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Volumn 25, Issue 13, 2005, Pages 5480-5491

Eukaryotic translation initiation factor 5 is critical for integrity of the scanning preinitiation complex and accurate control of GCN4 translation

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; AROMATIC CARBOXYLIC ACID; GUANOSINE TRIPHOSPHATE; INITIATION FACTOR 5; METHIONINE TRANSFER RNA; TRANSCRIPTION FACTOR GCN4;

EID: 20744451862     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.25.13.5480-5491.2005     Document Type: Article
Times cited : (42)

References (44)
  • 1
    • 0033828440 scopus 로고    scopus 로고
    • Eukaryote-specific domains in translation initiation factors: Implications for translation regulation and evolution of the translation system
    • Aravind, L., and E. V. Koonin. 2000. Eukaryote-specific domains in translation initiation factors: implications for translation regulation and evolution of the translation system. Genome Res. 10:1172-1184.
    • (2000) Genome Res. , vol.10 , pp. 1172-1184
    • Aravind, L.1    Koonin, E.V.2
  • 3
    • 0033559265 scopus 로고    scopus 로고
    • Conserved bipartite motifs in yeast eIF5 and eIF2Bε, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2
    • Asano, K., T. Krishnamoorthy, L. Phan, G. D. Pavill, and A. G. Hinnebusch. 1999. Conserved bipartite motifs in yeast eIF5 and eIF2Bε, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2. EMBO J. 18:1673-1688.
    • (1999) EMBO J. , vol.18 , pp. 1673-1688
    • Asano, K.1    Krishnamoorthy, T.2    Phan, L.3    Pavill, G.D.4    Hinnebusch, A.G.5
  • 4
    • 0032541138 scopus 로고    scopus 로고
    • Complex formation by all five homologues of mammalian translation initiation factor 3 subunits from yeast Saccharomyces cerevisiae
    • Asano, K., L. Phan, J. Anderson, and A. G. Hinnebusch. 1998. Complex formation by all five homologues of mammalian translation initiation factor 3 subunits from yeast Saccharomyces cerevisiae. J. Biol. Chem. 273:18573-18585.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18573-18585
    • Asano, K.1    Phan, L.2    Anderson, J.3    Hinnebusch, A.G.4
  • 5
    • 0035341204 scopus 로고    scopus 로고
    • Multiple roles for the carboxyl terminal domain of eIF5 in translation initiation complex assembly and GTPase activation
    • Asano, K., A. Shalev, L. Phan, K. Nielsen, J. Clayton, L. Valasek, T. F. Donahue, and A. G. Hinnebusch. 2001. Multiple roles for the carboxyl terminal domain of eIF5 in translation initiation complex assembly and GTPase activation. EMBO J. 20:2326-2337.
    • (2001) EMBO J. , vol.20 , pp. 2326-2337
    • Asano, K.1    Shalev, A.2    Phan, L.3    Nielsen, K.4    Clayton, J.5    Valasek, L.6    Donahue, T.F.7    Hinnebusch, A.G.8
  • 6
    • 0023484186 scopus 로고
    • 5-Fluoroorotic acid as a selective agent in yeast molecular genes
    • Boeke, J. D., J. Trueheart, G. Natsoulis, and G. R. Fink. 1987. 5-Fluoroorotic acid as a selective agent in yeast molecular genes. 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
  • 7
    • 1542368830 scopus 로고    scopus 로고
    • Structure of the catalytic fragment of translation initiation factor 2B and identification of a critically important catalytic residue
    • Boesen, T., S. S. Mohammad, G. D. Pavitt, and G. R. Andersen. 2004. Structure of the catalytic fragment of translation initiation factor 2B and identification of a critically important catalytic residue. J. Biol. Chem. 279:10584-10592.
