메뉴 건너뛰기




Volumn 287, Issue 52, 2012, Pages 43950-43960

Characterization and structure of the Aquifex aeolicus protein DUF752: A bacterial tRNA-methyltransferase (MnmC2) functioning without the usually fused oxidase domain (MnmC1)

Author keywords

[No Author keywords available]

Indexed keywords

AQUIFEX AEOLICUS; BIFUNCTIONAL; ENZYMATIC REACTION; FREE AMINO GROUPS; GENZYME; IN-VITRO; METHYLTRANSFERASES; NATURALLY OCCURRING; POST-TRANSCRIPTIONAL MODIFICATION; PROTEIN FUSION;

EID: 84871544347     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.409300     Document Type: Article
Times cited : (16)

References (52)
  • 1
    • 85075274229 scopus 로고    scopus 로고
    • (Grosjean, H., ed) . Landes Bioscience, Austin, TX
    • Grosjean, H. (2009) in DNA and RNA Modification Enzymes (Grosjean, H., ed) pp. 1-18, Landes Bioscience, Austin, TX
    • (2009) DNA and RNA Modification Enzymes , pp. 1-18
    • Grosjean, H.1
  • 4
    • 0019887281 scopus 로고
    • 5-(Carboxymethylamin-omethyl)- 2-thiouridine, a new modified nucleoside found at the first letter position of the anticodon
    • Yamada, Y., Murao, K., and Ishikura, H. (1981) 5-(Carboxymethylamin- omethyl)- 2-thiouridine, a new modified nucleoside found at the first letter position of the anticodon. Nucleic Acids Res. 9, 1933-1939
    • (1981) Nucleic Acids Res. , vol.9 , pp. 1933-1939
    • Yamada, Y.1    Murao, K.2    Ishikura, H.3
  • 5
    • 0024415902 scopus 로고
    • Codon recognition patterns as deduced from sequences of the complete set of transfer RNA species in Mycoplasma capricolum. Resemblance to mitochondria
    • DOI 10.1016/0022-2836(89)90168-X
    • Andachi, Y., Yamao, F., Muto, A., and Osawa, S. (1989) Codon recognition patterns as deduced from sequences of the complete set of transfer RNA species in Mycoplasma capricolum. Resemblance to mitochondria. J. Mol. Biol. 209, 37-54 (Pubitemid 19237806)
    • (1989) Journal of Molecular Biology , vol.209 , Issue.1 , pp. 37-54
    • Andachi, Y.1    Yamao, F.2    Muto, A.3    Osawa, S.4
  • 6
    • 0037011177 scopus 로고    scopus 로고
    • Taurine as a constituent of mitochondrial tRNAs: New insights into the functions of taurine and human mitochondrial diseases
    • DOI 10.1093/emboj/cdf656
    • Suzuki, T., Suzuki, T., Wada, T., Saigo, K., and Watanabe, K. (2002) Taurine as a constituent of mitochondrial tRNAs. New insights into the functions of taurine and human mitochondrial diseases. EMBO J. 21, 6581-6589 (Pubitemid 35448435)
    • (2002) EMBO Journal , vol.21 , Issue.23 , pp. 6581-6589
    • Suzuki, T.1    Suzuki, T.2    Wada, T.3    Saigo, K.4    Watanabe, K.5
  • 7
    • 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., Suzuki, T., Yukawa, M., Ohya, Y., Shindo, H., Watanabe, K., and Suzuki, T. (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
  • 8
    • 20044375499 scopus 로고    scopus 로고
    • (Curtiss, R., 3rd., Böck, A., Ingraham, J. L., Kaper, J. B., Maloy, S., Neidhardt, F. C., Riley, M. M., Squires, C. L., and Wanner, B. L., eds) American Society for Microbiology, Washington, D. C.
    • Björk, G. R., and Hagervall, T. G. (2005) in EcoSal-Escherichia coli and Salmonella: Cellular and Molecular Biology (Curtiss, R., 3rd., Böck, A., Ingraham, J. L., Kaper, J. B., Maloy, S., Neidhardt, F. C., Riley, M. M., Squires, C. L., and Wanner, B. L., eds) pp. 4.6.2, American Society for Microbiology, Washington, D. C.
    • (2005) EcoSal-Escherichia Coli and Salmonella: Cellular and Molecular Biology
    • Björk, G.R.1    Hagervall, T.G.2
  • 9
    • 46449083572 scopus 로고    scopus 로고
    • Bringing order to translation. The contributions of transfer RNA anticodon-domain modifications
    • Agris, P. F. (2008) Bringing order to translation. The contributions of transfer RNA anticodon-domain modifications. EMBO Rep. 9, 629-635
    • (2008) EMBO Rep. , vol.9 , pp. 629-635
    • Agris, P.F.1
  • 10
    • 71849108697 scopus 로고    scopus 로고
