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Volumn 330, Issue 5, 2003, Pages 917-924

Communication between eukaryotic translation initiation factors 1 and 1A on the yeast small ribosomal subunit

Author keywords

Expressed protein ligation; Fluorescence anisotropy; Thermodynamic framework

Indexed keywords

INITIATION FACTOR 1; PROTEIN SUBUNIT; RHODAMINE;

EID: 0037675905     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00665-X     Document Type: Article
Times cited : (79)

References (38)
  • 1
    • 0000091608 scopus 로고    scopus 로고
    • Pathway and mechanism of initiation of protein synthesis
    • N. Sonenberg, J.W.B. Hershey, & M.B. Mathews. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Hershey J.W.B., Merrick W.C. Pathway and mechanism of initiation of protein synthesis. Sonenberg N., Hershey J.W.B., Mathews M.B. Translational Control of Gene Expression. 2000;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
  • 2
    • 0036224032 scopus 로고    scopus 로고
    • Development and characterization of a reconstituted yeast translation initiation system
    • Algire M.A., Maag D., Savio P., Acker M.G., Tarun S.Z., Sachs A.B., et al. Development and characterization of a reconstituted yeast translation initiation system. RNA. 8:2002;382-397.
    • (2002) RNA , vol.8 , pp. 382-397
    • Algire, M.A.1    Maag, D.2    Savio, P.3    Acker, M.G.4    Tarun, S.Z.5    Sachs, A.B.6
  • 3
    • 0018095166 scopus 로고
    • The mechanism of action of protein synthesis initiation factors from rabbit reticulocytes
    • Benne R., Hershey J.W.B. The mechanism of action of protein synthesis initiation factors from rabbit reticulocytes. J. Biol. Chem. 253:1978;3078-3087.
    • (1978) J. Biol. Chem. , vol.253 , pp. 3078-3087
    • Benne, R.1    Hershey, J.W.B.2
  • 4
    • 0033580851 scopus 로고    scopus 로고
    • Distinct functions of eukaryotic translation initiation factors eIF1A and eIF3 in the formation of the 40 S ribosomal preinitiation complex
    • Chaudhuri J., Chowdhury D., Maitra U. Distinct functions of eukaryotic translation initiation factors eIF1A and eIF3 in the formation of the 40 S ribosomal preinitiation complex. J. Biol. Chem. 273:1999;17975-17980.
    • (1999) J. Biol. Chem. , vol.273 , pp. 17975-17980
    • Chaudhuri, J.1    Chowdhury, D.2    Maitra, U.3
  • 5
    • 0030910714 scopus 로고    scopus 로고
    • Function of eukaryotic translation initiation factor 1A (eIF1A) (formerly called eIF-4C) in initiation of protein synthesis
    • Chaudhuri J., Si K., Maitra U. Function of eukaryotic translation initiation factor 1A (eIF1A) (formerly called eIF-4C) in initiation of protein synthesis. J. Biol. Chem. 272:1997;7883-7891.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7883-7891
    • Chaudhuri, J.1    Si, K.2    Maitra, U.3
  • 6
    • 0037458626 scopus 로고    scopus 로고
    • Mammalian translation initiation factor eIF1 functions with eIF1A and eIF3 in the formation of a stable 40 S preinitiation complex
    • Majumdar R., Bandyopadhyay A., Maitra U. Mammalian translation initiation factor eIF1 functions with eIF1A and eIF3 in the formation of a stable 40 S preinitiation complex. J. Biol. Chem. 278:2003;6580-6587.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6580-6587
    • Majumdar, R.1    Bandyopadhyay, A.2    Maitra, U.3
  • 7
    • 0018883323 scopus 로고
    • The mechanism of action of eukaryotic initiation factor 4C in protein synthesis
    • Thomas A., Goumans H., Voorma H.O., Benne R. The mechanism of action of eukaryotic initiation factor 4C in protein synthesis. Eur. J. Biochem. 107:1980;39-45.
    • (1980) Eur. J. Biochem. , vol.107 , pp. 39-45
    • Thomas, A.1    Goumans, H.2    Voorma, H.O.3    Benne, R.4
  • 8
    • 0019322328 scopus 로고
    • Mode of action of protein synthesis initiation factor eIF-1 from rabbit reticulocytes
    • Thomas A., Spann W., Van Steeg H., Voorma H.O., Benne R. Mode of action of protein synthesis initiation factor eIF-1 from rabbit reticulocytes. FEBS Letters. 116:1980;67-71.
