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Volumn 23, Issue 24, 2003, Pages 9283-9292

Novel Methyltransferase for Modified Uridine Residues at the Wobble Position of tRNA

Author keywords

[No Author keywords available]

Indexed keywords

5 METHYLCARBONYLMETHYL 2 THIOURIDINE; 5 METHYLCARBONYLMETHYLURIDINE; FUNGAL ENZYME; METHYLTRANSFERASE; PAROMOMYCIN; PROTEIN TRM9; TRANSFER RNA; UNCLASSIFIED DRUG; URIDINE DERIVATIVE;

EID: 0345060040     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.23.24.9283-9292.2003     Document Type: Article
Times cited : (134)

References (59)
  • 1
    • 0017749003 scopus 로고
    • Characterization of a unique enzyme complex composed of S-adenosyl-L-methionine-tRNA-methyltransferase and aminoacyl-tRNA synthetase activities
    • Agris, P. F., D. Setzer, and C. W. Gehrke. 1977. Characterization of a unique enzyme complex composed of S-adenosyl-L-methionine-tRNA-methyltransferase and aminoacyl-tRNA synthetase activities. Nucleic Acids Res. 4:38-43.
    • (1977) Nucleic Acids Res. , vol.4 , pp. 38-43
    • Agris, P.F.1    Setzer, D.2    Gehrke, C.W.3
  • 2
    • 0015868989 scopus 로고
    • Biological function of 2-thiouridine in Escherichia coli glutamic acid transfer ribonucleic acid
    • Agris, P. F., D. Soll, and T. Seno. 1973. Biological function of 2-thiouridine in Escherichia coli glutamic acid transfer ribonucleic acid. Biochemistry 12: 4331-4337.
    • (1973) Biochemistry , vol.12 , pp. 4331-4337
    • Agris, P.F.1    Soll, D.2    Seno, T.3
  • 3
    • 0036795285 scopus 로고    scopus 로고
    • Two proteins that form a complex are required for 7-methylguanosine modification of yeast tRNA
    • Alexandrov, A., M. R. Martzen, and E. M. Phizicky. 2002. Two proteins that form a complex are required for 7-methylguanosine modification of yeast tRNA. RNA 8:1253-1266.
    • (2002) RNA , vol.8 , pp. 1253-1266
    • Alexandrov, A.1    Martzen, M.R.2    Phizicky, E.M.3
  • 4
    • 0034625166 scopus 로고    scopus 로고
    • The Gcd10p/Gcd14p complex is the essential two-subunit tRNA(1-methyladenosine) methyltransferase of Saccharomyces cerevisiae
    • Anderson, J., L. Phan, and A. G. Hinnebusch. 2000. The Gcd10p/Gcd14p complex is the essential two-subunit tRNA(1-methyladenosine) methyltransferase of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 97:5173-5178.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5173-5178
    • Anderson, J.1    Phan, L.2    Hinnebusch, A.G.3
  • 5
    • 0014687549 scopus 로고
    • A convenient procedure for preparing transfer ribonucleic acid from Escherichia coli
    • Avital, S., and D. Elson. 1969. A convenient procedure for preparing transfer ribonucleic acid from Escherichia coli. Biochim. Biophys. Acta. 179:297-307.
    • (1969) Biochim. Biophys. Acta , vol.179 , pp. 297-307
    • Avital, S.1    Elson, D.2
  • 9
    • 0035856524 scopus 로고    scopus 로고
    • Identification of the gene and characterization of the activity of the trans-aconitate methyltransferase from Saccharomyces cerevisiae
    • Cai, H., D. Dumlao, J. E. Katz, and S. Clarke. 2001. Identification of the gene and characterization of the activity of the trans-aconitate methyltransferase from Saccharomyces cerevisiae. Biochemistry 40:13699-13709.
    • (2001) Biochemistry , vol.40 , pp. 13699-13709
    • Cai, H.1    Dumlao, D.2    Katz, J.E.3    Clarke, S.4
  • 10
    • 0034699519 scopus 로고    scopus 로고
    • Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics
    • Carter, A. P., W. M. Clemons, D. E. Brodersen, R. J. Morgan-Warren, B. T. Wimberly, and V. Ramakrishnan. 2000. Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics. Nature 407:340-348.
