메뉴 건너뛰기




Volumn 28, Issue 24, 2008, Pages 7514-7531

Characterization of human GTPBP3, a GTP-binding protein involved in mitochondrial tRNA modification

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN 3; GUANOSINE TRIPHOSPHATASE; POTASSIUM; PROTEIN MNME; SMALL INTERFERING RNA; TRANSFER RNA; UNCLASSIFIED DRUG;

EID: 57349096320     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.00946-08     Document Type: Article
Times cited : (54)

References (57)
  • 1
    • 0033568447 scopus 로고    scopus 로고
    • Defective kinetics of cytochrome c oxidase and alteration of mitochondrial potential in fibroblasts and cytoplasmic hybrid cells with the mutation for myoclonus epilepsy with ragged-red fibres ("MERRF") at position 8344 nt
    • Antonická, H., D. Floryk, P. Klement, L. Stratilova, J. Heřmanská, H. Houštková, M. Kalous, Z. Drahota, J. Zeman, and J. Houštěk. 1999. Defective kinetics of cytochrome c oxidase and alteration of mitochondrial potential in fibroblasts and cytoplasmic hybrid cells with the mutation for myoclonus epilepsy with ragged-red fibres ("MERRF") at position 8344 nt. Biochem. J. 342:537-544.
    • (1999) Biochem. J , vol.342 , pp. 537-544
    • Antonická, H.1    Floryk, D.2    Klement, P.3    Stratilova, L.4    Heřmanská, J.5    Houštková, H.6    Kalous, M.7    Drahota, Z.8    Zeman, J.9    Houštěk, J.10
  • 3
    • 57349171087 scopus 로고    scopus 로고
    • Björk, G. R. 1998. Modified nucleosides at positions 34 and 37 of tRNAs and their predicted coding capacities, p. 577-581. In H. Grosjean, and R. Benne, R. (ed.), Modification and editing of RNA. ASM Press, Washington, DC.
    • Björk, G. R. 1998. Modified nucleosides at positions 34 and 37 of tRNAs and their predicted coding capacities, p. 577-581. In H. Grosjean, and R. Benne, R. (ed.), Modification and editing of RNA. ASM Press, Washington, DC.
  • 4
    • 57349156291 scopus 로고    scopus 로고
    • Björk, G. R., and T. G. Hagervall. July 2005, posting date. Chapter 4.6.2, Transfer RNA modification. In R. Curtiss III et al. (ed.), EcoSal - Escherichia coli and Salmonella: cellular and molecular biology. ASM Press, Washington, DC. http://www.ecosal.org.
    • Björk, G. R., and T. G. Hagervall. July 2005, posting date. Chapter 4.6.2, Transfer RNA modification. In R. Curtiss III et al. (ed.), EcoSal - Escherichia coli and Salmonella: cellular and molecular biology. ASM Press, Washington, DC. http://www.ecosal.org.
  • 5
    • 0035449350 scopus 로고    scopus 로고
    • Translational misreading: A tRNA modification counteracts a +2 ribosomal frameshift
    • Brégeon, D., V. Colot, M. Radman, and F. Taddei. 2001. Translational misreading: a tRNA modification counteracts a +2 ribosomal frameshift. Genes Dev. 15:2295-2306.
    • (2001) Genes Dev , vol.15 , pp. 2295-2306
    • Brégeon, D.1    Colot, V.2    Radman, M.3    Taddei, F.4
  • 6
    • 0033573089 scopus 로고    scopus 로고
    • The Escherichia coli trmE (mnmE) gene, involved in tRNA modification, codes for an evolutionarily conserved GTPase with unusual biochemical properties
    • Cabedo, H., F. Macián, M. Villarroya, J. C. Escudero, M. Martínez-Vicente, E. Knecht, and M.-E. Armengod. 1999. The Escherichia coli trmE (mnmE) gene, involved in tRNA modification, codes for an evolutionarily conserved GTPase with unusual biochemical properties. EMBO J. 18:7063-7076.
