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Volumn 584, Issue 2, 2010, Pages 396-404

Eukaryotic initiator tRNA: Finely tuned and ready for action

Author keywords

Initiator tRNA; Ribosome; Translation initiation

Indexed keywords

CYTOSINE; GUANOSINE; INITIATION FACTOR; INITIATION FACTOR 2; MESSENGER RNA; METHIONINE TRANSFER RNA; TRANSFER RNA;

EID: 71549155597     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.11.047     Document Type: Review
Times cited : (48)

References (84)
  • 1
    • 0025110827 scopus 로고
    • Expression and function of a human initiator tRNA gene in the yeast Saccharomyces cerevisiae
    • Francis M.A., and RajBhandary U.L. Expression and function of a human initiator tRNA gene in the yeast Saccharomyces cerevisiae. Mol. Cell. Biol. 10 (1990) 4486-4494
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 4486-4494
    • Francis, M.A.1    RajBhandary, U.L.2
  • 2
    • 41349089950 scopus 로고    scopus 로고
    • Elevated tRNA(iMet) synthesis can drive cell proliferation and oncogenic transformation
    • Marshall L., Kenneth N.S., and White R.J. Elevated tRNA(iMet) synthesis can drive cell proliferation and oncogenic transformation. Cell 133 (2008) 78-89
    • (2008) Cell , vol.133 , pp. 78-89
    • Marshall, L.1    Kenneth, N.S.2    White, R.J.3
  • 4
    • 3943080710 scopus 로고    scopus 로고
    • The molecular mechanics of eukaryotic translation
    • Kapp L.D., and Lorsch J.R. The molecular mechanics of eukaryotic translation. Annu Rev Biochem 73 (2004) 657-704
    • (2004) Annu Rev Biochem , vol.73 , pp. 657-704
    • Kapp, L.D.1    Lorsch, J.R.2
  • 5
    • 33846991130 scopus 로고    scopus 로고
    • The mechanism of translation initiation in eukaryotes
    • Mathews M.B., Sonenberg N., and Hershey J.W.B. (Eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Pestova T.V., Lorsch J.R., and Hellen C.U.T. The mechanism of translation initiation in eukaryotes. In: Mathews M.B., Sonenberg N., and Hershey J.W.B. (Eds). Translational Control in Biology and Medicine (2007), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY 87-128
    • (2007) Translational Control in Biology and Medicine , pp. 87-128
    • Pestova, T.V.1    Lorsch, J.R.2    Hellen, C.U.T.3
  • 6
    • 60149091189 scopus 로고    scopus 로고
    • Regulation of translation initiation in eukaryotes: mechanisms and biological targets
    • Sonenberg N., and Hinnebusch A.G. Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 136 (2009) 731-745
    • (2009) Cell , vol.136 , pp. 731-745
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 7
    • 0018577166 scopus 로고
    • Specific interaction of initiation factor IF2 of E. coli with formylmethionyl-tRNA f Met
    • Petersen H.U., Roll T., Grunberg-Manago M., and Clark B.F. Specific interaction of initiation factor IF2 of E. coli with formylmethionyl-tRNA f Met. Biochem Biophys Res Commun 91 (1979) 1068-1074
    • (1979) Biochem Biophys Res Commun , vol.91 , pp. 1068-1074
    • Petersen, H.U.1    Roll, T.2    Grunberg-Manago, M.3    Clark, B.F.4
  • 8
    • 0031026590 scopus 로고    scopus 로고
    • Effect of the amino acid attached to Escherichia coli initiator tRNA on its affinity for the initiation factor IF2 and on the IF2 dependence of its binding to the ribosome
    • Wu X.Q., and RajBhandary U.L. Effect of the amino acid attached to Escherichia coli initiator tRNA on its affinity for the initiation factor IF2 and on the IF2 dependence of its binding to the ribosome. J. Biol. Chem. 272 (1997) 1891-1895
    • (1997) J. Biol. Chem. , vol.272 , pp. 1891-1895
    • Wu, X.Q.1    RajBhandary, U.L.2
  • 9
    • 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., Kolupaeva V.G., Marintchev A., Wagner G., and Pestova T.V. Position of eukaryotic initiation factor eIF1 on the 40S ribosomal subunit determined by directed hydroxyl radical probing. Genes Dev. 17 (2003) 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
  • 10
    • 30444454334 scopus 로고    scopus 로고
    • The fidelity of translation initiation: reciprocal activities of eIF1, IF3 and YciH
