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Volumn 17, Issue 6, 2003, Pages 786-799

The yeast eIF3 subunits TIF32/a, NIP1/c, and eIF5 make critical connections with the 40S ribosome in vivo

Author keywords

40S ribosome binding; Eukaryotic translation initiation factor (eIF); Multifactor complex (MFC); Protein synthesis; TIF32 NIP1; Translational control

Indexed keywords

INITIATION FACTOR; INITIATION FACTOR 1; INITIATION FACTOR 2; INITIATION FACTOR 3; INITIATION FACTOR 5; PROTEIN SUBUNIT; SOLVENT; TRANSFER RNA; UNCLASSIFIED DRUG;

EID: 0037444342     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.1065403     Document Type: Article
Times cited : (127)

References (32)
  • 1
    • 0032541138 scopus 로고    scopus 로고
    • Complex formation by all five homologues of mammalian translation initiation factor 3 subunits from yeast Saccharomyces cerevisiae
    • Asano, K., Phan, L., Anderson, J., and Hinnebusch, A.G. 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
  • 2
    • 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., Krishnamoorthy, T., Phan, L., Pavitt, G.D., and Hinnebusch, A.G. 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    Pavitt, G.D.4    Hinnebusch, A.G.5
  • 4
    • 0035341204 scopus 로고    scopus 로고
    • Multiple roles for the carboxyl terminal domain of eIF5 in translation initiation complex assembly and GTPase activation
    • Asano, K., Shalev, A., Phan, L., Nielsen, K., Clayton, J., Valášek, L., Donahue, T.F., and Hinnebusch, A.G. 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    Valášek, L.6    Donahue, T.F.7    Hinnebusch, A.G.8
  • 5
    • 0026043416 scopus 로고
    • Eukaryotic initiation factors eIF-2 and elF-3: Interactions, structure and localization in ribosomal initiation complexes
    • Bommer, U.A., Lutsch, G., Stahl, J., and Bielka, H. 1991. Eukaryotic initiation factors eIF-2 and elF-3: Interactions, structure and localization in ribosomal initiation complexes. Biochimie 73: 1007-1019.
    • (1991) Biochimie , vol.73 , pp. 1007-1019
    • Bommer, U.A.1    Lutsch, G.2    Stahl, J.3    Bielka, H.4
  • 7
    • 0028947302 scopus 로고
    • Isolation of a protein complex containing translation initiation factor Prt1 from Saccharomyces cerevisiae
    • Danaie, P., Wittmer, B., Altmann, M., and Trachsel, H. 1995, Isolation of a protein complex containing translation initiation factor Prt1 from Saccharomyces cerevisiae. J. Biol. Chem. 270: 4288-4292.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4288-4292
    • Danaie, P.1    Wittmer, B.2    Altmann, M.3    Trachsel, H.4
  • 8
    • 0000091608 scopus 로고    scopus 로고
    • Pathway and mechanism of initiation of protein synthesis
    • eds. N. Sonenberg et al. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Hershey, J.W.B. and Merrick, W.C. 2000. Pathway and mechanism of initiation of protein synthesis. In Translational control of gene expression (eds. N. Sonenberg et al.), pp. 33-88. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2000) Translational Control of Gene Expression , pp. 33-88
    • Hershey, J.W.B.1    Merrick, W.C.2
  • 9
    • 0002470681 scopus 로고    scopus 로고
    • Mechanism and regulation of initiator methionyl-tRNA binding to ribosomes