    • (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
  • 11
    • 0032953571 scopus 로고    scopus 로고
    • The yeast Saccharomyces cerevisiae YDL112w ORF encodes the putative 2′-O-ribose methyltransferase catalyzing the formation of Gm18 in tRNAs
    • Cavaille, J., F. Chetouani, and J. P. Bachellerie. 1999. The yeast Saccharomyces cerevisiae YDL112w ORF encodes the putative 2′-O-ribose methyltransferase catalyzing the formation of Gm18 in tRNAs. RNA 5:66-81.
    • (1999) RNA , vol.5 , pp. 66-81
    • Cavaille, J.1    Chetouani, F.2    Bachellerie, J.P.3
  • 12
    • 0016819021 scopus 로고
    • Primary structure of tRNA Arg II of E. coli
    • Chakraburtty, K. 1975. Primary structure of tRNA Arg II of E. coli. Nucleic Acids Res. 2:1787-1792.
    • (1975) Nucleic Acids Res. , vol.2 , pp. 1787-1792
    • Chakraburtty, K.1
  • 13
    • 0013936167 scopus 로고
    • Codon-anticodon pairing: The wobble hypothesis
    • Crick, F. H. 1966. Codon-anticodon pairing: the wobble hypothesis. J. Mol. Biol. 19:548-555.
    • (1966) J. Mol. Biol. , vol.19 , pp. 548-555
    • Crick, F.H.1
  • 14
    • 0022996130 scopus 로고
    • 2-dimethylguanosine modification of both mitochondrial and cytoplasmic tRNA in Saccharomyces cerevisiae
    • 2-dimethylguanosine modification of both mitochondrial and cytoplasmic tRNA in Saccharomyces cerevisiae. J. Biol. Chem. 261:9703-9709.
    • (1986) J. Biol. Chem. , vol.261 , pp. 9703-9709
    • Ellis, S.R.1    Morales, M.J.2    Li, J.M.3    Hopper, A.K.4    Martin, N.C.5
  • 15
    • 0026495913 scopus 로고
    • Mammalian small molecule methyltransferases: Their structural and functional features
    • Fujioka, M. 1992. Mammalian small molecule methyltransferases: their structural and functional features. Int. J. Biochem. 24:1917-1924.
    • (1992) Int. J. Biochem. , vol.24 , pp. 1917-1924
    • Fujioka, M.1
  • 16
    • 0001184472 scopus 로고    scopus 로고
    • Appendix III: General properties of RNA-modifying and -editing enzymes
    • H. Grosjean and R. Benne (ed.). ASM Press, Washington, D.C.
    • Garcia, G. A., and D. M. Goodenough-Lashua. 1998. Appendix III: general properties of RNA-modifying and -editing enzymes, p. 555-565. In H. Grosjean and R. Benne (ed.), Modification and editing of RNA. ASM Press, Washington, D.C.
    • (1998) Modification and Editing of RNA , pp. 555-565
    • Garcia, G.A.1    Goodenough-Lashua, D.M.2
  • 18
    • 0024362769 scopus 로고
    • Ribonucleoside analysis by reversed-phase high-performance liquid chromatography
    • Gehrke, C. W., and K. C. Kuo. 1989. Ribonucleoside analysis by reversed-phase high-performance liquid chromatography. J. Chromatogr. 471:3-36.