    • Deciphering synonymous codons in the three domains of life. Co-evolution with specific tRNA modification enzymes
    • Grosjean, H., de Crécy-Lagard, V., and Marck, C. (2010) Deciphering synonymous codons in the three domains of life. Co-evolution with specific tRNA modification enzymes. FEBS Lett. 584, 252-264
    • (2010) FEBS Lett. , vol.584 , pp. 252-264
    • Grosjean, H.1    De Crécy-Lagard, V.2    Marck, C.3
  • 11
    • 77952560288 scopus 로고    scopus 로고
    • Unique features of animal mitochondrial translation systems. The non-universal genetic code, unusual features of the translational apparatus, and their relevance to human mitochondrial diseases
    • Watanabe, K. (2010) Unique features of animal mitochondrial translation systems. The non-universal genetic code, unusual features of the translational apparatus, and their relevance to human mitochondrial diseases. Proc. Jpn. Acad. Ser. B Phys. Biol. Sci. 86, 11-39
    • (2010) Proc. Jpn. Acad. Ser. B Phys. Biol. Sci. , vol.86 , pp. 11-39
    • Watanabe, K.1
  • 13
    • 33845672606 scopus 로고    scopus 로고
    • Further insights into the tRNA modification process controlled by proteins MnmE and GidA of Escherichia coli
    • DOI 10.1093/nar/gkl752
    • Yim, L., Moukadiri, I., Björk, G. R., and Armengod, M. E. (2006) Further insights into the tRNA modification process controlled by proteinsMnmE and GidA of Escherichia coli. Nucleic Acids Res. 34, 5892-5905 (Pubitemid 44941168)
    • (2006) Nucleic Acids Research , vol.34 , Issue.20 , pp. 5892-5905
    • Yim, L.1    Moukadiri, I.2    Bjork, G.R.3    Armengod, M.-E.4
  • 14
    • 69749105129 scopus 로고    scopus 로고
    • G-domain dimerization orchestrates the tRNA wobble modification reaction in the MnmE/ GidA complex
    • Meyer, S., Wittinghofer, A., and Versées, W. (2009) G-domain dimerization orchestrates the tRNA wobble modification reaction in the MnmE/ GidA complex. J. Mol. Biol. 392, 910-922
    • (2009) J. Mol. Biol. , vol.392 , pp. 910-922
    • Meyer, S.1    Wittinghofer, A.2    Versées, W.3
  • 16
    • 65149088650 scopus 로고    scopus 로고
    • Conserved cysteine residues of GidA are essential for biogenesis of 5-carboxymethylaminomethyluridine at tRNA anticodon
    • Osawa, T., Ito, K., Inanaga, H., Nureki, O., Tomita, K., and Numata, T. (2009) Conserved cysteine residues of GidA are essential for biogenesis of 5-carboxymethylaminomethyluridine at tRNA anticodon. Structure 17, 713-724
    • (2009) Structure , vol.17 , pp. 713-724
    • Osawa, T.1    Ito, K.2    Inanaga, H.3    Nureki, O.4    Tomita, K.5    Numata, T.6
  • 17
    • 73649122039 scopus 로고    scopus 로고
    • Evolutionarily conserved proteins MnmE and GidA catalyze the formation of two methyluridine derivatives at tRNA wobble positions
    • Moukadiri, I., Prado, S., Piera, J., Velázquez-Campoy, A., Björk, G. R., and Armengod, M. E. (2009) Evolutionarily conserved proteins MnmE and GidA catalyze the formation of two methyluridine derivatives at tRNA wobble positions. Nucleic Acids Res. 37, 7177-7193
    • (2009) Nucleic Acids Res. , vol.37 , pp. 7177-7193
    • Moukadiri, I.1    Prado, S.2    Piera, J.3    Velázquez-Campoy, A.4    Björk, G.R.5    Armengod, M.E.6
  • 18
  • 19
    • 0015927336 scopus 로고
    • Biosynthesis of 5-methylaminomethyl- 2-thiouridylate. I. Isolation of a new tRNA-methylase specific for 5-meth-ylaminomethyl- 2-thiouridylate
    • Taya, Y., and Nishimura, S. (1973) Biosynthesis of 5-methylaminomethyl- 2-thiouridylate. I. Isolation of a new tRNA-methylase specific for 5-meth-ylaminomethyl- 2-thiouridylate. Biochem. Biophys. Res. Commun. 51, 1062-1068
    • (1973) Biochem. Biophys. Res. Commun. , vol.51 , pp. 1062-1068
    • Taya, Y.1    Nishimura, S.2
  • 20
    • 0023664535 scopus 로고
    • Transfer RNA(5-methylaminomethyl-2-thiouridine)-methyltransferase from Escherichia coli K-12 has two enzymatic activities
    • Hagervall, T. G., Edmonds, C. G., McCloskey, J. A., and Björk, G. R. (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
  • 21