    • Lomakin I.B., Shirokikh N.E., Yusupov M.M., Hellen C.U., and Pestova T.V. The fidelity of translation initiation: reciprocal activities of eIF1, IF3 and YciH. EMBO J. 25 (2006) 196-210
    • (2006) EMBO J. , vol.25 , pp. 196-210
    • Lomakin, I.B.1    Shirokikh, N.E.2    Yusupov, M.M.3    Hellen, C.U.4    Pestova, T.V.5
  • 11
    • 0026095269 scopus 로고
    • Structural and sequence elements important for recognition of Escherichia coli formylmethionine tRNA by methionyl-tRNA transformylase are clustered in the acceptor stem
    • Lee C.P., Seong B.L., and RajBhandary U.L. Structural and sequence elements important for recognition of Escherichia coli formylmethionine tRNA by methionyl-tRNA transformylase are clustered in the acceptor stem. J. Biol. Chem. 266 (1991) 18012-18017
    • (1991) J. Biol. Chem. , vol.266 , pp. 18012-18017
    • Lee, C.P.1    Seong, B.L.2    RajBhandary, U.L.3
  • 12
    • 0026552726 scopus 로고
    • Nucleotides of tRNA governing the specificity of Escherichia coli methionyl-tRNA(fMet) formyltransferase
    • Guillon J.M., Meinnel T., Mechulam Y., Lazennec C., Blanquet S., and Fayat G. Nucleotides of tRNA governing the specificity of Escherichia coli methionyl-tRNA(fMet) formyltransferase. J. Mol. Biol. 224 (1992) 359-367
    • (1992) J. Mol. Biol. , vol.224 , pp. 359-367
    • Guillon, J.M.1    Meinnel, T.2    Mechulam, Y.3    Lazennec, C.4    Blanquet, S.5    Fayat, G.6
  • 13
    • 0002084108 scopus 로고
    • Initiator tRNAs and initiation of protein synthesis
    • Soll D., and RajBhandary U.L. (Eds), American Society for Microbiology, Washington, DC
    • RajBhandary U.L., and Chow C.M. Initiator tRNAs and initiation of protein synthesis. In: Soll D., and RajBhandary U.L. (Eds). tRNA: Structure, Biosynthesis and Function (1995), American Society for Microbiology, Washington, DC 511-528
    • (1995) tRNA: Structure, Biosynthesis and Function , pp. 511-528
    • RajBhandary, U.L.1    Chow, C.M.2
  • 14
    • 0033534614 scopus 로고    scopus 로고
    • Quantitative assessment of EF-1alpha. GTP binding to aminoacyl-tRNAs, aminoacyl-viral RNA, and tRNA shows close correspondence to the RNA binding properties of EF-Tu
    • Dreher T.W., Uhlenbeck O.C., and Browning K.S. Quantitative assessment of EF-1alpha. GTP binding to aminoacyl-tRNAs, aminoacyl-viral RNA, and tRNA shows close correspondence to the RNA binding properties of EF-Tu. J. Biol. Chem. 274 (1999) 666-672
    • (1999) J. Biol. Chem. , vol.274 , pp. 666-672
    • Dreher, T.W.1    Uhlenbeck, O.C.2    Browning, K.S.3
  • 15
    • 0036792830 scopus 로고    scopus 로고
    • tRNomics: analysis of tRNA genes from 50 genomes of Eukarya, Archaea, and Bacteria reveals anticodon-sparing strategies and domain-specific features
    • Marck C., and Grosjean H. tRNomics: analysis of tRNA genes from 50 genomes of Eukarya, Archaea, and Bacteria reveals anticodon-sparing strategies and domain-specific features. RNA 8 (2002) 1189-1232
    • (2002) RNA , vol.8 , pp. 1189-1232
    • Marck, C.1    Grosjean, H.2
  • 17
    • 0031172424 scopus 로고    scopus 로고
    • Changes of tRNA population during compensatory cell proliferation: differential expression of methionine-tRNA species
    • Kanduc D. Changes of tRNA population during compensatory cell proliferation: differential expression of methionine-tRNA species. Arch. Biochem. Biophys. 342 (1997) 1-5
    • (1997) Arch. Biochem. Biophys. , vol.342 , pp. 1-5
    • Kanduc, D.1
  • 18
    • 0027745663 scopus 로고
    • Discrimination between initiation and elongation of protein biosynthesis in yeast: identity assured by a nucleotide modification in the initiator tRNA
    • Forster C., Chakraburtty K., and Sprinzl M. Discrimination between initiation and elongation of protein biosynthesis in yeast: identity assured by a nucleotide modification in the initiator tRNA. Nucleic Acids Res. 21 (1993) 5679-5683
    • (1993) Nucleic Acids Res. , vol.21 , pp. 5679-5683
    • Forster, C.1    Chakraburtty, K.2    Sprinzl, M.3
  • 19
    • 0029787494 scopus 로고    scopus 로고
    • Interplay of methionine tRNAs with translation elongation factor Tu and translation initiation factor 2 in Escherichia coli