    • (1989) J. Chromatogr. , vol.471 , pp. 3-36
    • Gehrke, C.W.1    Kuo, K.C.2
  • 19
    • 0029966338 scopus 로고    scopus 로고
    • Enzymatic formation of modified nucleosides in tRNA: Dependence on tRNA architecture
    • Grosjean, H., J. Edqvist, K. B. Straby, and R. Giege. 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    Giege, R.4
  • 20
    • 0000960472 scopus 로고
    • On the physical basis for ambiguity in genetic coding interactions
    • Grosjean, H. J., S. de Henau, and D. M. Crothers. 1978. On the physical basis for ambiguity in genetic coding interactions. Proc. Natl. Acad. Sci. USA 75:610-614.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 610-614
    • Grosjean, H.J.1    De Henau, S.2    Crothers, D.M.3
  • 22
    • 0032553438 scopus 로고    scopus 로고
    • Reduced misreading of asparagine codons by Escherichia coli tRNALys with hypomodified derivatives of 5-methylaminomethyl-2-thiouridine in the wobble position
    • Hagervall, T. G., S. C. Pomerantz, and J. A. McCloskey. 1998. Reduced misreading of asparagine codons by Escherichia coli tRNALys with hypomodified derivatives of 5-methylaminomethyl-2-thiouridine in the wobble position. J. Mol. Biol. 284:33-42.
    • (1998) J. Mol. Biol. , vol.284 , pp. 33-42
    • Hagervall, T.G.1    Pomerantz, S.C.2    McCloskey, J.A.3
  • 23
    • 0028016099 scopus 로고
    • Protein carboxyl methylation in Saccharomyces cerevisiae: Evidence for STE14-dependent and STE14-independent pathways
    • Hrycyna, C. A., M. C. Yang, and S. Clarke. 1994. Protein carboxyl methylation in Saccharomyces cerevisiae: evidence for STE14-dependent and STE14-independent pathways. Biochemistry 33:9806-9812.
    • (1994) Biochemistry , vol.33 , pp. 9806-9812
    • Hrycyna, C.A.1    Yang, M.C.2    Clarke, S.3
  • 24
    • 0030019943 scopus 로고    scopus 로고
    • Specific initiation and switch to elongation of human immunodeficiency virus type 1 reverse transcription require the post-transcriptional modifications of primer tRNA3Lys
    • Isel, C., J. M. Lanchy, S. F. Le Grice, C. Ehresmann, B. Ehresmann, and R. Marquet. 1996. Specific initiation and switch to elongation of human immunodeficiency virus type 1 reverse transcription require the post-transcriptional modifications of primer tRNA3Lys. EMBO J. 15:917-924.
    • (1996) EMBO J. , vol.15 , pp. 917-924
    • Isel, C.1    Lanchy, J.M.2    Le Grice, S.F.3    Ehresmann, C.4    Ehresmann, B.5    Marquet, R.6
  • 25
    • 0027331556 scopus 로고
    • Modified nucleotides of tRNA(3Lys) modulate primer/template loop-loop interaction in the initiation complex of HIV-1 reverse transcription
    • Isel, C., R. Marquet, G. Keith, C. Ehresmann, and B. Ehresmann. 1993. Modified nucleotides of tRNA(3Lys) modulate primer/template loop-loop interaction in the initiation complex of HIV-1 reverse transcription. J. Biol. Chem. 268:25269-25272.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25269-25272
    • Isel, C.1    Marquet, R.2    Keith, G.3    Ehresmann, C.4    Ehresmann, B.5
  • 26
    • 0035890316 scopus 로고    scopus 로고
    • Protein phosphatase methyltransferase 1 (Ppm1p) is the sole activity responsible for modification of the major forms of protein phosphatase 2A in yeast
    • Kalhor, H. R., K. Luk, A. Ramos, P. Zobel-Thropp, and S. Clarke. 2001. Protein phosphatase methyltransferase 1 (Ppm1p) is the sole activity responsible for modification of the major forms of protein phosphatase 2A in yeast. Arch. Biochem. Biophys. 395:239-245.
    • (2001) Arch. Biochem. Biophys. , vol.395 , pp. 239-245
    • Kalhor, H.R.1    Luk, K.2    Ramos, A.3    Zobel-Thropp, P.4    Clarke, S.5
  • 28
    • 0018835662 scopus 로고
    • Reinvestigation of the primary structure of brewer's yeast tRNA 3 Arg
    • Keith, G., and G. Dirheimer. 1980. Reinvestigation of the primary structure of brewer's yeast tRNA 3 Arg. Biochem. Biophys. Res. Commun. 92:116-119.