    • (1999) EMBO J , vol.18 , pp. 7063-7076
    • Cabedo, H.1    Macián, F.2    Villarroya, M.3    Escudero, J.C.4    Martínez-Vicente, M.5    Knecht, E.6    Armengod, M.-E.7
  • 7
    • 0035133535 scopus 로고    scopus 로고
    • An upstream AG determines whether a downstream AG is selected during catalytic step II of splicing
    • Chua, K., and R. Reed. 2001. An upstream AG determines whether a downstream AG is selected during catalytic step II of splicing. Mol. Cell. Biol. 21:1509-1514.
    • (2001) Mol. Cell. Biol , vol.21 , pp. 1509-1514
    • Chua, K.1    Reed, R.2
  • 8
    • 0032561194 scopus 로고    scopus 로고
    • MTO1 codes for a mitochondrial protein required for respiration in paromomycin-resistant mutants of Saccharomyces cerevisiae
    • Colby, G., M. Wu, and A. Tzagoloff. 1998. MTO1 codes for a mitochondrial protein required for respiration in paromomycin-resistant mutants of Saccharomyces cerevisiae. J. Biol. Chem. 273:27945-27952.
    • (1998) J. Biol. Chem , vol.273 , pp. 27945-27952
    • Colby, G.1    Wu, M.2    Tzagoloff, A.3
  • 9
    • 0027218236 scopus 로고
    • MSS1, a nuclear-encoded mitochondrial GTPase involved in the expression of COX1 subunit of cytochrome c oxidase
    • Decoster, E., A. Vassal, and G. Faye. 1993. MSS1, a nuclear-encoded mitochondrial GTPase involved in the expression of COX1 subunit of cytochrome c oxidase. J. Mol. Biol. 232:79-88.
    • (1993) J. Mol. Biol , vol.232 , pp. 79-88
    • Decoster, E.1    Vassal, A.2    Faye, G.3
  • 10
    • 0021770444 scopus 로고
    • Novel E. coli mutants deficient in biosynthesis of 5-methylaminomethyl-2- thiouridine
    • Elseviers, D., L. A. Petrullo, and P. Gallagher. 1984. Novel E. coli mutants deficient in biosynthesis of 5-methylaminomethyl-2- thiouridine. Nucleic Acids Res. 12:3521-3534.
    • (1984) Nucleic Acids Res , vol.12 , pp. 3521-3534
    • Elseviers, D.1    Petrullo, L.A.2    Gallagher, P.3
  • 11
    • 0142009674 scopus 로고    scopus 로고
    • Changes in the proteolytic activities of proteasomes and lysosomes in human fibroblasts produced by serum withdrawal, amino-acid deprivation and confluent conditions
    • Fuertes, G., J. J. Martín de Llano, A. Villarroya, A. J. Rivett, and E. Knecht. 2003. Changes in the proteolytic activities of proteasomes and lysosomes in human fibroblasts produced by serum withdrawal, amino-acid deprivation and confluent conditions. Biochem. J. 375:75-86.
    • (2003) Biochem. J , vol.375 , pp. 75-86
    • Fuertes, G.1    Martín de Llano, J.J.2    Villarroya, A.3    Rivett, A.J.4    Knecht, E.5
  • 12
    • 0022296047 scopus 로고
    • Regulation of mitochondrial protein concentration: A plausible model which may permit assessing protein turnover
    • Grisolía, S., J. Hernández-Yago, and E. Knecht. 1985. Regulation of mitochondrial protein concentration: a plausible model which may permit assessing protein turnover. Curr. Topics Cell Regul. 27:387-396.
    • (1985) Curr. Topics Cell Regul , vol.27 , pp. 387-396
    • Grisolía, S.1    Hernández-Yago, J.2    Knecht, E.3
  • 13
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzmán, L. M., D. Belin, M. J. Carson, and J. Beckwith. 1995. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177:4121-4130.
    • (1995) J. Bacteriol , vol.177 , pp. 4121-4130
    • Guzmán, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 14
    • 0023664535 scopus 로고
    • Transfer RNA (5-methylaminomethyl-2-thiouridine)- methyltransferase from Escherichia coli K-12 has two enzymatic activities
    • Hagervall, T. G., C. G. Edmonds, J. A. McCloskey, and G. R. Björk. 1987. Transfer RNA (5-methylaminomethyl-2-thiouridine)- methyltransferase from Escherichia coli K-12 has two enzymatic activities. J. Biol. Chem. 262:8488-8495.