    • Guillon J.M., Heiss S., Soutourina J., Mechulam Y., Laalami S., Grunberg-Manago M., and Blanquet S. Interplay of methionine tRNAs with translation elongation factor Tu and translation initiation factor 2 in Escherichia coli. J. Biol. Chem. 271 (1996) 22321-22325
    • (1996) J. Biol. Chem. , vol.271 , pp. 22321-22325
    • Guillon, J.M.1    Heiss, S.2    Soutourina, J.3    Mechulam, Y.4    Laalami, S.5    Grunberg-Manago, M.6    Blanquet, S.7
  • 20
    • 0032789637 scopus 로고    scopus 로고
    • Genetic interactions between a null allele of the RIT1 gene encoding an initiator tRNA-specific modification enzyme and genes encoding translation factors in Saccharomyces cerevisiae
    • Astrom S.U., Nordlund M.E., Erickson F.L., Hannig E.M., and Bystrom A.S. Genetic interactions between a null allele of the RIT1 gene encoding an initiator tRNA-specific modification enzyme and genes encoding translation factors in Saccharomyces cerevisiae. Mol. Gen. Genet. 261 (1999) 967-976
    • (1999) Mol. Gen. Genet. , vol.261 , pp. 967-976
    • Astrom, S.U.1    Nordlund, M.E.2    Erickson, F.L.3    Hannig, E.M.4    Bystrom, A.S.5
  • 21
    • 0023502772 scopus 로고
    • Mutants of Escherichia coli formylmethionine tRNA: a single base change enables initiator tRNA to act as an elongator in vitro
    • Seong B.L., and RajBhandary U.L. Mutants of Escherichia coli formylmethionine tRNA: a single base change enables initiator tRNA to act as an elongator in vitro. Proc. Natl. Acad. Sci. USA 84 (1987) 8859-8863
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 8859-8863
    • Seong, B.L.1    RajBhandary, U.L.2
  • 22
    • 0031952186 scopus 로고    scopus 로고
    • Initiator-elongator discrimination in vertebrate tRNAs for protein synthesis
    • Drabkin H.J., Estrella M., and RajBhandary U.L. Initiator-elongator discrimination in vertebrate tRNAs for protein synthesis. Mol. Cell. Biol. 18 (1998) 1459-1466
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1459-1466
    • Drabkin, H.J.1    Estrella, M.2    RajBhandary, U.L.3
  • 23
    • 0027340369 scopus 로고
    • The yeast initiator tRNAMet can act as an elongator tRNA(Met) in vivo
    • Astrom S.U., von Pawel-Rammingen U., and Bystrom A.S. The yeast initiator tRNAMet can act as an elongator tRNA(Met) in vivo. J. Mol. Biol. 233 (1993) 43-58
    • (1993) J. Mol. Biol. , vol.233 , pp. 43-58
    • Astrom, S.U.1    von Pawel-Rammingen, U.2    Bystrom, A.S.3
  • 24
    • 0026528473 scopus 로고
    • Mutational analysis of conserved positions potentially important for initiator tRNA function in Saccharomyces cerevisiae
    • von Pawel-Rammingen U., Astrom S., and Bystrom A.S. Mutational analysis of conserved positions potentially important for initiator tRNA function in Saccharomyces cerevisiae. Mol Cell Biol 12 (1992) 1432-1442
    • (1992) Mol Cell Biol , vol.12 , pp. 1432-1442
    • von Pawel-Rammingen, U.1    Astrom, S.2    Bystrom, A.S.3
  • 25
    • 0027423265 scopus 로고
    • The role of nucleotides conserved in eukaryotic initiator methionine tRNAs in initiation of protein synthesis
    • Drabkin H.J., Helk B., and RajBhandary U.L. The role of nucleotides conserved in eukaryotic initiator methionine tRNAs in initiation of protein synthesis. J. Biol. Chem. 268 (1993) 25221-25228
    • (1993) J. Biol. Chem. , vol.268 , pp. 25221-25228
    • Drabkin, H.J.1    Helk, B.2    RajBhandary, U.L.3
  • 26
    • 60849128493 scopus 로고    scopus 로고
    • Understanding the sequence specificity of tRNA binding to elongation factor Tu using tRNA mutagenesis
    • Schrader J.M., Chapman S.J., and Uhlenbeck O.C. Understanding the sequence specificity of tRNA binding to elongation factor Tu using tRNA mutagenesis. J. Mol. Biol. 386 (2009) 1255-1264
    • (2009) J. Mol. Biol. , vol.386 , pp. 1255-1264
    • Schrader, J.M.1    Chapman, S.J.2    Uhlenbeck, O.C.3
  • 27
    • 0038381426 scopus 로고    scopus 로고
    • Common location of determinants in initiator transfer RNAs for initiator-elongator discrimination in bacteria and in eukaryotes
    • Stortchevoi A., Varshney U., and RajBhandary U.L. Common location of determinants in initiator transfer RNAs for initiator-elongator discrimination in bacteria and in eukaryotes. J. Biol. Chem. 278 (2003) 17672-17679