    • (2004) J. Biol. Chem. , vol.279 , pp. 10584-10592
    • Boesen, T.1    Mohammad, S.S.2    Pavitt, G.D.3    Andersen, G.R.4
  • 8
    • 0027411601 scopus 로고
    • Evidence that GCD6 and GCD7, translational regulators of GCN4, are subunits of the guanine nucleotide exchange factor for eIF-2 in Saccharomyces cerevisiae
    • Bushman, J. L., A. I. Asuru, R. L. Matts, and A. G. Hinnebusch. 1993. Evidence that GCD6 and GCD7, translational regulators of GCN4, are subunits of the guanine nucleotide exchange factor for eIF-2 in Saccharomyces cerevisiae. Mol. Cell. Biol. 13:1920-1932.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1920-1932
    • Bushman, J.L.1    Asuru, A.I.2    Matts, R.L.3    Hinnebusch, A.G.4
  • 9
    • 0027318447 scopus 로고
    • Eukaryotic translation initiation factor 5 from Saccharomyces cerevisiae: Cloning, characterization, and expression of the gene encoding the 45,346-Da protein
    • Chakravarti, D., and U. Maitra. 1993. Eukaryotic translation initiation factor 5 from Saccharomyces cerevisiae: cloning, characterization, and expression of the gene encoding the 45,346-Da protein. J. Biol. Chem. 268:10524-10533.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10524-10533
    • Chakravarti, D.1    Maitra, U.2
  • 11
    • 0035794125 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 5 functions as a GTPase activating protein
    • Das, S., R. Ghosh, and U. Maitra. 2001. Eukaryotic translation initiation factor 5 functions as a GTPase activating protein. J. Biol. Chem. 276:6720-6726.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6720-6726
    • Das, S.1    Ghosh, R.2    Maitra, U.3
  • 12
    • 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
  • 14
    • 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
  • 15
    • 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
  • 16
    • 0036790688 scopus 로고    scopus 로고
    • Characterization of the minimal catalytic domain within eIF2B: The guanine-nucleotide exchange factor for translation initiation
    • Gomez, E., S. S. Mohammad, and G. P. Pavitt. 2002. Characterization of the minimal catalytic domain within eIF2B: the guanine-nucleotide exchange factor for translation initiation. EMBO J. 21:5292-5301.
    • (2002) EMBO J. , vol.21 , pp. 5292-5301
    • Gomez, E.1    Mohammad, S.S.2    Pavitt, G.P.3
  • 17
    • 0028012044 scopus 로고
    • Effect of sequence context at stop codons on efficiency of reinitiation in GCN4 translational control
    • Grant, C. M., and A. G. Hinnebusch. 1994. Effect of sequence context at stop codons on efficiency of reinitiation in GCN4 translational control. Mol. Cell. Biol. 14:606-618.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 606-618
    • Grant, C.M.1    Hinnebusch, A.G.2
  • 18
    • 0027459940 scopus 로고
    • GCD11, a negative regulator of GCN4 expression, encodes the γ subunit of eIF-2 in Saccharomyces cerevisiae
    • Hannig, E. M., A. M. Cigan, B. A. Freeman, and T. G. Kinzy. 1992. GCD11, a negative regulator of GCN4 expression, encodes the γ subunit of eIF-2 in Saccharomyces cerevisiae. Mol. Cell. Biol. 13:506-520.
    • (1992) Mol. Cell. Biol. , vol.13 , pp. 506-520
    • Hannig, E.M.1    Cigan, A.M.2    Freeman, B.A.3    Kinzy, T.G.4
  • 19
    • 0023797126 scopus 로고
    • Molecular analysis of GCN3, a translational activator of GCN4: Evidence for posttranslational control of GCN3 regulatory function
    • Hannig, E. M., and A. G. Hinnebusch. 1988. Molecular analysis of GCN3, a translational activator of GCN4: evidence for posttranslational control of GCN3 regulatory function. Mol. Cell. Biol. 8:4808-4820.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4808-4820
    • Hannig, E.M.1    Hinnebusch, A.G.2
  • 20
    • 0041589832 scopus 로고    scopus 로고
    • The yeast eukaryotic initiation factor 4G (eIF4G) HEAT domain interacts with eIF1 and eIF5 and is involved in stringent AUG selection
    • He, H., T. von der Haar, R. C. Singh, M. Ii, B. Li, J. E. G. McCarthy, A. G. Hinnebusch, and K. Asano. 2003. The yeast eukaryotic initiation factor 4G (eIF4G) HEAT domain interacts with eIF1 and eIF5 and is involved in stringent AUG selection. Mol. Cell. Biol. 23:5431-5445.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5431-5445
    • He, H.1    Von Der Haar, T.2    Singh, R.C.3    Ii, M.4    Li, B.5    McCarthy, J.E.G.6    Hinnebusch, A.G.7    Asano, K.8
  • 21
    • 0031024024 scopus 로고    scopus 로고
    • eIF4G: A multipurpose ribosome adapter
    • Hentze, M. W. 1997. eIF4G: a multipurpose ribosome adapter. Science 275:500-501.
    • (1997) Science , vol.275 , pp. 500-501
    • Hentze, M.W.1
  • 22
    • 0000091608 scopus 로고    scopus 로고
    • Pathway and mechanism of initiation of protein synthesis
    • N. Sonenberg, J. W. B. Hershey, and M. B. Mathews (ed.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Hershey, J. W. B., and W. C. Merrick. 2000. Pathway and mechanism of initiation of protein synthesis, p. 33-88. 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, N.Y.