    • (1987) J. Biol. Chem , vol.262 , pp. 8488-8495
    • Hagervall, T.G.1    Edmonds, C.G.2    McCloskey, J.A.3    Björk, G.R.4
  • 15
    • 29544452864 scopus 로고    scopus 로고
    • Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions
    • Ikeuchi, Y., N. Shigi, J. Kato, A. Nishimura, and T. Suzuki. 2006. Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions. Mol. Cell 21:97-108.
    • (2006) Mol. Cell , vol.21 , pp. 97-108
    • Ikeuchi, Y.1    Shigi, N.2    Kato, J.3    Nishimura, A.4    Suzuki, T.5
  • 17
    • 0034505937 scopus 로고    scopus 로고
    • Protein degradation in mitochondria
    • Käser, M., and T. Langer. 2000. Protein degradation in mitochondria. Semin. Cell Dev. Biol. 11:181-190.
    • (2000) Semin. Cell Dev. Biol , vol.11 , pp. 181-190
    • Käser, M.1    Langer, T.2
  • 19
    • 6344221310 scopus 로고    scopus 로고
    • Codon-specific translational defect caused by a wobble modification deficiency in mutant tRNA from a human mitochondrial disease
    • Kirino, Y., T. Yasukawa, S. Ohta, S. Akira, K. Ishihara, K. Watanabe, and T. Suzuki. 2004. Codon-specific translational defect caused by a wobble modification deficiency in mutant tRNA from a human mitochondrial disease. Proc. Natl. Acad. Sci. USA 101:15070-15075.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 15070-15075
    • Kirino, Y.1    Yasukawa, T.2    Ohta, S.3    Akira, S.4    Ishihara, K.5    Watanabe, K.6    Suzuki, T.7
  • 20
    • 18844430007 scopus 로고    scopus 로고
    • Specific correlation between the wobble modification deficiency in mutant tRNAs and the clinical features of a human mitochondrial disease
    • Kirino, Y., Y. Goto, Y. Campos, J. Arenas, and T. Suzuki. 2005. Specific correlation between the wobble modification deficiency in mutant tRNAs and the clinical features of a human mitochondrial disease. Proc. Natl. Acad. Sci. USA 102:7127-7132.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 7127-7132
    • Kirino, Y.1    Goto, Y.2    Campos, Y.3    Arenas, J.4    Suzuki, T.5
  • 21
    • 0018901069 scopus 로고
    • Fate of proteins synthesized in mitochondria of cultured mammalian cells revealed by electron microscope radioautography
    • Knecht, E., J. Hernández-Yago, A. Martínez-Ramón, and S. Grisolía. 1980. Fate of proteins synthesized in mitochondria of cultured mammalian cells revealed by electron microscope radioautography. Exp. Cell Res. 125:191-199.
    • (1980) Exp. Cell Res , vol.125 , pp. 191-199
    • Knecht, E.1    Hernández-Yago, J.2    Martínez-Ramón, A.3    Grisolía, S.4
  • 22
    • 34250369119 scopus 로고    scopus 로고
    • Protein degradation within mitochondria: Versatile activities of AAA proteases and other peptidases
    • Koopen, M., and T. Langer. 2007. Protein degradation within mitochondria: versatile activities of AAA proteases and other peptidases. Mol. Biol. 42:221-242.
    • (2007) Mol. Biol , vol.42 , pp. 221-242
    • Koopen, M.1    Langer, T.2
  • 23
    • 0036837683 scopus 로고    scopus 로고
    • A human mitochondrial GTP binding protein related to tRNA modification may modulate phenotypic expression of the deafness-associated mitochondrial 12S rRNA mutation
    • Li, X., and M.-X. Guan. 2002. A human mitochondrial GTP binding protein related to tRNA modification may modulate phenotypic expression of the deafness-associated mitochondrial 12S rRNA mutation. Mol. Cell. Biol. 22:7701-7711.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 7701-7711
    • Li, X.1    Guan, M.-X.2
  • 24
    • 0345415102 scopus 로고    scopus 로고
    • Identification and characterization of mouse GTPBP3 gene encoding a mitochondrial GTP-binding protein involved in tRNA modification
    • Li, X., and M.-X. Guan. 2003. Identification and characterization of mouse GTPBP3 gene encoding a mitochondrial GTP-binding protein involved in tRNA modification. Biochem. Biophys. Res. Commun. 312:747-754.
