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Volumn 3, Issue 7, 1997, Pages 721-733

Transfer RNA recognition by the Escherichia coli Δ2-isopentenyl-pyrophosphate:tRNA Δ2-isopentenyl transferase: Dependence on the anticodon arm structure

Author keywords

Anticodon; Dimethylallyl diphosphate:tRNA dimethylallyltransferase; Identity elements; Isopentenyladenosine; Maturation; Modifying enzymes; Transferase; tRNA; tRNA prenyl transferase

Indexed keywords

PYROPHOSPHATE; TRANSFER RNA; TRANSFERASE;

EID: 0030750024     PISSN: 13558382     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (38)

References (67)
  • 2
    • 0014968396 scopus 로고
    • 6-(Δ-isopentenyl)-adenodine: Biosynthesis in vitro in transfer RNA by an enzyme purified from Escherichia coli
    • 6-(Δ-isopentenyl)-adenodine: Biosynthesis in vitro in transfer RNA by an enzyme purified from Escherichia coli. Biochem Biophys Res Commun 40:1481-1487.
    • (1970) Biochem Biophys Res Commun , vol.40 , pp. 1481-1487
    • Bartz, J.K.1    Kline, L.K.2    Söll, D.3
  • 3
    • 0002495140 scopus 로고
    • Biosynthesis and function of modified nucleosides
    • Söll D, RajBhandary U, eds. Washington: ASM Press
    • Björk GR. 1995a. Biosynthesis and function of modified nucleosides. In: Söll D, RajBhandary U, eds. tRNA Structure, biosynthesis and function. Washington: ASM Press. pp 165-205.
    • (1995) tRNA Structure, Biosynthesis and Function , pp. 165-205
    • Björk, G.R.1
  • 4
    • 0029169650 scopus 로고
    • Genetic dissection of synthesis and function of modified nucleosides in bacterial transfer RNA
    • Björk GR. 1995b. Genetic dissection of synthesis and function of modified nucleosides in bacterial transfer RNA. Prog Nucleic Acid Res Mol Biol 50:263-338.
    • (1995) Prog Nucleic Acid Res Mol Biol , vol.50 , pp. 263-338
    • Björk, G.R.1
  • 5
    • 0021256993 scopus 로고
    • A modified nucleoside in tRNA as a possible regulator of aerobiosis
    • Buck M, Ames B. 1984. A modified nucleoside in tRNA as a possible regulator of aerobiosis. Cell 36:523-531.
    • (1984) Cell , vol.36 , pp. 523-531
    • Buck, M.1    Ames, B.2
  • 6
    • 0028358669 scopus 로고
    • Modulation of the suppression efficiency and amino acid identity of an artificial yeast amber isoleucine transfer RNA in Escherichia coli by a G*U pair in the anticodon stem
    • Buttcher V, Senger B, Schumacher S, Reinbolt J, Fasiolo F. 1994. Modulation of the suppression efficiency and amino acid identity of an artificial yeast amber isoleucine transfer RNA in Escherichia coli by a G*U pair in the anticodon stem. Biochem Biophys Res Commun 200:370-377.
    • (1994) Biochem Biophys Res Commun , vol.200 , pp. 370-377
    • Buttcher, V.1    Senger, B.2    Schumacher, S.3    Reinbolt, J.4    Fasiolo, F.5
  • 8
    • 0016187305 scopus 로고
    • Genetic alteration of structure and function in glycine transfer RNA of Escherichia coli: Mechanism of suppression of the tryptophan synthetase A78 mutation
    • Carbon J. Fleck EW. 1974 Genetic alteration of structure and function in glycine transfer RNA of Escherichia coli: Mechanism of suppression of the tryptophan synthetase A78 mutation. J Mol Biol 85:371-391.