    • (2003) J. Biol. Chem. , vol.278 , pp. 17672-17679
    • Stortchevoi, A.1    Varshney, U.2    RajBhandary, U.L.3
  • 29
    • 0024459045 scopus 로고
    • Structural features that underlie the use of bacterial Met-tRNAfMet primarily as an elongator in eukaryotic protein synthesis
    • Wagner T., Rundquist C., Gross M., and Sigler P.B. Structural features that underlie the use of bacterial Met-tRNAfMet primarily as an elongator in eukaryotic protein synthesis. J. Biol. Chem. 264 (1989) 18506-18511
    • (1989) J. Biol. Chem. , vol.264 , pp. 18506-18511
    • Wagner, T.1    Rundquist, C.2    Gross, M.3    Sigler, P.B.4
  • 30
    • 0024988324 scopus 로고
    • The role of modified purine 64 in initiator/elongator discrimination of tRNA(iMet) from yeast and wheat germ
    • Kiesewetter S., Ott G., and Sprinzl M. The role of modified purine 64 in initiator/elongator discrimination of tRNA(iMet) from yeast and wheat germ. Nucleic Acids Res. 18 (1990) 4677-4682
    • (1990) Nucleic Acids Res. , vol.18 , pp. 4677-4682
    • Kiesewetter, S.1    Ott, G.2    Sprinzl, M.3
  • 31
    • 0028034499 scopus 로고
    • Rit1, a tRNA backbone-modifying enzyme that mediates initiator and elongator tRNA discrimination
    • Astrom S.U., and Bystrom A.S. Rit1, a tRNA backbone-modifying enzyme that mediates initiator and elongator tRNA discrimination. Cell 79 (1994) 535-546
    • (1994) Cell , vol.79 , pp. 535-546
    • Astrom, S.U.1    Bystrom, A.S.2
  • 32
    • 0024539405 scopus 로고
    • Presence of phosphorylated O-ribosyl-adenosine in T-psi-stem of yeast methionine initiator tRNA
    • Desgres J., Keith G., Kuo K.C., and Gehrke C.W. Presence of phosphorylated O-ribosyl-adenosine in T-psi-stem of yeast methionine initiator tRNA. Nucleic Acids Res. 17 (1989) 865-882
    • (1989) Nucleic Acids Res. , vol.17 , pp. 865-882
    • Desgres, J.1    Keith, G.2    Kuo, K.C.3    Gehrke, C.W.4
  • 33
    • 0025815046 scopus 로고
    • The 3 A crystal structure of yeast initiator tRNA: functional implications in initiator/elongator discrimination
    • Basavappa R., and Sigler P.B. The 3 A crystal structure of yeast initiator tRNA: functional implications in initiator/elongator discrimination. Embo J 10 (1991) 3105-3111
    • (1991) Embo J , vol.10 , pp. 3105-3111
    • Basavappa, R.1    Sigler, P.B.2
  • 35
    • 0033081413 scopus 로고    scopus 로고
    • The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA
    • Nissen P., Thirup S., Kjeldgaard M., and Nyborg J. The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA. Structure Fold Des 7 (1999) 143-156
    • (1999) Structure Fold Des , vol.7 , pp. 143-156
    • Nissen, P.1    Thirup, S.2    Kjeldgaard, M.3    Nyborg, J.4
  • 36
    • 0347123543 scopus 로고    scopus 로고
    • GTP-dependent recognition of the methionine moiety on initiator tRNA by translation factor eIF2
    • Kapp L.D., and Lorsch J.R. GTP-dependent recognition of the methionine moiety on initiator tRNA by translation factor eIF2. J. Mol. Biol. 335 (2004) 923-936
    • (2004) J. Mol. Biol. , vol.335 , pp. 923-936
    • Kapp, L.D.1    Lorsch, J.R.2
  • 37
    • 33646168052 scopus 로고    scopus 로고
    • Yeast initiator tRNA identity elements cooperate to influence multiple steps of translation initiation
    • Kapp L.D., Kolitz S.E., and Lorsch J.R. Yeast initiator tRNA identity elements cooperate to influence multiple steps of translation initiation. RNA 12 (2006) 751-764
    • (2006) RNA , vol.12 , pp. 751-764
    • Kapp, L.D.1    Kolitz, S.E.2    Lorsch, J.R.3
  • 38
    • 0029666095 scopus 로고    scopus 로고
    • The A1×U72 base pair conserved in eukaryotic initiator tRNAs is important specifically for binding to the eukaryotic translation initiation factor eIF2
    • Farruggio D., Chaudhuri J., Maitra U., and RajBhandary U.L. The A1×U72 base pair conserved in eukaryotic initiator tRNAs is important specifically for binding to the eukaryotic translation initiation factor eIF2. Mol. Cell. Biol. 16 (1996) 4248-4256
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4248-4256