    • (1980) Biochem. Biophys. Res. Commun. , vol.92 , pp. 116-119
    • Keith, G.1    Dirheimer, G.2
  • 29
    • 0016593692 scopus 로고
    • Selective labelling of the methyl carboxylate substituents found in the anticodon sequences of some species of yeast transfer RNA
    • Kennedy, T. D., and B. G. Lane. 1975. Selective labelling of the methyl carboxylate substituents found in the anticodon sequences of some species of yeast transfer RNA. Can. J. Biochem. 53:1-10.
    • (1975) Can. J. Biochem. , vol.53 , pp. 1-10
    • Kennedy, T.D.1    Lane, B.G.2
  • 30
    • 0016277653 scopus 로고
    • The primary structure of yeast glutamic acid tRNA specific to the GAA codon
    • Kobayashi, T., T. Irie, M. Yoshida, K. Takeishi, and T. Ukita. 1974. The primary structure of yeast glutamic acid tRNA specific to the GAA codon. Biochim. Biophys. Acta. 366:168-181.
    • (1974) Biochim. Biophys. Acta , vol.366 , pp. 168-181
    • Kobayashi, T.1    Irie, T.2    Yoshida, M.3    Takeishi, K.4    Ukita, T.5
  • 31
    • 0016610083 scopus 로고
    • Presence of the methylester of 5-carboxymethyl uridine in the wobble position of the anticodon of tRNAIII Arg from brewer's yeast
    • Kuntzel, B., J. Weissenbach, R. E. Wolff, T. D. Tumaitis-Kennedy, B. G. Lane, and G. Dirheimer. 1975. Presence of the methylester of 5-carboxymethyl uridine in the wobble position of the anticodon of tRNAIII Arg from brewer's yeast. Biochimie 57:61-70.
    • (1975) Biochimie , vol.57 , pp. 61-70
    • Kuntzel, B.1    Weissenbach, J.2    Wolff, R.E.3    Tumaitis-Kennedy, T.D.4    Lane, B.G.5    Dirheimer, G.6
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 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., and J. F. Curran. 2001. Analysis of codon:anticodon interactions within the ribosome provides new insights into codon reading and the genetic code structure. RNA 7:942-957.
    • (2001) RNA , vol.7 , pp. 942-957
    • Lim, V.I.1    Curran, J.F.2
  • 34
    • 0019460732 scopus 로고
    • Codon reading and translational error. Reading of the glutamine and lysine codons during protein synthesis in vitro
    • Lustig, F., P. Elias, T. Axberg, T. Samuelsson, I. Tittawella, and U. Lagerkvist. 1981. Codon reading and translational error. Reading of the glutamine and lysine codons during protein synthesis in vitro. J. Biol. Chem. 256:2635-2643.
    • (1981) J. Biol. Chem. , vol.256 , pp. 2635-2643
    • Lustig, F.1    Elias, P.2    Axberg, T.3    Samuelsson, T.4    Tittawella, I.5    Lagerkvist, U.6
  • 35
    • 0035854372 scopus 로고    scopus 로고
    • State of the arg: Protein methylation at arginine comes of age
    • McBride, A. E., and P. A. Silver. 2001. State of the arg: protein methylation at arginine comes of age. Cell 106:5-8.
    • (2001) Cell , vol.106 , pp. 5-8
    • McBride, A.E.1    Silver, P.A.2
  • 36
    • 0035542551 scopus 로고    scopus 로고
    • DNA methylation and control of gene expression in vertebrate development
    • Meehan, R. R., and I. Stancheva. 2001. DNA methylation and control of gene expression in vertebrate development. Essays Biochem. 37:59-70.
    • (2001) Essays Biochem. , vol.37 , pp. 59-70
    • Meehan, R.R.1    Stancheva, I.2
  • 37
    • 0032821744 scopus 로고    scopus 로고
    • Multisite-specific tRNA:m5C-methyltransferase (Trm4) in yeast Saccharomyces cerevisiae: Identification of the gene and substrate specificity of the enzyme
    • Motorin, Y., and H. Grosjean. 1999. Multisite-specific tRNA:m5C-methyltransferase (Trm4) in yeast Saccharomyces cerevisiae: identification of the gene and substrate specificity of the enzyme. RNA 5:1105-1118.