    • (2003) Biochem. Biophys. Res. Commun , vol.312 , pp. 747-754
    • Li, X.1    Guan, M.-X.2
  • 25
    • 0037178851 scopus 로고    scopus 로고
    • Isolation and characterization of the putative nuclear modifier gene MTO1 involved in the pathogenesis of deafness-associated mitochondrial 12 S rRNA A1555G mutation
    • Li, X., R. Li, X. Lin, and M.-X. Guan. 2002. Isolation and characterization of the putative nuclear modifier gene MTO1 involved in the pathogenesis of deafness-associated mitochondrial 12 S rRNA A1555G mutation. J. Biol. Chem. 277:27256-27264.
    • (2002) J. Biol. Chem , vol.277 , pp. 27256-27264
    • Li, X.1    Li, R.2    Lin, X.3    Guan, M.-X.4
  • 26
    • 0028593398 scopus 로고
    • Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV
    • Lim, K., J. H. Ho, K. Keeling, G. L. Gilliland, X. Ji, F. Rüker, and D. C. Carter. 1994. Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV. Protein Sci. 3:2233-2244.
    • (1994) Protein Sci , vol.3 , pp. 2233-2244
    • Lim, K.1    Ho, J.H.2    Keeling, K.3    Gilliland, G.L.4    Ji, X.5    Rüker, F.6    Carter, D.C.7
  • 27
    • 24744470965 scopus 로고    scopus 로고
    • Effects of mutagenesis in the switch I region and conserved arginines of Escherichia coli MnmE protein, a GTPase involved in tRNA modification
    • Martínez-Vicente, M., L. Yim, M. Villarroya, M. Mellado, E. Pérez-Payá, G. R. Björk, and M.-E. Armengod. 2005. Effects of mutagenesis in the switch I region and conserved arginines of Escherichia coli MnmE protein, a GTPase involved in tRNA modification. J. Biol. Chem. 280:30660-30670.
    • (2005) J. Biol. Chem , vol.280 , pp. 30660-30670
    • Martínez-Vicente, M.1    Yim, L.2    Villarroya, M.3    Mellado, M.4    Pérez-Payá, E.5    Björk, G.R.6    Armengod, M.-E.7
  • 28
    • 44949138270 scopus 로고    scopus 로고
    • Crystal structures of the conserved tRNA modifying enzyme GidA: Implications for its interaction with MnmE and substrate
    • Meyer, S., A. Scrima, W. Versées, and A. Wittinghofer. 2008. Crystal structures of the conserved tRNA modifying enzyme GidA: implications for its interaction with MnmE and substrate. J. Mol. Biol. 380:532-547.
    • (2008) J. Mol. Biol , vol.380 , pp. 532-547
    • Meyer, S.1    Scrima, A.2    Versées, W.3    Wittinghofer, A.4
  • 29
  • 30
    • 0027984792 scopus 로고
    • Polypyrimidine tract sequences direct selection of alternative branch sites and influence protein binding
    • Norton, P. A. 1994. Polypyrimidine tract sequences direct selection of alternative branch sites and influence protein binding. Nucleic Acids Res. 22:3854-3860.
    • (1994) Nucleic Acids Res , vol.22 , pp. 3854-3860
    • Norton, P.A.1
  • 31
    • 27944477787 scopus 로고    scopus 로고
    • Discrepancies between nitroglycerin and NO-releasing drugs on mitochondrial oxygen consumption, vasoactivity, and the release of
    • Nuñez, C., V. M. Víctor, R. Tur, A. Alvarez-Barrientos, S. Moncada, J. Esplugues, and P. D'Ocon. 2005. Discrepancies between nitroglycerin and NO-releasing drugs on mitochondrial oxygen consumption, vasoactivity, and the release of NO. Circ. Res. 97:1063-1069.