    • Farruggio, D.1    Chaudhuri, J.2    Maitra, U.3    RajBhandary, U.L.4
  • 39
    • 0021337227 scopus 로고
    • Isoleucyl initiator tRNA does not initiate eucaryotic protein synthesis
    • Wagner T., Gross M., and Sigler P.B. Isoleucyl initiator tRNA does not initiate eucaryotic protein synthesis. J. Biol. Chem. 259 (1984) 4706-4709
    • (1984) J. Biol. Chem. , vol.259 , pp. 4706-4709
    • Wagner, T.1    Gross, M.2    Sigler, P.B.3
  • 40
    • 0025015230 scopus 로고
    • Initiation of protein synthesis from a termination codon
    • Varshney U., and RajBhandary U.L. Initiation of protein synthesis from a termination codon. Proc. Natl. Acad. Sci. USA 87 (1990) 1586-1590
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1586-1590
    • Varshney, U.1    RajBhandary, U.L.2
  • 41
    • 0031842442 scopus 로고    scopus 로고
    • Initiation of protein synthesis in mammalian cells with codons other than AUG and amino acids other than methionine
    • Drabkin H.J., and RajBhandary U.L. Initiation of protein synthesis in mammalian cells with codons other than AUG and amino acids other than methionine. Mol. Cell. Biol. 18 (1998) 5140-5147
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5140-5147
    • Drabkin, H.J.1    RajBhandary, U.L.2
  • 43
    • 0018972388 scopus 로고
    • Three-dimensional structure of Escherichia coli initiator tRNAfMet
    • Woo N.H., Roe B.A., and Rich A. Three-dimensional structure of Escherichia coli initiator tRNAfMet. Nature 286 (1980) 346-351
    • (1980) Nature , vol.286 , pp. 346-351
    • Woo, N.H.1    Roe, B.A.2    Rich, A.3
  • 44
    • 0018496918 scopus 로고
    • Initiator tRNAs have a unique anticodon loop conformation
    • Wrede P., Woo N.H., and Rich A. Initiator tRNAs have a unique anticodon loop conformation. Proc. Natl. Acad. Sci. USA 76 (1979) 3289-3293
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 3289-3293
    • Wrede, P.1    Woo, N.H.2    Rich, A.3
  • 45
    • 0039993541 scopus 로고
    • Escherichia coli formylmethionine tRNA: mutations in GGGCCC sequence conserved in anticodon stem of initiator tRNAs affect initiation of protein synthesis and conformation of anticodon loop
    • Seong B.L., and RajBhandary U.L. Escherichia coli formylmethionine tRNA: mutations in GGGCCC sequence conserved in anticodon stem of initiator tRNAs affect initiation of protein synthesis and conformation of anticodon loop. Proc. Natl. Acad. Sci. USA 84 (1987) 334-338
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 334-338
    • Seong, B.L.1    RajBhandary, U.L.2
  • 46
    • 0029904026 scopus 로고    scopus 로고
    • Role of the three consecutive G:C base pairs conserved in the anticodon stem of initiator tRNAs in initiation of protein synthesis in Escherichia coli
    • Mandal N., Mangroo D., Dalluge J.J., McCloskey J.A., and RajBhandary U.L. Role of the three consecutive G:C base pairs conserved in the anticodon stem of initiator tRNAs in initiation of protein synthesis in Escherichia coli. RNA 2 (1996) 473-482
    • (1996) RNA , vol.2 , pp. 473-482
    • Mandal, N.1    Mangroo, D.2    Dalluge, J.J.3    McCloskey, J.A.4    RajBhandary, U.L.5
  • 47
    • 0031552368 scopus 로고    scopus 로고
    • On the conformation of the anticodon loops of initiator and elongator methionine tRNAs
    • Schweisguth D.C., and Moore P.B. On the conformation of the anticodon loops of initiator and elongator methionine tRNAs. J. Mol. Biol. 267 (1997) 505-519
    • (1997) J. Mol. Biol. , vol.267 , pp. 505-519
    • Schweisguth, D.C.1    Moore, P.B.2
  • 49
    • 33748582906 scopus 로고    scopus 로고
    • Crystal structure of a 70S ribosome-tRNA complex reveals functional interactions and rearrangements
    • Korostelev A., Trakhanov S., Laurberg M., and Noller H.F. Crystal structure of a 70S ribosome-tRNA complex reveals functional interactions and rearrangements. Cell 126 (2006) 1065-1077
    • (2006) Cell , vol.126 , pp. 1065-1077
    • Korostelev, A.1    Trakhanov, S.2    Laurberg, M.3    Noller, H.F.4
  • 50
    • 33751103912 scopus 로고    scopus 로고
    • Structural basis for messenger RNA movement on the ribosome