    • eds. N. Sonenberg et al. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Hinnebusch, A.G. 2000. Mechanism and regulation of initiator methionyl-tRNA binding to ribosomes. In Translational control of gene expression (eds. N. Sonenberg et al.), pp. 185-243. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2000) Translational Control of Gene Expression , pp. 185-243
    • Hinnebusch, A.G.1
  • 10
    • 0030886675 scopus 로고    scopus 로고
    • GTP hydrolysis controls stringent selection of the AUG start codon during translation initiation in Saccharomyces cerevisiae
    • Huang, H., Yoon, H., Hannig, E.M., and Donahue, T.F. 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
  • 11
    • 0035260658 scopus 로고    scopus 로고
    • Mechanism of ribosome recruitment by hepatitis C IRES RNA
    • Kieft, J.S., Zhou, K., Jubin, R., and Doudna, J.A. 2001. Mechanism of ribosome recruitment by hepatitis C IRES RNA. RNA 7: 194-206.
    • (2001) RNA , vol.7 , pp. 194-206
    • Kieft, J.S.1    Zhou, K.2    Jubin, R.3    Doudna, J.A.4
  • 12
    • 0022704950 scopus 로고
    • Structure and location of initiation factor eIF-3 within native small ribosomal subunits from eukaryotes
    • Lutsch, G., Benndorf, R., Westermann, P., Bommer, U.A., and Bielka, H. 1986. Structure and location of initiation factor eIF-3 within native small ribosomal subunits from eukaryotes. Eur. J. Cell Biol. 40: 257-265.
    • (1986) Eur. J. Cell Biol. , vol.40 , pp. 257-265
    • Lutsch, G.1    Benndorf, R.2    Westermann, P.3    Bommer, U.A.4    Bielka, H.5
  • 13
    • 0032544922 scopus 로고    scopus 로고
    • Binding of Escherichia coli initiation factor IF2 to 30S ribosomal subunits: A functional role for the N-terminus of the factor
    • Moreno, J.M., Kildsgaard, J., Siwanowicz, I., Mortensen, K.K., and Sperling-Petersen, H.U. 1998. Binding of Escherichia coli initiation factor IF2 to 30S ribosomal subunits: A functional role for the N-terminus of the factor. Biochem. Biophys. Res. Commun. 252: 465-471.
    • (1998) Biochem. Biophys. Res. Commun. , vol.252 , pp. 465-471
    • Moreno, J.M.1    Kildsgaard, J.2    Siwanowicz, I.3    Mortensen, K.K.4    Sperling-Petersen, H.U.5
  • 14
    • 0037439198 scopus 로고    scopus 로고
    • Domains of eIF1A that mediate binding to eIF2, eIF3 and eIF5B and promote ternary complex recruitment in vivo
    • Olsen, D.S., Savner, E.M., Mathew, A., Zhang, F., Krishnamoorthy, T., Phan, L., and Hinnebusch, A.G. 2002. Domains of eIF1A that mediate binding to eIF2, eIF3 and eIF5B and promote ternary complex recruitment in vivo. EMBO J. 22: 193-204.
    • (2002) EMBO J. , vol.22 , pp. 193-204
    • Olsen, D.S.1    Savner, E.M.2    Mathew, A.3    Zhang, F.4    Krishnamoorthy, T.5    Phan, L.6    Hinnebusch, A.G.7
  • 15
    • 0037112055 scopus 로고    scopus 로고
    • The roles of individual eukaryotic translation initiation factors in ribosomal scanning and initiation codon selection
    • Pestova, T.V. and Kolupaeva, V.G. 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
  • 16
    • 0032572776 scopus 로고    scopus 로고
    • Eukaryotic ribosomes require initiation factors 1 and 1A to locate initiation codons
    • Pestova, T.V., Borukhov, S.I., and Hellen, C.U.T. 1998. Eukaryotic ribosomes require initiation factors 1 and 1A to locate initiation codons. Nature 394: 854-859.
    • (1998) Nature , vol.394 , pp. 854-859
    • Pestova, T.V.1    Borukhov, S.I.2    Hellen, C.U.T.3
  • 17
    • 0031876171 scopus 로고    scopus 로고
    • Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5
    • Phan, L., Zhang, X., Asano, K., Anderson, J., Vornlocher, H.P., Greenberg, J.R., Qin, J., and Hinnebusch, A.G. 1998. Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5. Mol. Cell. Biol. 18: 4935-4946.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4935-4946
    • Phan, L.1    Zhang, X.2    Asano, K.3    Anderson, J.4    Vornlocher, H.P.5    Greenberg, J.R.6    Qin, J.7    Hinnebusch, A.G.8
  • 19
    • 0028926048 scopus 로고
    • Protein-protein interactions: Methods for detection and analysis
    • Phizicky, E.M. and Fields, S. 1995. Protein-protein interactions: Methods for detection and analysis. Microbiol. Rev. 59: 94-123.
    • (1995) Microbiol. Rev. , vol.59 , pp. 94-123
    • Phizicky, E.M.1    Fields, S.2
  • 20
    • 0032579887 scopus 로고    scopus 로고
    • The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae
    • Planta, R.J. and Mager, W.H. 1998. The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae. Yeast 14:471-477.
    • (1998) Yeast , vol.14 , pp. 471-477
    • Planta, R.J.1    Mager, W.H.2
  • 21
    • 0025375223 scopus 로고
    • Major determinants of the specificity of interaction between small nuclear ribonucleoproteins U1 A and U2B″ and their cognate RNAs
    • Scherly, D., Boelens, W., Dathan, N.A., van Venrooij, W.J., and Mattaj, I.W. 1990. Major determinants of the specificity of interaction between small nuclear ribonucleoproteins U1 A and U2B″ and their cognate RNAs. Nature 345: 502-506.
    • (1990) Nature , vol.345 , pp. 502-506
    • Scherly, D.1    Boelens, W.2    Dathan, N.A.3    Van Venrooij, W.J.4    Mattaj, I.W.5
  • 22
    • 0037007203 scopus 로고    scopus 로고
    • The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors
    • Schmitt, E., Blanquet, S., and Mechulam, Y. 2002. The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors. EMBO J. 21: 1821-1832.
    • (2002) EMBO J. , vol.21 , pp. 1821-1832
    • Schmitt, E.1    Blanquet, S.2    Mechulam, Y.3
  • 23
    • 0031901132 scopus 로고    scopus 로고
    • Specific interaction of eukaryotic translation initiation factor 3 with the 5′ nontranslated regions of hepatitis C virus and classical swine fever RNAs
    • Sizova, D.V., Kolupaeva, V.G., Pestova, T.V., Shatsky, I.N., and Hellen, C.U. 1998. Specific interaction of eukaryotic translation initiation factor 3 with the 5′ nontranslated regions of hepatitis C virus and classical swine fever RNAs. J. Virology 72:4775-4782.
    • (1998) J. Virology , vol.72 , pp. 4775-4782
    • Sizova, D.V.1    Kolupaeva, V.G.2    Pestova, T.V.3    Shatsky, I.N.4    Hellen, C.U.5
  • 24
    • 0035798380 scopus 로고    scopus 로고
    • Structure of the 80S ribosome from Saccharomyces cerevisiae - tRNA-ribosome and sub-unit-subunit interactions
    • Spahn, C.M., Beckmann, R., Eswar, N., Penczek, P.A., Sali, A., Blobel, G., and Frank, J. 2001a. Structure of the 80S ribosome from Saccharomyces cerevisiae - tRNA-ribosome and sub-unit-subunit interactions. Cell 107: 373-386.
    • (2001) Cell , vol.107 , pp. 373-386
    • Spahn, C.M.1    Beckmann, R.2    Eswar, N.3    Penczek, P.A.4    Sali, A.5    Blobel, G.6    Frank, J.7
  • 25
    • 0035831269 scopus 로고    scopus 로고
    • Hepatitis C virus IRES RNA-induced changes in the conformation of the 40S ribosomal subunit
