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Volumn 338, Issue 3, 2004, Pages 439-444

Modified nucleotides in tRNALys and tRNAVal are important for translocation

Author keywords

ASL, anticodon stem loop; Decoding; mnm, methylaminomethyluridine; Ribosome; Translocation; tRNA; Wobble

Indexed keywords

AMINOACYL TRANSFER RNA; FUNCTIONAL GROUP; MESSENGER RNA; NUCLEOTIDE DERIVATIVE; PEPTIDE TRANSFER RIBONUCLEIC ACID; TRANSFER RNA; UNCLASSIFIED DRUG;

EID: 1842686227     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.02.070     Document Type: Article
Times cited : (57)

References (40)
  • 2
    • 0037415690 scopus 로고    scopus 로고
    • Wobble modification differences and subcellular localization of tRNAs in Leishmania tarentolae: Implication for tRNA sorting mechanism
    • Kaneko T., Suzuki T., Kapushoc S.T., Rubio M.A., Ghazvini J., et al. Wobble modification differences and subcellular localization of tRNAs in Leishmania tarentolae: implication for tRNA sorting mechanism. EMBO J. 22:2003;657-667.
    • (2003) EMBO J. , vol.22 , pp. 657-667
    • Kaneko, T.1    Suzuki, T.2    Kapushoc, S.T.3    Rubio, M.A.4    Ghazvini, J.5
  • 3
    • 0028180696 scopus 로고
    • Many of the conserved nucleotides of tRNA(Phe) are not essential for ternary complex formation and peptide elongation
    • Nazarenko I.A., Harrington K.M., Uhlenbeck O.C. Many of the conserved nucleotides of tRNA(Phe) are not essential for ternary complex formation and peptide elongation. EMBO J. 13:1994;2464-2471.
    • (1994) EMBO J. , vol.13 , pp. 2464-2471
    • Nazarenko, I.A.1    Harrington, K.M.2    Uhlenbeck, O.C.3
  • 4
    • 0033572751 scopus 로고    scopus 로고
    • Effect of modified nucleotides on Escherichia coli tRNAGlu structure and on its aminoacylation by glutamyl-tRNA synthetase. Predominant and distinct roles of the mnm5 and s2 modifications of U34
    • Madore E., Florentz C., Giege R., Sekine S., Yokoyama S., Lapointe J. Effect of modified nucleotides on Escherichia coli tRNAGlu structure and on its aminoacylation by glutamyl-tRNA synthetase. Predominant and distinct roles of the mnm5 and s2 modifications of U34. Eur. J. Biochem. 266:1999;1128-1135.
    • (1999) Eur. J. Biochem. , vol.266 , pp. 1128-1135
    • Madore, E.1    Florentz, C.2    Giege, R.3    Sekine, S.4    Yokoyama, S.5    Lapointe, J.6
  • 5
    • 10744229752 scopus 로고    scopus 로고
    • An RNA-modifying enzyme that governs both the codon and amino acid specificities of isoleucine tRNA
    • Soma A., Ikeuchi Y., Kanemasa S., Kobayashi K., Ogasawara N., Ote T., et al. An RNA-modifying enzyme that governs both the codon and amino acid specificities of isoleucine tRNA. Mol. Cell. 12:2003;689-698.
    • (2003) Mol. Cell. , vol.12 , pp. 689-698
    • Soma, A.1    Ikeuchi, Y.2    Kanemasa, S.3    Kobayashi, K.4    Ogasawara, N.5    Ote, T.6
  • 6
    • 0013997436 scopus 로고
    • The genetic code - Yesterday, today, and tomorrow
    • Crick F.H. The genetic code - yesterday, today, and tomorrow. Cold Spring Harbor Symp. Quant. Biol. 31:1966;1-9.
    • (1966) Cold Spring Harbor Symp. Quant. Biol. , vol.31 , pp. 1-9
    • Crick, F.H.1
  • 7
    • 0035801225 scopus 로고    scopus 로고
    • Wobble modification defect in tRNA disturbs codon-anticodon interaction in a mitochondrial disease
    • Yasukawa T., Suzuki T., Ishii N., Ohta S., Watanabe K. Wobble modification defect in tRNA disturbs codon-anticodon interaction in a mitochondrial disease. EMBO J. 20:2001;4794-4802.
    • (2001) EMBO J. , vol.20 , pp. 4794-4802
    • Yasukawa, T.1    Suzuki, T.2    Ishii, N.3    Ohta, S.4    Watanabe, K.5
  • 8
    • 0019828676 scopus 로고
    • Biological and structural differences between tRNAVal species isolated from rat ascites hepatoma cells and normal rat liver
    • Shindo-Okada N., Kuchino Y., Harada F., Okada N., Nishimura S. Biological and structural differences between tRNAVal species isolated from rat ascites hepatoma cells and normal rat liver. J. Biochem. (Tokyo). 90:1981;535-544.