    • (2005) Circ. Res , vol.97 , pp. 1063-1069
    • Nuñez, C.1    Víctor, V.M.2    Tur, R.3    Alvarez-Barrientos, A.4    Moncada, S.5    Esplugues, J.6    D'Ocon, P.7
  • 32
    • 0037669010 scopus 로고    scopus 로고
    • Low conservation of the alternative splicing patterns in the human and mouse genomes
    • Nurtdinov, R. M., I. I. Artamonova, A. A. Mironov, and M. S. Gelfand. 2003. Low conservation of the alternative splicing patterns in the human and mouse genomes. Hum. Mol. Genet. 12:1313-1320.
    • (2003) Hum. Mol. Genet , vol.12 , pp. 1313-1320
    • Nurtdinov, R.M.1    Artamonova, I.I.2    Mironov, A.A.3    Gelfand, M.S.4
  • 33
    • 0035176759 scopus 로고    scopus 로고
    • Enhanced oxidative damage in human cells harbouring A3243G mutation of mitochondrial DNA: Implication of oxidative stress in the pathogenesis of mitochondrial diabetes
    • Pang, C.-Y., H.-C. Lee, and Y.-H. Wei. 2001. Enhanced oxidative damage in human cells harbouring A3243G mutation of mitochondrial DNA: implication of oxidative stress in the pathogenesis of mitochondrial diabetes. Diabetes Res. Clin. Pract. 54(Suppl. 2):S45-S56.
    • (2001) Diabetes Res. Clin. Pract , vol.54 , Issue.SUPPL. 2
    • Pang, C.-Y.1    Lee, H.-C.2    Wei, Y.-H.3
  • 34
    • 0024808994 scopus 로고
    • The organization of 3′ splice-site sequences in mammalian introns
    • Reed, R. 1989. The organization of 3′ splice-site sequences in mammalian introns. Genes Dev. 3:2113-2123.
    • (1989) Genes Dev , vol.3 , pp. 2113-2123
    • Reed, R.1
  • 35
    • 0027233694 scopus 로고
    • A mutational analysis of the polypyrimidine tract of introns. Effects of sequence differences in pyrimidine tracts on splicing
    • Roscigno, R. F., M. Weiner, and M. A. García-Blanco. 1993. A mutational analysis of the polypyrimidine tract of introns. Effects of sequence differences in pyrimidine tracts on splicing. J. Biol. Chem. 268:11222-11229.
    • (1993) J. Biol. Chem , vol.268 , pp. 11222-11229
    • Roscigno, R.F.1    Weiner, M.2    García-Blanco, M.A.3
  • 36
    • 33750927660 scopus 로고    scopus 로고
    • Evidence for adaptive selection acting on the tRNA and rRNA genes of human mitochondrial DNA
    • Ruiz-Pesini, E., and D. C. Wallace. 2006. Evidence for adaptive selection acting on the tRNA and rRNA genes of human mitochondrial DNA. Hum. Mutat. 27:1072-1081.
    • (2006) Hum. Mutat , vol.27 , pp. 1072-1081
    • Ruiz-Pesini, E.1    Wallace, D.C.2
  • 37
  • 39
    • 33745520400 scopus 로고    scopus 로고
    • Dimerisation-dependent GTPase reaction of MnmE: How potassium acts as GTPase-activating element
    • Scrima, A., and A. Wittinghofer. 2006. Dimerisation-dependent GTPase reaction of MnmE: how potassium acts as GTPase-activating element. EMBO J. 25:2940-2951.
    • (2006) EMBO J , vol.25 , pp. 2940-2951
    • Scrima, A.1    Wittinghofer, A.2
  • 40
    • 13244284641 scopus 로고    scopus 로고
    • The structure of the TrmE GTP-binding protein and its implications for tRNA modification
    • Scrima, A., I. R. Vetter, M.-E. Armengod, and A. Wittinghofer. 2005. The structure of the TrmE GTP-binding protein and its implications for tRNA modification. EMBO J. 24:23-33.
    • (2005) EMBO J , vol.24 , pp. 23-33
    • Scrima, A.1    Vetter, I.R.2    Armengod, M.-E.3    Wittinghofer, A.4
  • 42
    • 0027214101 scopus 로고
    • Scanning and competition between AGs are involved in 3′ splice site selection in mammalian introns
    • Smith, C. W. J., T. T. Chu, and B. Nadal-Ginard. 1993. Scanning and competition between AGs are involved in 3′ splice site selection in mammalian introns. Mol. Cell. Biol. 13:4939-4952.