    • (1999) RNA , vol.5 , pp. 1105-1118
    • Motorin, Y.1    Grosjean, H.2
  • 38
    • 0017171104 scopus 로고
    • The methylation of tRNA
    • Nau, F. 1976. The methylation of tRNA. Biochimie 58:629-645.
    • (1976) Biochimie , vol.58 , pp. 629-645
    • Nau, F.1
  • 39
    • 84889123167 scopus 로고    scopus 로고
    • Ph.D. thesis, University of California-Los Angeles, Los Angeles
    • Niewmierzycka, A. 1998. Ph.D. thesis. University of California-Los Angeles, Los Angeles.
    • (1998)
    • Niewmierzycka, A.1
  • 40
    • 0033534476 scopus 로고    scopus 로고
    • S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase
    • Niewmierzycka, A., and S. Clarke. 1999. S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase. J. Biol. Chem. 274:814-824.
    • (1999) J. Biol. Chem. , vol.274 , pp. 814-824
    • Niewmierzycka, A.1    Clarke, S.2
  • 41
    • 0034130606 scopus 로고    scopus 로고
    • Identification of the TRM2 gene encoding the tRNA(m5U54) methyltransferase of Saccharomyces cerevisiae
    • Nordlund, M. E., J. O. Johansson, U. von Pawel-Rammingen, and A. S. Bystrom. 2000. Identification of the TRM2 gene encoding the tRNA(m5U54)methyltransferase of Saccharomyces cerevisiae. RNA 6:844-860.
    • (2000) RNA , vol.6 , pp. 844-860
    • Nordlund, M.E.1    Johansson, J.O.2    Von Pawel-Rammingen, U.3    Bystrom, A.S.4
  • 42
    • 0017619363 scopus 로고
    • Lysine transfer RNA from liver: A sulfur-containing species that codes for AAG
    • Ortwerth, B. J., and J. V. Carlson. 1977. Lysine transfer RNA from liver: a sulfur-containing species that codes for AAG. Arch. Biochem. Biophys. 178:278-284.
    • (1977) Arch. Biochem. Biophys. , vol.178 , pp. 278-284
    • Ortwerth, B.J.1    Carlson, J.V.2
  • 43
    • 0037007220 scopus 로고    scopus 로고
    • Trm7p catalyses the formation of two 2′-O-methylriboses in yeast tRNA anticodon loop
    • Pintard, L., F. Lecointe, J. M. Bujnicki, C. Bonnerot, H. Grosjean, and B. Lapeyre. 2002. Trm7p catalyses the formation of two 2′-O-methylriboses in yeast tRNA anticodon loop. EMBO J. 21:1811-1820.
    • (2002) EMBO J. , vol.21 , pp. 1811-1820
    • Pintard, L.1    Lecointe, F.2    Bujnicki, J.M.3    Bonnerot, C.4    Grosjean, H.5    Lapeyre, B.6
  • 44
    • 0025612935 scopus 로고
    • Analysis of RNA hydrolyzates by liquid chromatography-mass spectrometry
    • Pomerantz, S. C., and J. A. McCloskey. 1990. Analysis of RNA hydrolyzates by liquid chromatography-mass spectrometry. Methods Enzymol. 193:796-824.
    • (1990) Methods Enzymol. , vol.193 , pp. 796-824
    • Pomerantz, S.C.1    McCloskey, J.A.2
  • 48
    • 0034680364 scopus 로고    scopus 로고
    • Hypermodified nucleosides in the anticodon of tRNALys stabilize a canonical U-turn structure
    • Sundaram, M., P. C. Durant, and D. R. Davis. 2000. Hypermodified nucleosides in the anticodon of tRNALys stabilize a canonical U-turn structure. Biochemistry. 39:12575-12584.
    • (2000) Biochemistry , vol.39 , pp. 12575-12584
    • Sundaram, M.1    Durant, P.C.2    Davis, D.R.3
  • 50
    • 0016493932 scopus 로고
    • Sequence of E. coli tRNA-Glu1 by automated sequential degradation
    • Uziel, M., and A. J. Weinberger. 1975. Sequence of E. coli tRNA-Glu1 by automated sequential degradation. Nucleic Acids Res. 2:469-475.