    • (1974) J Mol Biol , vol.85 , pp. 371-391
    • Carbon, J.1    Fleck, E.W.2
  • 9
    • 0024371122 scopus 로고
    • 2-isopentenyl)-adenosine tRNA modification, and spontaneous mutagenesis in Eschericia coli K-12
    • 2-isopentenyl)-adenosine tRNA modification, and spontaneous mutagenesis in Eschericia coli K-12 J Bacteriol 171:3233-3246.
    • (1989) J Bacteriol , vol.171 , pp. 3233-3246
    • Connolly, D.M.1    Winkler, M.E.2
  • 10
    • 0029116609 scopus 로고
    • tRNA-guanine transglycosylase from Eschericia coli - Minimal tRNA structure and squence requirements for recognition
    • Curnow AW, Garcia GA. 1995. tRNA-guanine transglycosylase from Eschericia coli - Minimal tRNA structure and squence requirements for recognition. J Biol Chem 270:17264-17267.
    • (1995) J Biol Chem , vol.270 , pp. 17264-17267
    • Curnow, A.W.1    Garcia, G.A.2
  • 11
    • 0023084849 scopus 로고
    • Isolation and characterization of MOD5, a gene required for isopentenylation of cytoplasmic and mitochondrial tRNAs of Saccharomyces cerevisiae
    • Dihanich ME, Najarian D, Clark R, Gillman EC, Martin NC, Hopper AK. 1987. Isolation and characterization of MOD5, a gene required for isopentenylation of cytoplasmic and mitochondrial tRNAs of Saccharomyces cerevisiae, Mol Cell Biol 7:177-184.
    • (1987) Mol Cell Biol , vol.7 , pp. 177-184
    • Dihanich, M.E.1    Najarian, D.2    Clark, R.3    Gillman, E.C.4    Martin, N.C.5    Hopper, A.K.6
  • 13
    • 0026068372 scopus 로고
    • Phe in a homologous yeast in vitro system
    • Phe in a homologous yeast in vitro system. Biochimie 73:1021-1025.
    • (1991) Biochimie , vol.73 , pp. 1021-1025
    • Droogmans, L.1    Grosjean, H.2
  • 14
    • 0022410359 scopus 로고
    • Serine-specific tRNAs in Escherichia coli: Relative abundance and sequence
    • Fischer W, Sprinzl M. 1985. Serine-specific tRNAs in Escherichia coli: Relative abundance and sequence. Biochem Int 11:661-668.
    • (1985) Biochem Int , vol.11 , pp. 661-668
    • Fischer, W.1    Sprinzl, M.2
  • 15
    • 0014427414 scopus 로고
    • 2-isopentenyl)-adenosine: Biosynthesis in vitro by an enzyme extract from yeast and rat liver
    • 2-isopentenyl)-adenosine: Biosynthesis in vitro by an enzyme extract from yeast and rat liver. Biochem Biophys Res Commun 31:571-576.
    • (1968) Biochem Biophys Res Commun , vol.31 , pp. 571-576
    • Fittler, F.1    Kline, L.K.2    Hall, R.H.3
  • 17
    • 0014667184 scopus 로고
    • 6(γ′γ-dimethylallyl)-adenosine in transfer RNA of Escherichia coli
    • 6(γ′γ-dimethylallyl)-adenosine in transfer RNA of Escherichia coli. Biochem Biophys Res Commun 36: 435-441.
    • (1969) Biochem Biophys Res Commun , vol.36 , pp. 435-441
    • Gefter, M.L.1
  • 19
    • 8344231824 scopus 로고
    • RNA bent for recognition
    • Green MR. 1991. RNA bent for recognition. Curr Biol 1:245-247.
    • (1991) Curr Biol , vol.1 , pp. 245-247
    • Green, M.R.1
  • 21
    • 0029966338 scopus 로고    scopus 로고
    • Enzymatic formation of modified nucleosides in tRNA: Dependence on tRNA architecture
    • Grosjean H, Edqvist J, Straby KB, Giegé R. 1996. Enzymatic formation of modified nucleosides in tRNA: Dependence on tRNA architecture. J Mol Biol 255:67-85.