    • (1980) FEBS Letters , vol.116 , pp. 67-71
    • Thomas, A.1    Spann, W.2    Van Steeg, H.3    Voorma, H.O.4    Benne, R.5
  • 9
    • 0017707116 scopus 로고
    • Initiation of mammalian protein synthesis. II. The assembly of the initiation complex with purified initiation factors
    • Trachsel H., Erni B., Schreier M.H., Staehelin T. Initiation of mammalian protein synthesis. II. The assembly of the initiation complex with purified initiation factors. J. Mol. Biol. 116:1977;755-767.
    • (1977) J. Mol. Biol. , vol.116 , pp. 755-767
    • Trachsel, H.1    Erni, B.2    Schreier, M.H.3    Staehelin, T.4
  • 10
    • 0026609868 scopus 로고
    • The suil suppressor locus in Saccharomyces cerevisiae encodes a translation factor that functions during tRNA(iMet) recognition of the start codon
    • Yoon H.J., Donahue T.F. The suil suppressor locus in Saccharomyces cerevisiae encodes a translation factor that functions during tRNA(iMet) recognition of the start codon. Mol. Cell. Biol. 12:1992;248-260.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 248-260
    • Yoon, H.J.1    Donahue, T.F.2
  • 11
    • 0037112055 scopus 로고    scopus 로고
    • The roles of individual eukaryotic translation initiation factors in ribosomal scanning and initiation codon selection
    • Pestova T.V., Kolupaeva V.G. The roles of individual eukaryotic translation initiation factors in ribosomal scanning and initiation codon selection. Genes Dev. 16:2002;2906-2922.
    • (2002) Genes Dev. , vol.16 , pp. 2906-2922
    • Pestova, T.V.1    Kolupaeva, V.G.2
  • 12
    • 0032572776 scopus 로고    scopus 로고
    • Eukaryotic ribosomes require initiation factors 1 and 1A to locate initiation codons
    • Pestova T.V., Borukhov S.I., Hellen C.U.T. Eukaryotic ribosomes require initiation factors 1 and 1A to locate initiation codons. Nature. 394:1998;854-859.
    • (1998) Nature , vol.394 , pp. 854-859
    • Pestova, T.V.1    Borukhov, S.I.2    Hellen, C.U.T.3
  • 13
    • 0030002818 scopus 로고    scopus 로고
    • SUI1/p16 is required for the activity of eukaryotic translation initiation factor 3 in Saccharomyces cerevisiae
    • Naranda T., MacMillan S.E., Donahue T.F., Hershey J.W. SUI1/p16 is required for the activity of eukaryotic translation initiation factor 3 in Saccharomyces cerevisiae. Mol. Cell. Biol. 16:1996;2307-2313.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2307-2313
    • Naranda, T.1    MacMillan, S.E.2    Donahue, T.F.3    Hershey, J.W.4
  • 14
    • 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., et al. Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5. Mol. Cell. Biol. 18:1998;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
  • 15
    • 0033830375 scopus 로고    scopus 로고
    • Physical and functional interaction between the eukaryotic orthologs of prokaryotic translation initiation factors IF1 and IF2
    • Choi S.K., Olsen D.S., Roll-Mecak A., Martung A., Remo K.L., Burley S.K., et al. Physical and functional interaction between the eukaryotic orthologs of prokaryotic translation initiation factors IF1 and IF2. Mol. Cell. Biol. 20:2000;7183-7191.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7183-7191
    • Choi, S.K.1    Olsen, D.S.2    Roll-Mecak, A.3    Martung, A.4    Remo, K.L.5    Burley, S.K.6
  • 16
    • 0037452587 scopus 로고    scopus 로고
    • Mapping the binding interface between human eukaryotic initiation factors 1A and 5B: A new interaction between old partners
    • Marintchev A., Kolupaeva V.G., Pestova T.V., Wagner G. Mapping the binding interface between human eukaryotic initiation factors 1A and 5B: a new interaction between old partners. Proc. Natl Acad. Sci. USA. 100:2003;1535-1540.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 1535-1540
    • Marintchev, A.1    Kolupaeva, V.G.2    Pestova, T.V.3    Wagner, G.4
  • 17
    • 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., Hinnebusch A.G. Domains of eIF1A that mediate binding to eIF2, eIF3 and eIF5B and promote ternary complex recruitment in vivo. EMBO J. 22:2003;193-204.