    • Spahn, C.M., Kieft, J.S., Grassucci, R.A., Penczek, P.A., Zhou, K., Doudna, J.A., and Frank, J. 2001b. Hepatitis C virus IRES RNA-induced changes in the conformation of the 40S ribosomal subunit. Science 291: 1959-1962.
    • (2001) Science , vol.291 , pp. 1959-1962
    • Spahn, C.M.1    Kieft, J.S.2    Grassucci, R.A.3    Penczek, P.A.4    Zhou, K.5    Doudna, J.A.6    Frank, J.7
  • 26
    • 0026752980 scopus 로고
    • Eukaryotic initiation factor 3 does not prevent association through physical blockage of the ribosomal subunit-subunit interface
    • Srivastava, S., Verschoor, A., and Frank, J. 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
  • 27
    • 0035900747 scopus 로고    scopus 로고
    • Dual function of eIF3j/Hcr1p in processing 20 S pre-rRNA and translation initiation
    • Valášek, L., Hašek, J., Nielsen, K.H., and Hinnebusch, A.G. 2001a. Dual function of eIF3j/Hcr1p in processing 20 S pre-rRNA and translation initiation. J. Biol. Chem. 276: 43351-43360.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43351-43360
    • Valášek, L.1    Hašek, J.2    Nielsen, K.H.3    Hinnebusch, A.G.4
  • 28
    • 0035865256 scopus 로고    scopus 로고
    • Related eIF3 subunits TIF32 and HCR1 interact with an RNA recognition motif in PRT1 required for eIF3 integrity and ribosome binding
    • Valášek, L., Phan, L., Schoenfeld, L.W., Valášková, V., and Hinnebusch, A.G. 2001b. Related eIF3 subunits TIF32 and HCR1 interact with an RNA recognition motif in PRT1 required for eIF3 integrity and ribosome binding. EMBO J. 20:891-904.
    • (2001) EMBO J. , vol.20 , pp. 891-904
    • Valášek, L.1    Phan, L.2    Schoenfeld, L.W.3    Valášková, V.4    Hinnebusch, A.G.5
  • 29
    • 0036846237 scopus 로고    scopus 로고
    • Direct eIF2-eIF3 contact in the multifactor complex is important for translation initiation in vivo
    • Valášek, L., Nielsen, K.H., and Hinnebusch, A.G. 2002. Direct eIF2-eIF3 contact in the multifactor complex is important for translation initiation in vivo. EMBO J. 21: 5886-5898.
    • (2002) EMBO J. , vol.21 , pp. 5886-5898
    • Valášek, L.1    Nielsen, K.H.2    Hinnebusch, A.G.3
  • 30
    • 0030832613 scopus 로고    scopus 로고
    • Identification of partners of TIF34, a component of the yeast eIF3 complex, required for cell proliferation and translation initiation
    • Verlhac, M.-H., Chen, R.-H., Hanachi, P., Hershey, J.W.B., and Derynck, R. 1997. Identification of partners of TIF34, a component of the yeast eIF3 complex, required for cell proliferation and translation initiation. EMBO J. 16: 6812-6822.
    • (1997) EMBO J. , vol.16 , pp. 6812-6822
    • Verlhac, M.-H.1    Chen, R.-H.2    Hanachi, P.3    Hershey, J.W.B.4    Derynck, R.5
  • 31
    • 0033546406 scopus 로고    scopus 로고
    • A 110-kilodalton subunit of translation initiation factor eIF3 and an associated 135-kilodalton protein are encoded by the Saccharomyces cerevisiae TIF32 and TIF31 genes
    • Vornlocher, H.P., Hanachi, P., Ribeiro, S., and Hershey, J.W.B. 1999. A 110-kilodalton subunit of translation initiation factor eIF3 and an associated 135-kilodalton protein are encoded by the Saccharomyces cerevisiae TIF32 and TIF31 genes. J. Biol. Chem. 274: 16802-16812.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16802-16812
    • Vornlocher, H.P.1    Hanachi, P.2    Ribeiro, S.3    Hershey, J.W.B.4


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