    • Yusupova G., Jenner L., Rees B., Moras D., and Yusupov M. Structural basis for messenger RNA movement on the ribosome. Nature 444 (2006) 391-394
    • (2006) Nature , vol.444 , pp. 391-394
    • Yusupova, G.1    Jenner, L.2    Rees, B.3    Moras, D.4    Yusupov, M.5
  • 51
    • 50849106034 scopus 로고    scopus 로고
    • A unique conformation of the anticodon stem-loop is associated with the capacity of tRNAfMet to initiate protein synthesis
    • Barraud P., Schmitt E., Mechulam Y., Dardel F., and Tisné C. A unique conformation of the anticodon stem-loop is associated with the capacity of tRNAfMet to initiate protein synthesis. Nucleic Acids Res. 36 (2008) 4894-4901
    • (2008) Nucleic Acids Res. , vol.36 , pp. 4894-4901
    • Barraud, P.1    Schmitt, E.2    Mechulam, Y.3    Dardel, F.4    Tisné, C.5
  • 52
    • 67651180795 scopus 로고    scopus 로고
    • Contribution of ribosomal residues to P-site tRNA binding
    • Shoji S., Abdi N.M., Bundschuh R., and Fredrick K. Contribution of ribosomal residues to P-site tRNA binding. Nucleic Acids Res. 37 (2009) 4033-4042
    • (2009) Nucleic Acids Res. , vol.37 , pp. 4033-4042
    • Shoji, S.1    Abdi, N.M.2    Bundschuh, R.3    Fredrick, K.4
  • 53
    • 0032428969 scopus 로고    scopus 로고
    • The essential Gcd10p-Gcd14p nuclear complex is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA
    • Anderson J., et al. The essential Gcd10p-Gcd14p nuclear complex is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA. Genes Dev. 12 (1998) 3650-3662
    • (1998) Genes Dev. , vol.12 , pp. 3650-3662
    • Anderson, J.1
  • 54
    • 0034625166 scopus 로고    scopus 로고
    • The Gcd10p/Gcd14p complex is the essential two-subunit tRNA(1-methyladenosine) methyltransferase of Saccharomyces cerevisiae
    • Anderson J., Phan L., and Hinnebusch A.G. The Gcd10p/Gcd14p complex is the essential two-subunit tRNA(1-methyladenosine) methyltransferase of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 97 (2000) 5173-5178
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5173-5178
    • Anderson, J.1    Phan, L.2    Hinnebusch, A.G.3
  • 55
    • 2642574393 scopus 로고    scopus 로고
    • Nuclear surveillance and degradation of hypomodified initiator tRNAMet in S. cerevisiae
    • Kadaba S., Krueger A., Trice T., Krecic A.M., Hinnebusch A.G., and Anderson J. Nuclear surveillance and degradation of hypomodified initiator tRNAMet in S. cerevisiae. Genes Dev. 18 (2004) 1227-1240
    • (2004) Genes Dev. , vol.18 , pp. 1227-1240
    • Kadaba, S.1    Krueger, A.2    Trice, T.3    Krecic, A.M.4    Hinnebusch, A.G.5    Anderson, J.6
  • 56
    • 2342574137 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis Rv2118c codes for a single-component homotetrameric m1A58 tRNA methyltransferase
    • Varshney U., Ramesh V., Madabushi A., Gaur R., Subramanya H.S., and RajBhandary U.L. Mycobacterium tuberculosis Rv2118c codes for a single-component homotetrameric m1A58 tRNA methyltransferase. Nucleic Acids Res. 32 (2004) 1018-1027
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1018-1027
    • Varshney, U.1    Ramesh, V.2    Madabushi, A.3    Gaur, R.4    Subramanya, H.S.5    RajBhandary, U.L.6
  • 58
    • 0029077732 scopus 로고
    • An anticodon sequence mutant of Escherichia coli initiator tRNA: possible importance of a newly acquired base modification next to the anticodon on its activity in initiation
    • Mangroo D., Limbach P.A., McCloskey J.A., and RajBhandary U.L. An anticodon sequence mutant of Escherichia coli initiator tRNA: possible importance of a newly acquired base modification next to the anticodon on its activity in initiation. J. Bacteriol. 177 (1995) 2858-2862
    • (1995) J. Bacteriol. , vol.177 , pp. 2858-2862
    • Mangroo, D.1    Limbach, P.A.2    McCloskey, J.A.3    RajBhandary, U.L.4
  • 59
    • 0025018043 scopus 로고
    • Domains of initiator tRNA and initiation codon crucial for initiator tRNA selection by Escherichia coli IF3
    • Hartz D., Binkley J., Hollingsworth T., and Gold L. Domains of initiator tRNA and initiation codon crucial for initiator tRNA selection by Escherichia coli IF3. Genes Dev. 4 (1990) 1790-1800
    • (1990) Genes Dev. , vol.4 , pp. 1790-1800
