 39
    • 0020479804 scopus 로고
    • Import of proteins into mitochondria: yeast cells grown in the presence of carbonyl cyanide m-chlorophenylhydrazone accumulate massive amounts of some mitochondrial precursor polypeptides
    • Reid, G. A., and G. Schatz. 1982. Import of proteins into mitochondria: yeast cells grown in the presence of carbonyl cyanide m-chlorophenylhydrazone accumulate massive amounts of some mitochondrial precursor polypeptides. J. Biol. Chem. 257:13056-13061.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13056-13061
    • Reid, G.A.1    Schatz, G.2
  • 40
    • 0029742167 scopus 로고    scopus 로고
    • The role of the AUU initiation codon in the negative feedback regulation of the gene for translation initiation factor IF3 in Escherichia coli
    • Sacerdot, C., et al. 1996. The role of the AUU initiation codon in the negative feedback regulation of the gene for translation initiation factor IF3 in Escherichia coli. Mol. Microbiol. 21:331-346.
    • (1996) Mol. Microbiol. , vol.21 , pp. 331-346
    • Sacerdot, C.1
  • 42
    • 0025362399 scopus 로고
    • A rapid and simple method for preparation of RNA from Saccharomyces cerevisiae
    • Schmitt, M. E., T. A. Brown, and B. L. Trumpower. 1990. A rapid and simple method for preparation of RNA from Saccharomyces cerevisiae. Nucleic Acids Res. 18:3091-3092.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 3091-3092
    • Schmitt, M.E.1    Brown, T.A.2    Trumpower, B.L.3
  • 43
    • 0032778953 scopus 로고    scopus 로고
    • Mutations in translation initiation factors lead to increased rates of deadenylation and decapping of mRNAs in Saccharomyces cerevisiae
    • Schwartz, D. C., and R. Parker. 1999. Mutations in translation initiation factors lead to increased rates of deadenylation and decapping of mRNAs in Saccharomyces cerevisiae. Mol. Cell. Biol. 19:5247-5256.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5247-5256
    • Schwartz, D.C.1    Parker, R.2
  • 44
    • 3042668591 scopus 로고    scopus 로고
    • Comparative analysis of orthologous eukaryotic mRNAs: potential hidden functional signals
    • Shabalina, S. A., A. Y. Ogurtsov, I. B. Rogozin, E. V. Koonin, and D. J. Lipman. 2004. Comparative analysis of orthologous eukaryotic mRNAs: potential hidden functional signals. Nucleic Acids Res. 32:1774-1782.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1774-1782
    • Shabalina, S.A.1    Ogurtsov, A.Y.2    Rogozin, I.B.3    Koonin, E.V.4    Lipman, D.J.5
  • 45
    • 0029745401 scopus 로고    scopus 로고
    • Escherichia coli translation initiation factor 3 discriminates the initiation codon in vivo
    • Sussman, J. K., E. L. Simons, and R. W. Simons. 1996. Escherichia coli translation initiation factor 3 discriminates the initiation codon in vivo. Mol. Microbiol. 21:347-360.
    • (1996) Mol. Microbiol. , vol.21 , pp. 347-360
    • Sussman, J.K.1    Simons, E.L.2    Simons, R.W.3
  • 46
    • 79951524206 scopus 로고    scopus 로고
    • Identification of compounds that decrease the fidelity of start codon recognition by the eukaryotic translational machinery
    • Takacs, J. E., et al. 2011. Identification of compounds that decrease the fidelity of start codon recognition by the eukaryotic translational machinery. RNA 17:439-452.
    • (2011) RNA , vol.17 , pp. 439-452
    • Takacs, J.E.1
  • 47
    • 0032896616 scopus 로고    scopus 로고
    • Translation initiation factor 3 antagonizes authentic start codon selection on leaderless mRNAs
    • Tedin, K., et al. 1999. Translation initiation factor 3 antagonizes authentic start codon selection on leaderless mRNAs. Mol. Microbiol. 31:67-77.
    • (1999) Mol. Microbiol. , vol.31 , pp. 67-77
    • Tedin, K.1
  • 48
    • 6344291066 scopus 로고    scopus 로고
    • Interactions of eukaryotic translation initiation factor 3 (eIF3) subunit NIP1/c with eIF1 and eIF5 promote preinitiation complex assembly and regulate start codon selection
    • Valasek, L., K. H. Nielsen, F. Zhang, C. A. Fekete, and A. G. Hinnebusch. 2004. Interactions of eukaryotic translation initiation factor 3 (eIF3) subunit NIP1/c with eIF1 and eIF5 promote preinitiation complex assembly and regulate start codon selection. Mol. Cell. Biol. 24:9437-9455.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9437-9455
    • Valasek, L.1    Nielsen, K.H.2    Zhang, F.3    Fekete, C.A.4    Hinnebusch, A.G.5
  • 49
    • 0026609868 scopus 로고
    • The sui1 suppressor locus in Saccharomyces cerevisiae encodes a translation factor that functions during tRNAi Met recognition of the start codon
    • Yoon, H. J., and T. F. Donahue. 1992. The sui1 suppressor locus in Saccharomyces cerevisiae encodes a translation factor that functions during tRNAi Met recognition of the start codon. Mol. Cell. Biol. 12:248-260.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 248-260
    • Yoon, H.J.1    Donahue, T.F.2
  • 50
    • 0242721615 scopus 로고    scopus 로고
    • Recruitment of SWI/SNF by Gcn4p does not require Snf2p or Gcn5p but depends strongly on SWI/SNF integrity, SRB mediator, and SAGA
    • Yoon, S., H. Qiu, M. J. Swanson, and A. G. Hinnebusch. 2003. Recruitment of SWI/SNF by Gcn4p does not require Snf2p or Gcn5p but depends strongly on SWI/SNF integrity, SRB mediator, and SAGA. Mol. Cell. Biol. 23:8829-8845.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8829-8845
    • Yoon, S.1    Qiu, H.2    Swanson, M.J.3    Hinnebusch, A.G.4


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