    • (1996) J Mol Biol , vol.255 , pp. 67-85
    • Grosjean, H.1    Edqvist, J.2    Straby, K.B.3    Giegé, R.4
  • 22
    • 0022424144 scopus 로고
    • Nucleobde sequences of two serine tRNAs with a GGA anticodon: The structure-function relationships in the serine family of E. coli tRNAs
    • Grosjean H. Nicoghosian K, Haumont E, Söll D, Cedergren R. 1985. Nucleobde sequences of two serine tRNAs with a GGA anticodon: The structure-function relationships in the serine family of E. coli tRNAs. Nucleic Acids Res 13:5697-5706.
    • (1985) Nucleic Acids Res , vol.13 , pp. 5697-5706
    • Grosjean, H.1    Nicoghosian, K.2    Haumont, E.3    Söll, D.4    Cedergren, R.5
  • 23
    • 0014723638 scopus 로고
    • 2-isopentenyl)-adenosine: Chemical reactions, biosynthesis, metabolism, and significance to the structure and function of tRNA
    • 2-isopentenyl)-adenosine: Chemical reactions, biosynthesis, metabolism, and significance to the structure and function of tRNA. Prog Nucleic Acid Res Mol Biol 10:57-86.
    • (1970) Prog Nucleic Acid Res Mol Biol , vol.10 , pp. 57-86
    • Hall, R.H.1
  • 24
    • 0024284965 scopus 로고
    • A simple structural feature is a major determinant of the identity of a transfer RNA
    • Hou YM, Schimmel P. 1968. A simple structural feature is a major determinant of the identity of a transfer RNA. Nature 333:140-145.
    • (1968) Nature , vol.333 , pp. 140-145
    • Hou, Y.M.1    Schimmel, P.2
  • 25
    • 0014597878 scopus 로고
    • 2-isopentenyl)-adenosine. Biosynthesis in transfer ribonucleic acid in vitro
    • 2-isopentenyl)-adenosine. Biosynthesis in transfer ribonucleic acid in vitro. Biochemistry 8:4361-4371.
    • (1969) Biochemistry , vol.8 , pp. 4361-4371
    • Kline, L.K.1    Fittler, F.2    Hall, R.H.3
  • 26
    • 0021687639 scopus 로고
    • Different base/base mismatches are corrected with different efficiencies by the methyldirected DNA mismatch-repair system of E. coli
    • Kramer B, Kramer W, Fritz HJ. 1984 Different base/base mismatches are corrected with different efficiencies by the methyldirected DNA mismatch-repair system of E. coli. Cell 38:879-887.
    • (1984) Cell , vol.38 , pp. 879-887
    • Kramer, B.1    Kramer, W.2    Fritz, H.J.3
  • 27
    • 0017411721 scopus 로고
    • Complementary specificity of restriction endonucleases of Diplococcus pneuminiae with respect to DNA methylation
    • Lacks S, Greenberg B. 1977 Complementary specificity of restriction endonucleases of Diplococcus pneuminiae with respect to DNA methylation. J Mol Biol 114:153-168.
    • (1977) J Mol Biol , vol.114 , pp. 153-168
    • Lacks, S.1    Greenberg, B.2
  • 28
    • 0030926773 scopus 로고    scopus 로고
    • Regulation of substrate recognition by the MiaA tRNA prenyl transferase modification enzyme of Escherichia coli K-12
    • Forthcoming
    • Leung HCE, Chen Y, Winkler ME. 1997. Regulation of substrate recognition by the MiaA tRNA prenyl transferase modification enzyme of Escherichia coli K-12. J Biol Chem. Forthcoming.
    • (1997) J Biol Chem.
    • Leung, H.C.E.1    Chen, Y.2    Winkler, M.E.3
  • 31
    • 0029917148 scopus 로고    scopus 로고
    • Single atomic group in RNA helix needed for positive and negative tRNA synthetase discrimination
    • Liu HJ, Yap LP, Musier-Forsyth K. 1996. Single atomic group in RNA helix needed for positive and negative tRNA synthetase discrimination. J Am Chem Soc 118:2523-2524.