    • (2003) 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
  • 18
    • 0031915895 scopus 로고    scopus 로고
    • Universally conserved translation initiation factors
    • Kyrpides N.C., Woese C.R. Universally conserved translation initiation factors. Proc. Natl Acad. Sci. USA. 95:1998;224-228.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 224-228
    • Kyrpides, N.C.1    Woese, C.R.2
  • 20
    • 0029051704 scopus 로고
    • Specific protection of 16 S rRNA by translational initiation factors
    • Moazed D., Samaha R.R., Gualerzi C., Noller H.F. Specific protection of 16 S rRNA by translational initiation factors. J. Mol. Biol. 248:1995;207-210.
    • (1995) J. Mol. Biol. , vol.248 , pp. 207-210
    • Moazed, D.1    Samaha, R.R.2    Gualerzi, C.3    Noller, H.F.4
  • 21
    • 0033522507 scopus 로고    scopus 로고
    • Structure and interactions of the translation initiation factor eIF1
    • Fletcher C.M., Pestova T.V., Hellen C.U., Wagner G. Structure and interactions of the translation initiation factor eIF1. EMBO J. 18:1999;2631-2637.
    • (1999) EMBO J. , vol.18 , pp. 2631-2637
    • Fletcher, C.M.1    Pestova, T.V.2    Hellen, C.U.3    Wagner, G.4
  • 22
    • 0035355352 scopus 로고    scopus 로고
    • A subcomplex of three eIF3 subunits binds eIF1 and eIF5 and stimulates ribosome binding of mRNA and tRNA(i)(Met)
    • Phan L., Schoenfeld L.W., Valasek L., Nielsen K.H., Hinnebusch A.G. A subcomplex of three eIF3 subunits binds eIF1 and eIF5 and stimulates ribosome binding of mRNA and tRNA(i)(Met). EMBO J. 20:2001;2954-2965.
    • (2001) EMBO J. , vol.20 , pp. 2954-2965
    • Phan, L.1    Schoenfeld, L.W.2    Valasek, L.3    Nielsen, K.H.4    Hinnebusch, A.G.5
  • 23
    • 0023051839 scopus 로고
    • Binding of Escherichia coli protein synthesis initiation factor IF1 to 30 S ribosomal subunits measured by fluorescence polarization
    • Zucker F.H., Hershey J.W. Binding of Escherichia coli protein synthesis initiation factor IF1 to 30 S ribosomal subunits measured by fluorescence polarization. Biochemistry. 25:1986;3682-3690.
    • (1986) Biochemistry , vol.25 , pp. 3682-3690
    • Zucker, F.H.1    Hershey, J.W.2
  • 24
    • 0020030957 scopus 로고
    • The binding of fluorescein-labeled protein synthesis initiation factor 2 to Escherichia coli 30 S ribosomal subunits determined by fluorescence polarization
    • Weiel J., Hershey J.W. The binding of fluorescein-labeled protein synthesis initiation factor 2 to Escherichia coli 30 S ribosomal subunits determined by fluorescence polarization. J. Biol. Chem. 257:1982;1215-1220.
    • (1982) J. Biol. Chem. , vol.257 , pp. 1215-1220
    • Weiel, J.1    Hershey, J.W.2
  • 25
    • 0019890811 scopus 로고
    • Fluorescence polarization studies of the interaction of Escherichia coli protein synthesis initiation factor 3 with 30 S ribosomal subunits
    • Weiel J., Hershey J.W. Fluorescence polarization studies of the interaction of Escherichia coli protein synthesis initiation factor 3 with 30 S ribosomal subunits. Biochemistry. 20:1981;5859-5865.
    • (1981) Biochemistry , vol.20 , pp. 5859-5865
    • Weiel, J.1    Hershey, J.W.2
  • 26
    • 0017903902 scopus 로고
    • Fluorescence polarization studies of the binding of fluorescein-labeled initiation factor IF3 to 30 S ribosomal subunits from Escherichia coli
    • Weiel J., Hershey J.W. Fluorescence polarization studies of the binding of fluorescein-labeled initiation factor IF3 to 30 S ribosomal subunits from Escherichia coli. FEBS Letters. 87:1978;103-106.
    • (1978) FEBS Letters , vol.87 , pp. 103-106
    • Weiel, J.1    Hershey, J.W.2
  • 27
    • 0344351815 scopus 로고    scopus 로고
    • Semisynthesis of cytotoxic proteins using a modified protein splicing element
    • Evans T.J., Benner J., Xu M. Semisynthesis of cytotoxic proteins using a modified protein splicing element. Protein Sci. 7:1998;2256-2264.