    • (2000) Translational Control of Gene Expression , pp. 33-88
    • Hershey, J.W.B.1    Merrick, W.C.2
  • 23
    • 0030803256 scopus 로고    scopus 로고
    • Translational regulation of yeast GCN4: A window on factors that control initiator-tRNA binding to the ribosome
    • Hinnebusch, A. G. 1997. Translational regulation of yeast GCN4: a window on factors that control initiator-tRNA binding to the ribosome. J. Biol. Chem. 272:21661-21664.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21661-21664
    • Hinnebusch, A.G.1
  • 24
    • 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
  • 25
    • 0029144599 scopus 로고
    • Multidomain organization of eukaryotic guanine nucleotide exchange translation initiation factor eIF-2B subunits revealed by analysis of conserved sequence motifs
    • Koonin, E. V. 1995. Multidomain organization of eukaryotic guanine nucleotide exchange translation initiation factor eIF-2B subunits revealed by analysis of conserved sequence motifs. Protein Sci. 4:1608-1617.
    • (1995) Protein Sci. , vol.4 , pp. 1608-1617
    • Koonin, E.V.1
  • 26
    • 0023425901 scopus 로고
    • Effects of intercistronic length on the efficiency of reinitiation by eukaryotic ribosomes
    • Kozak, M. 1987. Effects of intercistronic length on the efficiency of reinitiation by eukaryotic ribosomes. Mol. Cell. Biol. 7:3438-3445.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 3438-3445
    • Kozak, M.1
  • 27
    • 0033061571 scopus 로고    scopus 로고
    • Initiation of translation in prokaryotes and eukaryotes
    • Kozak, M. 1999. Initiation of translation in prokaryotes and eukaryotes. Gene 234:187-208.
    • (1999) Gene , vol.234 , pp. 187-208
    • Kozak, M.1
  • 28
    • 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
  • 29
    • 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
  • 30
    • 0033957406 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 4E (eIF4E) binding site and the middle one-third of eIF4GI constitute the core domain for cap-dependent translation, and the C-terminal one-third functions as a modulatory region
    • Merino, S., H. Imataka, Y. V. Svitkin, T. V. Pestova, and N. Sonenberg. 2000. Eukaryotic translation initiation factor 4E (eIF4E) binding site and the middle one-third of eIF4GI constitute the core domain for cap-dependent translation, and the C-terminal one-third functions as a modulatory region. Mol. Cell. Biol. 20:468-477.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 468-477
    • Merino, S.1    Imataka, H.2    Svitkin, Y.V.3    Pestova, T.V.4    Sonenberg, N.5
  • 31
    • 0034459468 scopus 로고    scopus 로고
    • Upstream open reading frames as regulators of mRNA translation
    • Morris, D. R., and A. P. Geballe. 2000. Upstream open reading frames as regulators of mRNA translation. Mol. Cell. Biol. 20:8635-8642.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8635-8642
    • Morris, D.R.1    Geballe, A.P.2
  • 32
    • 0022512237 scopus 로고
    • Multiple upstream AUG codons mediate translational control of GCN4
    • Mueller, P. P., and A. G. Hinnebusch. 1986. Multiple upstream AUG codons mediate translational control of GCN4. Cell 45:201-207.
    • (1986) Cell , vol.45 , pp. 201-207
    • Mueller, P.P.1    Hinnebusch, A.G.2
  • 33
    • 0034973590 scopus 로고    scopus 로고
    • Transcriptional profiling shows that Gcn4p is a master regulator of gene expression during amino acid starvation in yeast
    • Matarajan, K., M. R. Meyer, B. M. Jackson, D. Slade, C. Roberts, A. G. Hinnebusch, and M. J. Marton. 2001. Transcriptional profiling shows that Gcn4p is a master regulator of gene expression during amino acid starvation in yeast. Mol. Cell. Biol. 21:4347-4368.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 4347-4368
    • Matarajan, K.1    Meyer, M.R.2    Jackson, B.M.3    Slade, D.4    Roberts, C.5    Hinnebusch, A.G.6    Marton, M.J.7
  • 34
    • 1842576663 scopus 로고    scopus 로고
    • Functions of eIF3 downstream of 48S assembly impact AUG recognition and GCN4 translational control
    • Nielsen, K. H., B. Szamecz, L. Valasek, A. Jivotovskaya, B. S. Shin, and A. G. Hinnebusch. 2004. Functions of eIF3 downstream of 48S assembly impact AUG recognition and GCN4 translational control. EMBO J. 23:1166-1177.