    • (1993) Mol. Cell. Biol , vol.13 , pp. 4939-4952
    • Smith, C.W.J.1    Chu, T.T.2    Nadal-Ginard, B.3
  • 44
    • 0037011177 scopus 로고    scopus 로고
    • Taurine as a constituent of mitochondrial tRNA: New insights into the functions of taurine and human mitochondrial diseases
    • Suzuki, T., T. Suzuki, T. Wada, K. Saigo, and K. Watanabe. 2002. Taurine as a constituent of mitochondrial tRNA: new insights into the functions of taurine and human mitochondrial diseases. EMBO J. 21:6581-6589.
    • (2002) EMBO J , vol.21 , pp. 6581-6589
    • Suzuki, T.1    Suzuki, T.2    Wada, T.3    Saigo, K.4    Watanabe, K.5
  • 45
    • 13744254695 scopus 로고    scopus 로고
    • A large-scale analysis of mRNA polyadenylation of human and mouse genes
    • Tian, B., J. Hu, H. Zhang, and C. Lutz. 2005. A large-scale analysis of mRNA polyadenylation of human and mouse genes. Nucleic Acids Res. 33:201-212.
    • (2005) Nucleic Acids Res , vol.33 , pp. 201-212
    • Tian, B.1    Hu, J.2    Zhang, H.3    Lutz, C.4
  • 46
    • 12544259245 scopus 로고    scopus 로고
    • Mitochondria-specific RNA-modifying enzymes responsible for the biosynthesis of the wobble base in mitochondrial tRNAs. Implications for the molecular pathogenesis of human mitochondrial diseases
    • Umeda, N., T. Suzuki, M. Yukawa, Y. Ohya, H. Shindo, K. Watanabe, and T. Suzuki. 2005. Mitochondria-specific RNA-modifying enzymes responsible for the biosynthesis of the wobble base in mitochondrial tRNAs. Implications for the molecular pathogenesis of human mitochondrial diseases. J. Biol. Chem. 280:1613-1624.
    • (2005) J. Biol. Chem , vol.280 , pp. 1613-1624
    • Umeda, N.1    Suzuki, T.2    Yukawa, M.3    Ohya, Y.4    Shindo, H.5    Watanabe, K.6    Suzuki, T.7
  • 47
    • 0024506187 scopus 로고
    • Vanadate inhibits degradation of short-lived, but not of long-lived, proteins in L-132 human cells
    • Vargas, J. L., F. Aniento, J. Cervera, and E. Knecht. 1989. Vanadate inhibits degradation of short-lived, but not of long-lived, proteins in L-132 human cells. Biochem. J. 258:33-40.
    • (1989) Biochem. J , vol.258 , pp. 33-40
    • Vargas, J.L.1    Aniento, F.2    Cervera, J.3    Knecht, E.4
  • 48
    • 0034461401 scopus 로고    scopus 로고
    • Characterization of GTPase activity of TrmE, a member of a novel GTPase superfamily, from Thermotoga maritime
    • Yamanaka, K., J. Hwang, and M. Inouye. 2000. Characterization of GTPase activity of TrmE, a member of a novel GTPase superfamily, from Thermotoga maritime. J. Bacteriol. 182:7078-7082.
    • (2000) J. Bacteriol , vol.182 , pp. 7078-7082
    • Yamanaka, K.1    Hwang, J.2    Inouye, M.3
  • 49
    • 23844437940 scopus 로고    scopus 로고
    • Mutations in MTO2 related to tRNA modification impair mitochondrial gene expression and protein synthesis in the presence of a paromomycin resistance mutation in mitochondrial 15 S rRNA
    • Yan, Q., X. Li, G. Faye, and M.-X. Guan. 2005. Mutations in MTO2 related to tRNA modification impair mitochondrial gene expression and protein synthesis in the presence of a paromomycin resistance mutation in mitochondrial 15 S rRNA. J. Biol. Chem. 280:29151-29157.