    • (1996) J Am Chem Soc , vol.118 , pp. 2523-2524
    • Liu, H.J.1    Yap, L.P.2    Musier-Forsyth, K.3
  • 32
    • 0027366671 scopus 로고
    • Reproducing the three-dimensional structure of a tRNA molecule from structural constrants
    • Major F, Gauthetet D, Cedergren R. 1993. Reproducing the three-dimensional structure of a tRNA molecule from structural constrants. Proc Natl Acad Sci USA 90:9408-9412.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9408-9412
    • Major, F.1    Gauthetet, D.2    Cedergren, R.3
  • 33
    • 0029904026 scopus 로고    scopus 로고
    • Role of the three consecutive G:C base pairs conserved in the anticodon stem of initiator tRNA in initiation of protein synthesis in Escherichia coli
    • Mandal N, Mangroo D, Dalluge JJ, McCloskey JA, RajBhandary UL. 1996. Role of the three consecutive G:C base pairs conserved in the anticodon stem of initiator tRNA in initiation of protein synthesis in Escherichia coli. RNA 2:473-482.
    • (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
  • 34
    • 0029077732 scopus 로고
    • An anticodon sequnce 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 PA, McCloskey JA, RajBhandary UL. 1995. An anticodon sequnce 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 177:2858-2862.
    • (1995) J Bacteriol , vol.177 , pp. 2858-2862
    • Mangroo, D.1    Limbach, P.A.2    McCloskey, J.A.3    RajBhandary, U.L.4
  • 35
    • 0031019672 scopus 로고    scopus 로고
    • Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: A binding mechanism for recombinant enzyme
    • Moore JA, Poulter CD. 1997. Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: A binding mechanism for recombinant enzyme. Biochemistry 36:604-614.
    • (1997) Biochemistry , vol.36 , pp. 604-614
    • Moore, J.A.1    Poulter, C.D.2
  • 36
    • 0022328469 scopus 로고
    • tRNA, suppression, and the code
    • Murgola EJ. 1985. tRNA, suppression, and the code. Annu Rev Genet 19:57-80.
    • (1985) Annu Rev Genet , vol.19 , pp. 57-80
    • Murgola, E.J.1
  • 37
    • 0002229790 scopus 로고
    • Translational supression: When two wrongs do make a right
    • Söll D, RajBhandary U, eds. Washinton: ASM Press
    • Murgola EJ. 1995. Translational supression: When two wrongs do make a right. In: Söll D, RajBhandary U, eds. tRNA: Structure, biosynthesis and function. Washinton: ASM Press. pp 491-509.
    • (1995) tRNA: Structure, Biosynthesis and Function , pp. 491-509
    • Murgola, E.J.1
  • 39
    • 0021349997 scopus 로고
    • Missense and nonsense suppressors derived from a glycine tRNA by nucleotide insertion and deletion in vivo
    • Murgola EJ. Prather NE, Pagel FT, Mims BH, Hijazi KA. 1984. Missense and nonsense suppressors derived from a glycine tRNA by nucleotide insertion and deletion in vivo. Mol Gen Genet 193: 76-91.
    • (1984) Mol Gen Genet , vol.193 , pp. 76-91
    • Murgola, E.J.1    Prather, N.E.2    Pagel, F.T.3    Mims, B.H.4    Hijazi, K.A.5
  • 40
    • 0027536912 scopus 로고
    • Aminoacylation of RNA oligonucleotides - Minimalist structures and origin of specificity
    • Musier-Forsyth K, Schimmel P. 1993. Aminoacylation of RNA oligonucleotides - Minimalist structures and origin of specificity. FASEB J 7:282-289.