    • Hartz, D.1    Binkley, J.2    Hollingsworth, T.3    Gold, L.4
  • 60
    • 0034955379 scopus 로고    scopus 로고
    • Altered discrimination of start codons and initiator tRNAs by mutant initiation factor 3
    • O'Connor M., Gregory S.T., RajBhandary U.L., and Dahlberg A.E. Altered discrimination of start codons and initiator tRNAs by mutant initiation factor 3. RNA 7 (2001) 969-978
    • (2001) RNA , vol.7 , pp. 969-978
    • O'Connor, M.1    Gregory, S.T.2    RajBhandary, U.L.3    Dahlberg, A.E.4
  • 62
    • 0034759978 scopus 로고    scopus 로고
    • Interaction of translation initiation factor 3 with the 30S ribosomal subunit
    • Dallas A., and Noller H.F. Interaction of translation initiation factor 3 with the 30S ribosomal subunit. Mol. Cell 8 (2001) 855-864
    • (2001) Mol. Cell , vol.8 , pp. 855-864
    • Dallas, A.1    Noller, H.F.2
  • 63
    • 27944442879 scopus 로고    scopus 로고
    • Involvement of 16S rRNA nucleotides G1338 and A1339 in discrimination of initiator tRNA
    • Lancaster L., and Noller H.F. Involvement of 16S rRNA nucleotides G1338 and A1339 in discrimination of initiator tRNA. Mol. Cell 20 (2005) 623-632
    • (2005) Mol. Cell , vol.20 , pp. 623-632
    • Lancaster, L.1    Noller, H.F.2
  • 64
    • 36249023651 scopus 로고    scopus 로고
    • Characterization of 16S rRNA mutations that decrease the fidelity of translation initiation
    • Qin D., Abdi N.M., and Fredrick K. Characterization of 16S rRNA mutations that decrease the fidelity of translation initiation. RNA 13 (2007) 2348-2355
    • (2007) RNA , vol.13 , pp. 2348-2355
    • Qin, D.1    Abdi, N.M.2    Fredrick, K.3
  • 65
    • 33745943856 scopus 로고    scopus 로고
    • How initiation factors maximize the accuracy of tRNA selection in initiation of bacterial protein synthesis
    • Antoun A., Pavlov M.Y., Lovmar M., and Ehrenberg M. How initiation factors maximize the accuracy of tRNA selection in initiation of bacterial protein synthesis. Mol. Cell 23 (2006) 183-193
    • (2006) Mol. Cell , vol.23 , pp. 183-193
    • Antoun, A.1    Pavlov, M.Y.2    Lovmar, M.3    Ehrenberg, M.4
  • 67
    • 50049130690 scopus 로고    scopus 로고
    • Genetic identification of yeast 18S rRNA residues required for efficient recruitment of initiator tRNA(Met) and AUG selection
    • Dong J., Nanda J.S., Rahman H., Pruitt M.R., Shin B.S., Wong C.M., Lorsch J.R., and Hinnebusch A.G. Genetic identification of yeast 18S rRNA residues required for efficient recruitment of initiator tRNA(Met) and AUG selection. Genes Dev. 22 (2008) 2242-2255
    • (2008) Genes Dev. , vol.22 , pp. 2242-2255
    • Dong, J.1    Nanda, J.S.2    Rahman, H.3    Pruitt, M.R.4    Shin, B.S.5    Wong, C.M.6    Lorsch, J.R.7    Hinnebusch, A.G.8
  • 68
    • 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. 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
  • 69
    • 31344481752 scopus 로고    scopus 로고
    • Communication between eukaryotic translation initiation factors 5 and 1A within the ribosomal pre-initiation complex plays a role in start site selection
    • Maag D., Algire M.A., and Lorsch J.R. Communication between eukaryotic translation initiation factors 5 and 1A within the ribosomal pre-initiation complex plays a role in start site selection. J. Mol. Biol. 356 (2006) 724-737
    • (2006) J. Mol. Biol. , vol.356 , pp. 724-737
    • Maag, D.1    Algire, M.A.2    Lorsch, J.R.3
  • 70
    • 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. N- and C-terminal residues of eIF1A have opposing effects on the fidelity of start codon selection. EMBO J. 26 (2007) 1602-1614
    • (2007) EMBO J. , vol.26 , pp. 1602-1614
    • Fekete, C.A.1
  • 71
    • 0024280899 scopus 로고
    • tRNAi(met) functions in directing the scanning ribosome to the start site of translation
    • Cigan A.M., Feng L., and Donahue T.F. tRNAi(met) functions in directing the scanning ribosome to the start site of translation. Science 242 (1988) 93-97
    • (1988) Science , vol.242 , pp. 93-97
    • Cigan, A.M.1    Feng, L.2    Donahue, T.F.3
  • 72
    • 58149104495 scopus 로고    scopus 로고