    • (2005) J. Biol. Chem , vol.280 , pp. 29151-29157
    • Yan, Q.1    Li, X.2    Faye, G.3    Guan, M.-X.4
  • 50
    • 33644879973 scopus 로고    scopus 로고
    • Human TRMU encoding the mitochondrial 5-methylaminomethyl-2-thiouridine-methyltransferase is a putative nuclear modifier gene for the phenotypic expression of the deafness-associated 12S rRNA mutations
    • Yan, Q., Y. Bykhovskaya, R. Li, E. Mengesha, M. Shohat, X. Estivill, N. Fischel-Ghodsian, and M.-X. Guan. 2006. Human TRMU encoding the mitochondrial 5-methylaminomethyl-2-thiouridine-methyltransferase is a putative nuclear modifier gene for the phenotypic expression of the deafness-associated 12S rRNA mutations. Biochem. Biophys. Res. Commun. 342:1130-1136.
    • (2006) Biochem. Biophys. Res. Commun , vol.342 , pp. 1130-1136
    • Yan, Q.1    Bykhovskaya, Y.2    Li, R.3    Mengesha, E.4    Shohat, M.5    Estivill, X.6    Fischel-Ghodsian, N.7    Guan, M.-X.8
  • 52
    • 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
  • 53
    • 0033968067 scopus 로고    scopus 로고
    • Defect in modification at the anticodon wobble nucleotide of mitochondrial tRNALys with the MERRF encephalomyopathy pathogenic mutation
    • Yasukawa, T., T. Suzuki, N. Ishii, Y. Ueda, S. Ohta, and K. Watanabe. 2000. Defect in modification at the anticodon wobble nucleotide of mitochondrial tRNALys with the MERRF encephalomyopathy pathogenic mutation. FEBS Lett. 467:175-178.
    • (2000) FEBS Lett , vol.467 , pp. 175-178
    • Yasukawa, T.1    Suzuki, T.2    Ishii, N.3    Ueda, Y.4    Ohta, S.5    Watanabe, K.6
  • 54
    • 0036838879 scopus 로고    scopus 로고
    • Wobble modification defect suppresses translational activity of tRNAs with MERRF and MELAS mutations
    • Yasukawa, T., T. Suzuki, S. Ohta, and K. Watanabe. 2002. Wobble modification defect suppresses translational activity of tRNAs with MERRF and MELAS mutations. Mitochondrion 2:129-141.
    • (2002) Mitochondrion , vol.2 , pp. 129-141
    • Yasukawa, T.1    Suzuki, T.2    Ohta, S.3    Watanabe, K.4
  • 55
    • 0034635519 scopus 로고    scopus 로고
    • Leu(UUR) with pathogenic mutations of mitochondrial myopathy, encephalopathy, lactic acidosis, and stroke-like episodes
    • Leu(UUR) with pathogenic mutations of mitochondrial myopathy, encephalopathy, lactic acidosis, and stroke-like episodes. J. Biol. Chem. 275:4251-4257.
    • (2000) J. Biol. Chem , vol.275 , pp. 4251-4257
    • Yasukawa, T.1    Suzuki, T.2    Suzuki, T.3    Ueda, T.4    Ohta, S.5    Watanabe, K.6
  • 56
    • 33845672606 scopus 로고    scopus 로고
    • Further insights into the tRNA modification process controlled by proteins MnmE and GidA of Escherichia coli
    • Yim, L., I. Moukadiri, G. R. Björk, and M.-E. Armengod. 2006. Further insights into the tRNA modification process controlled by proteins MnmE and GidA of Escherichia coli. Nucleic Acids Res. 34:5892-5905.
    • (2006) Nucleic Acids Res , vol.34 , pp. 5892-5905
    • Yim, L.1    Moukadiri, I.2    Björk, G.R.3    Armengod, M.-E.4
  • 57
    • 0043210520 scopus 로고    scopus 로고
    • The GTPase activity and C-terminal cysteine of the Escherichia coli MnmE protein are essential for its tRNA modifying function
    • Yim, L., M. Martínez-Vicente, M. Villarroya, C. Aguado, E. Knecht, and M.-E. Armengod. 2003. The GTPase activity and C-terminal cysteine of the Escherichia coli MnmE protein are essential for its tRNA modifying function. J. Biol. Chem. 278:28378-28387.
    • (2003) J. Biol. Chem , vol.278 , pp. 28378-28387
    • Yim, L.1    Martínez-Vicente, M.2    Villarroya, M.3    Aguado, C.4    Knecht, E.5    Armengod, M.-E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.