    • (1993) FASEB J , vol.7 , pp. 282-289
    • Musier-Forsyth, K.1    Schimmel, P.2
  • 41
    • 0023080579 scopus 로고
    • DNA sequence and transcript mapping of MOD5: Features of the 5′ region which suggest two translational starts
    • Najarian D. Dihanich ME, Martin NC, Hopper AK. 1987. DNA sequence and transcript mapping of MOD5: Features of the 5′ region which suggest two translational starts. Mol Cell Biol 7:185-191.
    • (1987) Mol Cell Biol , vol.7 , pp. 185-191
    • Najarian, D.1    Dihanich, M.E.2    Martin, N.C.3    Hopper, A.K.4
  • 42
    • 0028595685 scopus 로고
    • A UGU sequence in the anticodon loop is a minimum requirement for recognition by Escherichia coli tRNA-guanine transglycosylase
    • Nakanishi S, Ueda T, Hori H, Yamazaki N, Okada N, Watanabe K. 1994. A UGU sequence in the anticodon loop is a minimum requirement for recognition by Escherichia coli tRNA-guanine transglycosylase. J Biol Chem 269:32221-32225.
    • (1994) J Biol Chem , vol.269 , pp. 32221-32225
    • Nakanishi, S.1    Ueda, T.2    Hori, H.3    Yamazaki, N.4    Okada, N.5    Watanabe, K.6
  • 43
    • 0015278178 scopus 로고
    • Minor components in transfer RNA: Their characterization, location, and function
    • Nishimura S. 1972. Minor components in transfer RNA: Their characterization, location, and function. Prog Nucleic Acid Res Mol Biol 12:49-85.
    • (1972) Prog Nucleic Acid Res Mol Biol , vol.12 , pp. 49-85
    • Nishimura, S.1
  • 46
    • 0026315514 scopus 로고
    • Folding of circularly permuted transfer RNAs
    • Pan T, Gutell RR, Uhlenbeck OC. 1991. Folding of circularly permuted transfer RNAs. Science 254:1361-1364.
    • (1991) Science , vol.254 , pp. 1361-1364
    • Pan, T.1    Gutell, R.R.2    Uhlenbeck, O.C.3
  • 48
    • 0028609454 scopus 로고
    • Synthesis and function of isopentenyl adenosine derivatives in tRNA
    • Persson BC, Esberg B, Olafsson O, Björk GR. 1994. Synthesis and function of isopentenyl adenosine derivatives in tRNA. Biochimie 76:1152-1160.
    • (1994) Biochimie , vol.76 , pp. 1152-1160
    • Persson, B.C.1    Esberg, B.2    Olafsson, O.3    Björk, G.R.4
  • 49
    • 0021100349 scopus 로고
    • supG and supL in Escherichia coli code for mutant lysine tRNAs
    • Prather NE, Mims BH, Murgola EJ. 1983. supG and supL in Escherichia coli code for mutant lysine tRNAs. Nucleic Acids Res 11:8283-8286.
    • (1983) Nucleic Acids Res , vol.11 , pp. 8283-8286
    • Prather, N.E.1    Mims, B.H.2    Murgola, E.J.3
  • 50
    • 0019844244 scopus 로고
    • Nucleotide insertion in the anticodon loop of a glycine transfer RNA causes missense suppression
    • Prather NE, Murgola EJ, Mims BH. 1981a. Nucleotide insertion in the anticodon loop of a glycine transfer RNA causes missense suppression. Proc Natl Acad Sci USA 78:7408-7411.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 7408-7411
    • Prather, N.E.1    Murgola, E.J.2    Mims, B.H.3
  • 51
    • 0019878337 scopus 로고
    • Primary structure of an unusual glycine tRNA UGA suppressor
    • Prather NE, Murgola EJ, Mims BH. 1981b. Primary structure of an unusual glycine tRNA UGA suppressor. Nucleic Acids Res 9:6421-6428.
    • (1981) Nucleic Acids Res , vol.9 , pp. 6421-6428
    • Prather, N.E.1    Murgola, E.J.2    Mims, B.H.3
  • 52
    • 0023338540 scopus 로고
    • Glu-Suoc a more efficient suppressor
    • Glu-Suoc a more efficient suppressor. EMBO J 6:1449-1506.