    • (1975) Nucleic Acids Res. , vol.2 , pp. 469-475
    • Uziel, M.1    Weinberger, A.J.2
  • 51
    • 0034886697 scopus 로고    scopus 로고
    • Crystal structure of paromomycin docked into the eubacterial ribosomal decoding A site
    • Vicens, Q., and E. Westhof. 2001. Crystal structure of paromomycin docked into the eubacterial ribosomal decoding A site. Structure (Cambridge) 9:647-658.
    • (2001) Structure (Cambridge) , vol.9 , pp. 647-658
    • Vicens, Q.1    Westhof, E.2
  • 52
    • 0017825833 scopus 로고
    • Pairing properties of the methylester of 5-carboxymethyl uridine in the wobble position of yeast tRNA3Arg
    • Weissenbach, J., and G. Dirheimer. 1978. Pairing properties of the methylester of 5-carboxymethyl uridine in the wobble position of yeast tRNA3Arg. Biochim. Biophys. Acta. 518:530-534.
    • (1978) Biochim. Biophys. Acta , vol.518 , pp. 530-534
    • Weissenbach, J.1    Dirheimer, G.2
  • 53
    • 0016262896 scopus 로고
    • Primary structure of E. coli alanine transfer RNA: Relation to the yeast phenylalanyl tRNA synthetase recognition site
    • Williams, R. J., W. Nagel, B. Roe, and B. Dudock. 1974. Primary structure of E. coli alanine transfer RNA: relation to the yeast phenylalanyl tRNA synthetase recognition site. Biochem. Biophys. Res. Commun. 60:1215-1221.
    • (1974) Biochem. Biophys. Res. Commun. , vol.60 , pp. 1215-1221
    • Williams, R.J.1    Nagel, W.2    Roe, B.3    Dudock, B.4
  • 55
    • 0035801225 scopus 로고    scopus 로고
    • Wobble modification defect in tRNA disturbs codon-anticodon interaction in a mitochondrial disease
    • Yasukawa, T., T. Suzuki, N. Ishii, S. Ohta, and K. Watanabe. 2001. Wobble modification defect in tRNA disturbs codon-anticodon interaction in a mitochondrial disease. EMBO J. 20:4794-4802.
    • (2001) EMBO J. , vol.20 , pp. 4794-4802
    • Yasukawa, T.1    Suzuki, T.2    Ishii, N.3    Ohta, S.4    Watanabe, K.5
  • 57
    • 0002365884 scopus 로고
    • Modified nucleosides and codon recognition
    • D. Soll and U. L. RajBhandary (ed.). ASM Press, Washington, D.C.
    • Yokoyama, S., and S. Nishimura. 1995. Modified nucleosides and codon recognition, p. 207-223. In D. Soll and U. L. RajBhandary (ed.), tRNA: structure, biosynthesis, and function. ASM Press, Washington, D.C.
    • (1995) tRNA: Structure, Biosynthesis, and Function , pp. 207-223
    • Yokoyama, S.1    Nishimura, S.2
  • 58
    • 0032491583 scopus 로고    scopus 로고
    • Delta-N-methylarginine is a novel posttranslational modification of arginine residues in yeast proteins
    • Zobel-Thropp, P., J. D. Gary, and S. Clarke. 1998. Delta-N-methylarginine is a novel posttranslational modification of arginine residues in yeast proteins. J. Biol. Chem. 273:29283-29286.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29283-29286
    • Zobel-Thropp, P.1    Gary, J.D.2    Clarke, S.3
  • 59
    • 0034711220 scopus 로고    scopus 로고
    • A novel post-translational modification of yeast elongation factor 1A. Methylesterification at the C terminus
    • Zobel-Thropp, P., M. C. Yang, L. Machado, and S. Clarke. 2000. A novel post-translational modification of yeast elongation factor 1A. Methylesterification at the C terminus. J. Biol. Chem. 275:37150-37158.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37150-37158
    • Zobel-Thropp, P.1    Yang, M.C.2    Machado, L.3    Clarke, S.4


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