    • (1998) Protein Sci. , vol.7 , pp. 2256-2264
    • Evans, T.J.1    Benner, J.2    Xu, M.3
  • 28
    • 0032499752 scopus 로고    scopus 로고
    • Expressed protein ligation: A general method for protein engineering
    • Muir T.W., Dolan S., Cole P.A. Expressed protein ligation: a general method for protein engineering. Proc. Natl Acad. Sci. USA. 95:1998;6705-6710.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6705-6710
    • Muir, T.W.1    Dolan, S.2    Cole, P.A.3
  • 29
    • 0037936779 scopus 로고    scopus 로고
    • Merging fluorescence resonance energy transfer and expressed protein ligation to analyze protein-protein interactions
    • Scheibner K.A., Zhang Z., Cole P.A. Merging fluorescence resonance energy transfer and expressed protein ligation to analyze protein-protein interactions. Anal. Biochem. 317:2003;226-232.
    • (2003) Anal. Biochem. , vol.317 , pp. 226-232
    • Scheibner, K.A.1    Zhang, Z.2    Cole, P.A.3
  • 31
    • 0026497842 scopus 로고
    • RNA binding assays for Tat-derived peptides: Implications for specificity
    • Weeks K.M., Crothers D.M. RNA binding assays for Tat-derived peptides: implications for specificity. Biochemistry. 31:1992;10281-10287.
    • (1992) Biochemistry , vol.31 , pp. 10281-10287
    • Weeks, K.M.1    Crothers, D.M.2
  • 32
    • 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., Hinnebusch A.G. Complex formation by all five homologues of mammalian translation initiation factor 3 subunits from yeast Saccharomyces cerevisiae. J. Biol. Chem. 273:1998;18573-18585.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18573-18585
    • Asano, K.1    Phan, L.2    Anderson, J.3    Hinnebusch, A.G.4
  • 34
    • 0036428702 scopus 로고    scopus 로고
    • Intracellular translation initiation factor levels in Saccharomyces cerevisiae and their role in cap-complex function
    • Von Der Haar T., McCarthy J.E. Intracellular translation initiation factor levels in Saccharomyces cerevisiae and their role in cap-complex function. Mol. Microbiol. 46:2002;531-544.
    • (2002) Mol. Microbiol. , vol.46 , pp. 531-544
    • Von Der Haar, T.1    McCarthy, J.E.2
  • 35
    • 0036846237 scopus 로고    scopus 로고
    • Direct eIF2-eIF3 contact in the multifactor complex is important for translation initiation in vivo
    • Valasek L., Nielsen K.H., Hinnebusch A.G. Direct eIF2-eIF3 contact in the multifactor complex is important for translation initiation in vivo. EMBO J. 21:2002;5886-5898.
    • (2002) EMBO J. , vol.21 , pp. 5886-5898
    • Valasek, L.1    Nielsen, K.H.2    Hinnebusch, A.G.3
  • 36
    • 0013112952 scopus 로고
    • Yeast translation initiation suppressor sui2 encodes the alpha subunit of eukaryotic initiation factor 2 and shares sequence identity with the human alpha subunit
    • Cigan A.M., Pabich E.K., Feng L., Donahue T.F. Yeast translation initiation suppressor sui2 encodes the alpha subunit of eukaryotic initiation factor 2 and shares sequence identity with the human alpha subunit. Proc. Natl Acad. Sci. USA. 86:1989;2784-2788.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 2784-2788
    • Cigan, A.M.1    Pabich, E.K.2    Feng, L.3    Donahue, T.F.4
  • 37
    • 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., Donahue T.F. GTP hydrolysis controls stringent selection of the AUG start codon during translation initiation in Saccharomyces cerevisiae. Genes Dev. 11:1997;2396-2413.
    • (1997) Genes Dev. , vol.11 , pp. 2396-2413
    • Huang, H.1    Yoon, H.2    Hannig, E.M.3    Donahue, T.F.4
  • 38
    • 0015530179 scopus 로고
    • Lac repressor binding to non-operator DNA: Detailed studies and a comparison of equilibrium and rate competition methods
    • Lin S.Y., Riggs A.D. Lac repressor binding to non-operator DNA: detailed studies and a comparison of equilibrium and rate competition methods. J. Mol. Biol. 72:1972;671-690.
    • (1972) J. Mol. Biol. , vol.72 , pp. 671-690
    • Lin, S.Y.1    Riggs, A.D.2


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