    • (1987) EMBO J , vol.6 , pp. 1449-1506
    • Raftery, L.A.1    Yarus, M.2
  • 53
    • 0016341896 scopus 로고
    • Molecular mechanism for missense suppresion in E. coli
    • Roberts JW, Carbon J. 1974. Molecular mechanism for missense suppresion in E. coli. Nature 250:412-414.
    • (1974) Nature , vol.250 , pp. 412-414
    • Roberts, J.W.1    Carbon, J.2
  • 54
    • 0029991713 scopus 로고    scopus 로고
    • Crystal structure of tRNA-guanine transglycosylase: RNA modification by base exchange
    • Roier C, Reuter K, Suck D, Ficner R. 1996. Crystal structure of tRNA-guanine transglycosylase: RNA modification by base exchange. EMBO J 15:2850-2857.
    • (1996) EMBO J , vol.15 , pp. 2850-2857
    • Roier, C.1    Reuter, K.2    Suck, D.3    Ficner, R.4
  • 55
    • 0015523674 scopus 로고
    • 2-isopentenylpyrophosphate: Transfer ribonucleic acid 2-isopentenyltranferase from Escherichia coli. Purification and properties of the enzyme
    • 2-isopentenylpyrophosphate: transfer ribonucleic acid 2-isopentenyltranferase from Escherichia coli. Purification and properties of the enzyme. J Biol Chem 247:5675-5680.
    • (1972) J Biol Chem , vol.247 , pp. 5675-5680
    • Rosenbaum, N.1    Gefter, M.L.2
  • 60
    • 0024451607 scopus 로고
    • The selenocysteineinserting opal suppressor serine tRNA from E. coli is highly unsual in structure and modification
    • Schön A, Bock A, Ott G, Sprinzl M, Söll D. 1989. The selenocysteineinserting opal suppressor serine tRNA from E. coli is highly unsual in structure and modification. Nucleic Acids Res 17:7159-7165.
    • (1989) Nucleic Acids Res , vol.17 , pp. 7159-7165
    • Schön, A.1    Bock, A.2    Ott, G.3    Sprinzl, M.4    Söll, D.5
  • 63
    • 0021049671 scopus 로고
    • Sequence specificity of tRNA-modifying enzymes: An analysis of 258 tRNA sequences
    • Tsang TH, Ames BN, Buck M. 1983. Sequence specificity of tRNA-modifying enzymes: An analysis of 258 tRNA sequences. Biochim Biophys Acta 741:180-196.
    • (1983) Biochim Biophys Acta , vol.741 , pp. 180-196
    • Tsang, T.H.1    Ames, B.N.2    Buck, M.3
  • 65
    • 0019913580 scopus 로고
    • Translational efficiency of tRNA's: Uses of and extended anticodon
    • Yarus M. 1982. Translational efficiency of tRNA's: Uses of and extended anticodon. Science 218:646-652.
    • (1982) Science , vol.218 , pp. 646-652
    • Yarus, M.1
  • 66
    • 0023027061 scopus 로고
    • The translational efficiency of tRNA is a property of the anticodon arm
    • Yarus M, Cline SW, Raftery L, Wier P, Bradley D. 1986. The translational efficiency of tRNA is a property of the anticodon arm. J Biol Chem 261:10496-10505.
    • (1986) J Biol Chem , vol.261 , pp. 10496-10505
    • Yarus, M.1    Cline, S.W.2    Raftery, L.3    Wier, P.4    Bradley, D.5
  • 67
    • 0017254452 scopus 로고
    • Aminoecylation and nucleotide modification of in vitro synthesised transfer RNA
    • Zeevi M, Daniel V. 1976. Aminoecylation and nucleotide modification of in vitro synthesised transfer RNA. Nature 260:72-74.
    • (1976) Nature , vol.260 , pp. 72-74
    • Zeevi, M.1    Daniel, V.2


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