    • (1981) J. Biochem. (Tokyo) , vol.90 , pp. 535-544
    • Shindo-Okada, N.1    Kuchino, Y.2    Harada, F.3    Okada, N.4    Nishimura, S.5
  • 10
    • 0034961959 scopus 로고    scopus 로고
    • Analysis of codon:anticodon interactions within the ribosome provides new insights into codon reading and the genetic code structure
    • Lim V.I., Curran J.F. Analysis of codon:anticodon interactions within the ribosome provides new insights into codon reading and the genetic code structure. RNA. 7:2001;942-957.
    • (2001) RNA , vol.7 , pp. 942-957
    • Lim, V.I.1    Curran, J.F.2
  • 12
    • 0035801515 scopus 로고    scopus 로고
    • Improvement of reading frame maintenance is a common function for several tRNA modifications
    • Urbonavicius J., Qian Q., Durand J.M., Hagervall T.G., Bjork G.R. Improvement of reading frame maintenance is a common function for several tRNA modifications. EMBO J. 20:2001;4863-4873.
    • (2001) EMBO J. , vol.20 , pp. 4863-4873
    • Urbonavicius, J.1    Qian, Q.2    Durand, J.M.3    Hagervall, T.G.4    Bjork, G.R.5
  • 13
    • 1342271370 scopus 로고    scopus 로고
    • Transfer RNA modifications that alter +1 frameshifting in general fail to affect -1 frameshifting
    • Urbonavicius J., Stahl G., Durand J.M., Ben Salem S.N., Qian Q., Farabaugh P.J., Bjork G.R. Transfer RNA modifications that alter +1 frameshifting in general fail to affect -1 frameshifting. RNA. 9:2003;760-768.
    • (2003) RNA , vol.9 , pp. 760-768
    • Urbonavicius, J.1    Stahl, G.2    Durand, J.M.3    Ben Salem, S.N.4    Qian, Q.5    Farabaugh, P.J.6    Bjork, G.R.7
  • 14
    • 0034603196 scopus 로고    scopus 로고
    • Large-scale movement of elongation factor G and extensive conformational change of the ribosome during translocation
    • Stark H., Rodnina M.V., Wieden H.J., van Heel M., Wintermeyer W. Large-scale movement of elongation factor G and extensive conformational change of the ribosome during translocation. Cell. 100:2000;301-309.
    • (2000) Cell , vol.100 , pp. 301-309
    • Stark, H.1    Rodnina, M.V.2    Wieden, H.J.3    Van Heel, M.4    Wintermeyer, W.5
  • 15
    • 0037154986 scopus 로고    scopus 로고
    • Ribosome structure and the mechanism of translation
    • Ramakrishnan V. Ribosome structure and the mechanism of translation. Cell. 108:2002;557-572.
    • (2002) Cell , vol.108 , pp. 557-572
    • Ramakrishnan, V.1
  • 16
    • 0036809730 scopus 로고    scopus 로고
    • Universally conserved interactions between the ribosome and the anticodon stem-loop of a site tRNA important for translocation
    • Phelps S.S., Jerinic O., Joseph S. Universally conserved interactions between the ribosome and the anticodon stem-loop of A site tRNA important for translocation. Mol. Cell. 10:2002;799-807.
    • (2002) Mol. Cell , vol.10 , pp. 799-807
    • Phelps, S.S.1    Jerinic, O.2    Joseph, S.3
  • 17
    • 0032617148 scopus 로고    scopus 로고
    • Thermodynamic contribution of nucleoside modifications to yeast tRNA(Phe) anticodon stem loop analogs
    • Agris P.F., Guenther R., Sochacka E., Newman W., Czerwinska G., Liu G., et al. Thermodynamic contribution of nucleoside modifications to yeast tRNA(Phe) anticodon stem loop analogs. Acta Biochim. Pol. 46:1999;163-172.
    • (1999) Acta Biochim. Pol. , vol.46 , pp. 163-172
    • Agris, P.F.1    Guenther, R.2    Sochacka, E.3    Newman, W.4    Czerwinska, G.5    Liu, G.6
  • 18
    • 0034619418 scopus 로고    scopus 로고
    • Functional anticodon architecture of human tRNALys3 includes disruption of intraloop hydrogen bonding by the naturally occurring amino acid modification, t6A
    • Stuart J.W., Gdaniec Z., Guenther R., Marszalek M., Sochacka E., Malkiewicz A., Agris P.F. Functional anticodon architecture of human tRNALys3 includes disruption of intraloop hydrogen bonding by the naturally occurring amino acid modification, t6A. Biochemistry. 39:2000;13396-13404.