    • (2004) EMBO J. , vol.23 , pp. 1166-1177
    • Nielsen, K.H.1    Szamecz, B.2    Valasek, L.3    Jivotovskaya, A.4    Shin, B.S.5    Hinnebusch, A.G.6
  • 35
    • 0035929148 scopus 로고    scopus 로고
    • A plant viral "reinitiation" factor interacts with the host translational machinery
    • Park, H.-S., A. Himmelbach, K. S. Browning, T. Hohn, and L. A. Ryabova. 2001. A plant viral "reinitiation" factor interacts with the host translational machinery. Cell 106:723-733.
    • (2001) Cell , vol.106 , pp. 723-733
    • Park, H.-S.1    Himmelbach, A.2    Browning, K.S.3    Hohn, T.4    Ryabova, L.A.5
  • 36
    • 0035191271 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 5 (eIF5) acts as a classical GTPase-activator protein
    • Paulin, F. E., L. E. Campbell, K. O'Brien, J. Loughlin, and C. G. Proud. 2001. Eukaryotic translation initiation factor 5 (eIF5) acts as a classical GTPase-activator protein. Curr. Biol. 11:55-59.
    • (2001) Curr. Biol. , vol.11 , pp. 55-59
    • Paulin, F.E.1    Campbell, L.E.2    O'Brien, K.3    Loughlin, J.4    Proud, C.G.5
  • 39
    • 0037184985 scopus 로고    scopus 로고
    • Uncoupling of initiation factor eIF5B/IF2 GTPase and translational activities by mutations that lower ribosome affinity
    • Shin, B. S., D. Maag, A. Roll-Mecak, M. S. Arefin, S. K. Burley, J. R. Lorsch, and T. E. Dever. 2002. Uncoupling of initiation factor eIF5B/IF2 GTPase and translational activities by mutations that lower ribosome affinity. Cell 111:1015-1025.
    • (2002) Cell , vol.111 , pp. 1015-1025
    • Shin, B.S.1    Maag, D.2    Roll-Mecak, A.3    Arefin, M.S.4    Burley, S.K.5    Lorsch, J.R.6    Dever, T.E.7
  • 40
    • 9644291558 scopus 로고    scopus 로고
    • Physical association of eukaryotic initiation factor 5 (eIF5) carboxyl terminal domain with the lysine-rich eIF2β segment strongly enhances its binding to eIF3
    • Singh, C. R., Y. Yamamoto, and K. Asano. 2004. Physical association of eukaryotic initiation factor 5 (eIF5) carboxyl terminal domain with the lysine-rich eIF2β segment strongly enhances its binding to eIF3. J. Biol. Chem. 279:49644-49655.
    • (2004) J. Biol. Chem. , vol.279 , pp. 49644-49655
    • Singh, C.R.1    Yamamoto, Y.2    Asano, K.3
  • 41
    • 3843096103 scopus 로고    scopus 로고
    • Efficient incorporation of eIF1 into the multifactor complex is critical for formation of functional ribosomal preinitiation complexes in vivo
    • Singh, C. R., H. Hui, M. Ii, Y. Yamamoto, and K. Asano. 2004. Efficient incorporation of eIF1 into the multifactor complex is critical for formation of functional ribosomal preinitiation complexes in vivo. J. Biol. Chem. 279:31910-31920.
    • (2004) J. Biol. Chem. , vol.279 , pp. 31910-31920
    • Singh, C.R.1    Hui, H.2    Ii, M.3    Yamamoto, Y.4    Asano, K.5
  • 42
    • 0026752980 scopus 로고
    • Eukaryotic initiation factor 3 does not prevent association through physical blockage of the ribosomal subunit-subunit interface
    • Srivastava, S., A. Verschoor, and J. Frank. 1992. Eukaryotic initiation factor 3 does not prevent association through physical blockage of the ribosomal subunit-subunit interface. J. Mol. Biol. 220:301-304.
    • (1992) J. Mol. Biol. , vol.220 , pp. 301-304
    • Srivastava, S.1    Verschoor, A.2    Frank, J.3
  • 43
    • 0037444342 scopus 로고    scopus 로고
    • The yeast eIF3 subunits TIF32/a, NIP1/c, and eIF5 make critical connections with the 40S ribosome in vivo
    • Valášek, L., A. A. Mathew, B. S. Shin, K. H. Nielsen, B. Szamecz, and A. G. Hinnebusch. 2003. The yeast eIF3 subunits TIF32/a, NIP1/c, and eIF5 make critical connections with the 40S ribosome in vivo. Genes Dev. 17:786-799.
    • (2003) Genes Dev. , vol.17 , pp. 786-799
    • Valášek, L.1    Mathew, A.A.2    Shin, B.S.3    Nielsen, K.H.4    Szamecz, B.5    Hinnebusch, A.G.6
  • 44
    • 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
    • Valášek, 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
    • Valášek, L.1    Nielsen, K.H.2    Zhang, F.3    Fekete, C.A.4    Hinnebusch, A.G.5


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