    • Kinetic and thermodynamic analysis of the role of start codon/anticodon base pairing during eukaryotic translation initiation
    • Kolitz S.E., Takacs J.E., and Lorsch J.R. Kinetic and thermodynamic analysis of the role of start codon/anticodon base pairing during eukaryotic translation initiation. RNA 15 (2009) 138-152
    • (2009) RNA , vol.15 , pp. 138-152
    • Kolitz, S.E.1    Takacs, J.E.2    Lorsch, J.R.3
  • 73
    • 18844408328 scopus 로고    scopus 로고
    • An active role for tRNA in decoding beyond codon:anticodon pairing
    • Cochella L., and Green R. An active role for tRNA in decoding beyond codon:anticodon pairing. Science 308 (2005) 1178-1180
    • (2005) Science , vol.308 , pp. 1178-1180
    • Cochella, L.1    Green, R.2
  • 74
    • 0017140445 scopus 로고
    • Codon-dependent rearrangement of the three-dimensional structure of phenylalanine tRNA, exposing the T-psi-C-G sequence for binding to the 50S ribosomal subunit
    • Schwarz U., Menzel H.M., and Gassen H.G. Codon-dependent rearrangement of the three-dimensional structure of phenylalanine tRNA, exposing the T-psi-C-G sequence for binding to the 50S ribosomal subunit. Biochemistry 15 (1976) 2484-2490
    • (1976) Biochemistry , vol.15 , pp. 2484-2490
    • Schwarz, U.1    Menzel, H.M.2    Gassen, H.G.3
  • 75
    • 0019169607 scopus 로고
    • Comparison of the structures of free and ribosome-bound tRNAPhe by using slow tritium exchange
    • Farber N., and Cantor C.R. Comparison of the structures of free and ribosome-bound tRNAPhe by using slow tritium exchange. Proc. Natl. Acad. Sci. USA 77 (1980) 5135-5139
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 5135-5139
    • Farber, N.1    Cantor, C.R.2
  • 76
    • 0021100578 scopus 로고
    • Structural investigation of Phe-tRNAPhe from E. coli bound to the ribosomal A-site
    • Bertram S., Goringer U., and Wagner R. Structural investigation of Phe-tRNAPhe from E. coli bound to the ribosomal A-site. Nucleic Acids Res. 11 (1983) 575-589
    • (1983) Nucleic Acids Res. , vol.11 , pp. 575-589
    • Bertram, S.1    Goringer, U.2    Wagner, R.3
  • 77
    • 0022666946 scopus 로고
    • Anticodon-anticodon interaction induces conformational changes in tRNA: yeast tRNAAsp, a model for tRNA-mRNA recognition
    • Moras D., Dock A.C., Dumas P., Westhof E., Romby P., Ebel J.P., and Giege R. Anticodon-anticodon interaction induces conformational changes in tRNA: yeast tRNAAsp, a model for tRNA-mRNA recognition. Proc. Natl. Acad. Sci. USA 83 (1986) 932-936
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 932-936
    • Moras, D.1    Dock, A.C.2    Dumas, P.3    Westhof, E.4    Romby, P.5    Ebel, J.P.6    Giege, R.7
  • 78
    • 0028109919 scopus 로고
    • Transient conformational states of aminoacyl-tRNA during ribosome binding catalyzed by elongation factor Tu
    • Rodnina M.V., Fricke R., and Wintermeyer W. Transient conformational states of aminoacyl-tRNA during ribosome binding catalyzed by elongation factor Tu. Biochemistry 33 (1994) 12267-12275
    • (1994) Biochemistry , vol.33 , pp. 12267-12275
    • Rodnina, M.V.1    Fricke, R.2    Wintermeyer, W.3
  • 79
    • 0029096083 scopus 로고
    • Interaction of tRNAs with the ribosome at the A and P sites
    • Dabrowski M., Spahn C.M., and Nierhaus K.H. Interaction of tRNAs with the ribosome at the A and P sites. EMBO J. 14 (1995) 4872-4882
    • (1995) EMBO J. , vol.14 , pp. 4872-4882
    • Dabrowski, M.1    Spahn, C.M.2    Nierhaus, K.H.3
  • 82
    • 20444365142 scopus 로고    scopus 로고
    • The cryo-EM structure of a translation initiation complex from Escherichia coli
    • Allen G.S., Zavialov A., Gursky R., Ehrenberg M., and Frank J. The cryo-EM structure of a translation initiation complex from Escherichia coli. Cell 121 (2005) 703-712
    • (2005) Cell , vol.121 , pp. 703-712
    • Allen, G.S.1    Zavialov, A.2    Gursky, R.3    Ehrenberg, M.4    Frank, J.5
  • 84
    • 0034903851 scopus 로고    scopus 로고
    • Translation: in retrospect and prospect
    • Woese C.R. Translation: in retrospect and prospect. RNA 7 (2001) 1055-1067
    • (2001) RNA , vol.7 , pp. 1055-1067
    • Woese, C.R.1


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