    • (2000) Biochemistry , vol.39 , pp. 13396-13404
    • Stuart, J.W.1    Gdaniec, Z.2    Guenther, R.3    Marszalek, M.4    Sochacka, E.5    Malkiewicz, A.6    Agris, P.F.7
  • 19
    • 0034680364 scopus 로고    scopus 로고
    • Hypermodified nucleosides in the anticodon of tRNA(Lys) stabilize a canonical U-turn structure
    • Sundaram M., Durant P.C., Davis D.R. Hypermodified nucleosides in the anticodon of tRNA(Lys) stabilize a canonical U-turn structure. Biochemistry. 39:2000;15652.
    • (2000) Biochemistry , vol.39 , pp. 15652
    • Sundaram, M.1    Durant, P.C.2    Davis, D.R.3
  • 20
    • 0032526979 scopus 로고    scopus 로고
    • EF-G-catalyzed translocation of anticodon stem-loop analogs of transfer RNA in the ribosome
    • Joseph S., Noller H.F. EF-G-catalyzed translocation of anticodon stem-loop analogs of transfer RNA in the ribosome. EMBO J. 17:1998;3478-3483.
    • (1998) EMBO J. , vol.17 , pp. 3478-3483
    • Joseph, S.1    Noller, H.F.2
  • 21
    • 0037459218 scopus 로고    scopus 로고
    • Rapid kinetic analysis of EF-G-dependent mRNA translocation in the ribosome
    • Studer S.M., Feinberg J.S., Joseph S. Rapid kinetic analysis of EF-G-dependent mRNA translocation in the ribosome. J. Mol. Biol. 327:2003;369-381.
    • (2003) J. Mol. Biol. , vol.327 , pp. 369-381
    • Studer, S.M.1    Feinberg, J.S.2    Joseph, S.3
  • 22
    • 0028986353 scopus 로고
    • The methylthio group (ms2) of N6-(4-hydroxyisopentenyl)-2- methylthioadenosine (ms2io6A) present next to the anticodon contributes to the decoding efficiency of the tRNA
    • Esberg B., Bjork G.R. The methylthio group (ms2) of N6-(4- hydroxyisopentenyl)-2-methylthioadenosine (ms2io6A) present next to the anticodon contributes to the decoding efficiency of the tRNA. J. Bacteriol. 177:1995;1967-1975.
    • (1995) J. Bacteriol. , vol.177 , pp. 1967-1975
    • Esberg, B.1    Bjork, G.R.2
  • 23
    • 0017182937 scopus 로고
    • Structural domains of transfer RNA molecules
    • Quigley G.J., Rich A. Structural domains of transfer RNA molecules. Science. 194:1976;796-806.
    • (1976) Science , vol.194 , pp. 796-806
    • Quigley, G.J.1    Rich, A.2
  • 25
    • 0031023569 scopus 로고    scopus 로고
    • Identification of 2′-hydroxyl groups required for interaction of a tRNA anticodon stem-loop region with the ribosome
    • von Ahsen U., Green R., Schroeder R., Noller H.F. Identification of 2′-hydroxyl groups required for interaction of a tRNA anticodon stem-loop region with the ribosome. RNA. 3:1997;49-56.
    • (1997) RNA , vol.3 , pp. 49-56
    • Von Ahsen, U.1    Green, R.2    Schroeder, R.3    Noller, H.F.4
  • 26
    • 0033744175 scopus 로고    scopus 로고
    • The crystal structure of HIV reverse-transcription primer tRNA(Lys,3) shows a canonical anticodon loop
    • Benas P., Bec G., Keith G., Marquet R., Ehresmann C., Ehresmann B., Dumas P. The crystal structure of HIV reverse-transcription primer tRNA(Lys,3) shows a canonical anticodon loop. RNA. 6:2000;1347-1355.
    • (2000) RNA , vol.6 , pp. 1347-1355
    • Benas, P.1    Bec, G.2    Keith, G.3    Marquet, R.4    Ehresmann, C.5    Ehresmann, B.6    Dumas, P.7
  • 27
    • 0029894141 scopus 로고    scopus 로고
    • NMR studies of the effects of the 5′-phosphate group on conformational properties of 5-methylaminomethyluridine found in the first position of the anticodon of Escherichia coli tRNA(Arg)4
    • Sakamoto K., Kawai G., Watanabe S., Niimi T., Hayashi N., Muto Y., et al. NMR studies of the effects of the 5′-phosphate group on conformational properties of 5-methylaminomethyluridine found in the first position of the anticodon of Escherichia coli tRNA(Arg)4. Biochemistry. 35:1996;6533-6538.
    • (1996) Biochemistry , vol.35 , pp. 6533-6538
    • Sakamoto, K.1    Kawai, G.2    Watanabe, S.3    Niimi, T.4    Hayashi, N.5    Muto, Y.6
  • 29
    • 0000635454 scopus 로고
    • Thiolation of uridine carbon-2 restricts motional dynamics of the transfer RNA wobble position nucleoside
    • Agris P.F., et al. Thiolation of uridine carbon-2 restricts motional dynamics of the transfer RNA wobble position nucleoside. J. Am. Chem. Soc. 114:1992;2652-2656.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 2652-2656
    • Agris, P.F.1
  • 31
    • 0034699519 scopus 로고    scopus 로고
    • Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics
    • Carter A.P., Clemons W.M., Brodersen D.E., Morgan-Warren R.J., Wimberly B.T., Ramakrishnan V. Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics. Nature. 407:2000;340-348.
    • (2000) Nature , vol.407 , pp. 340-348
    • Carter, A.P.1    Clemons, W.M.2    Brodersen, D.E.3    Morgan-Warren, R.J.4    Wimberly, B.T.5    Ramakrishnan, V.6
  • 32
    • 0036303671 scopus 로고    scopus 로고
    • Solution conformations of unmodified and A(37)N(6)-dimethylallyl modified anticodon stem-loops of Escherichia coli tRNA(Phe)
    • Cabello-Villegas J., Winkler M.E., Nikonowicz E.P. Solution conformations of unmodified and A(37)N(6)-dimethylallyl modified anticodon stem-loops of Escherichia coli tRNA(Phe). J. Mol. Biol. 319:2002;1015-1034.
    • (2002) J. Mol. Biol. , vol.319 , pp. 1015-1034
    • Cabello-Villegas, J.1    Winkler, M.E.2    Nikonowicz, E.P.3
  • 33
    • 0021104265 scopus 로고
    • Binding of yeast tRNAPhe anticodon arm to Escherichia coli 30 S ribosomes
    • Rose S.J. III, Lowary P.T., Uhlenbeck O.C. Binding of yeast tRNAPhe anticodon arm to Escherichia coli 30 S ribosomes. J. Mol. Biol. 167:1983;103-117.
    • (1983) J. Mol. Biol. , vol.167 , pp. 103-117
    • Rose III, S.J.1    Lowary, P.T.2    Uhlenbeck, O.C.3
  • 34
    • 0026524798 scopus 로고
    • Conformational rigidity of specific pyrimidine residues in tRNA arises from posttranscriptional modifications that enhance steric interaction between the base and the 2′-hydroxyl group
    • Kawai G., Yamamoto Y., Kamimura T., Masegi T., Sekine M., Hata T., et al. Conformational rigidity of specific pyrimidine residues in tRNA arises from posttranscriptional modifications that enhance steric interaction between the base and the 2′-hydroxyl group. Biochemistry. 31:1992;1040-1046.
    • (1992) Biochemistry , vol.31 , pp. 1040-1046
    • Kawai, G.1    Yamamoto, Y.2    Kamimura, T.3    Masegi, T.4    Sekine, M.5    Hata, T.6
  • 36
    • 0034083601 scopus 로고    scopus 로고
    • Effects of anticodon 2′-O-methylations on tRNA codon recognition in an Escherichia coli cell-free translation
    • Satoh A., Takai K., Ouchi R., Yokoyama S., Takaku H. Effects of anticodon 2′-O-methylations on tRNA codon recognition in an Escherichia coli cell-free translation. RNA. 6:2000;680-686.
    • (2000) RNA , vol.6 , pp. 680-686
    • Satoh, A.1    Takai, K.2    Ouchi, R.3    Yokoyama, S.4    Takaku, H.5
  • 38
    • 1242309517 scopus 로고    scopus 로고
    • Decoding the genome, a modified view
    • Agris P.F. Decoding the genome, a modified view. Nucl. Acids Res. 32:2004;223-238.
    • (2004) Nucl. Acids Res. , vol.32 , pp. 223-238
    • Agris, P.F.1
  • 39
    • 0019913580 scopus 로고
    • Translational efficiency of transfer RNA's: Uses of an extended anticodon
    • Yarus M. Translational efficiency of transfer RNA's: uses of an extended anticodon. Science. 218:1982;646-652.
    • (1982) Science , vol.218 , pp. 646-652
    • Yarus, M.1
  • 40
    • 0024252185 scopus 로고
    • Extension inhibition analysis of translation initiation complexes
    • Hartz D., McPheeters D.S., Traut R., Gold L. Extension inhibition analysis of translation initiation complexes. Methods Enzymol. 164:1988;419-425.
    • (1988) Methods Enzymol. , vol.164 , pp. 419-425
    • Hartz, D.1    McPheeters, D.S.2    Traut, R.3    Gold, L.4


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