    • 3343024377 scopus 로고    scopus 로고
    • Identification of a bifunctional enzyme MnmC involved in the biosynthesis of a hypermodified uridine in the wobble position of tRNA
    • DOI 10.1261/rna.7470904
    • Bujnicki, J. M., Oudjama, Y., Roovers, M., Owczarek, S., Caillet, J., and Droogmans, L. (2004) Identification of a bifunctional enzyme MnmC involved in the biosynthesis of a hypermodified uridine in the wobble position of tRNA. RNA 10, 1236-1242 (Pubitemid 38989009)
    • (2004) RNA , vol.10 , Issue.8 , pp. 1236-1242
    • Bujnicki, J.M.1    Oudjama, Y.2    Roovers, M.3    Owczarek, S.4    Caillet, J.5    Droogmans, L.6
  • 23
    • 0021770444 scopus 로고
    • Novel E. coli mutants deficient in biosynthesis of 5-methylaminomethyl-2- thiouridine
    • Elseviers, D., Petrullo, L. A., and Gallagher, P. J. (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.J.3
  • 25
    • 34548740836 scopus 로고    scopus 로고
    • In vitro detection of the enzymatic activity of folate-dependent tRNA (Uracil-54,-C5)-methyltransferase. Evolutionary implications
    • Urbonavicius, J., Brochier-Armanet, C., Skouloubris, S., Myllykallio, H., and Grosjean, H. (2007) In vitro detection of the enzymatic activity of folate-dependent tRNA (Uracil-54,-C5)-methyltransferase. Evolutionary implications. Methods Enzymol. 425, 103-119
    • (2007) Methods Enzymol. , vol.425 , pp. 103-119
    • Urbonavicius, J.1    Brochier-Armanet, C.2    Skouloubris, S.3    Myllykallio, H.4    Grosjean, H.5
  • 26
    • 0029838532 scopus 로고    scopus 로고
    • Purification of a rat neurotensin receptor expressed in Escherichia coli
    • Tucker, J., and Grisshammer, R. (1996) Purification of a rat neurotensin receptor expressed in Escherichia coli. Biochem. J. 317, 891-899 (Pubitemid 26308267)
    • (1996) Biochemical Journal , vol.317 , Issue.3 , pp. 891-899
    • Tucker, J.1    Grisshammer, R.2
  • 27
    • 79959332480 scopus 로고    scopus 로고
    • Crystal structure of the bifunctional tRNA modification enzyme MnmC from Escherichia coli
    • Kitamura, A., Sengoku, T., Nishimoto, M., Yokoyama, S., and Bessho, Y. (2011) Crystal structure of the bifunctional tRNA modification enzyme MnmC from Escherichia coli. Protein Sci. 20, 1105-1113
    • (2011) Protein Sci. , vol.20 , pp. 1105-1113
    • Kitamura, A.1    Sengoku, T.2    Nishimoto, M.3    Yokoyama, S.4    Bessho, Y.5
  • 28
    • 2142689200 scopus 로고    scopus 로고
    • SOLVE and RESOLVE. Automated structure solution, density modification, and model building
    • Terwilliger, T. (2004) SOLVE and RESOLVE. Automated structure solution, density modification, and model building. J. Synchrotron Radiat. 11, 49-52
    • (2004) J. Synchrotron Radiat. , vol.11 , pp. 49-52
    • Terwilliger, T.1
  • 30
    • 0028103275 scopus 로고
    • The CCP4 suite. Programs for protein crystallography
    • Collaborative Computational Project No. 4
    • Collaborative Computational Project No. 4 (1994) The CCP4 suite. Programs for protein crystallography. Acta Crystallogr. D. Biol. Crystallogr. 50, 760-763
    • (1994) Acta Crystallogr. D. Biol. Crystallogr. , vol.50 , pp. 760-763
  • 31
    • 0000243829 scopus 로고
    • PROCHECK. A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK. A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 32
    • 0019935329 scopus 로고
    • Quantitative enzymatic hydrolysis of tRNAs. Reversed-phase high-performance liquid chromatography of tRNA nucleosides
    • Gehrke, C. W., Kuo, K. C., McCune, R. A., Gerhardt, K. O., and Agris, P. F. (1982) Quantitative enzymatic hydrolysis of tRNAs. Reversed-phase highperformance liquid chromatography of tRNA nucleosides. J. Chromatogr. 230, 297-308 (Pubitemid 12058025)
    • (1982) Journal of Chromatography , vol.230 , Issue.2 , pp. 297-308
    • Gehrke, C.W.1    Kuo, K.C.2    McCune, R.A.3
  • 33
    • 0024362769 scopus 로고
    • Ribonucleoside analysis by reversed-phase high-performance liquid chromatography
    • DOI 10.1016/S0021-9673(00)94152-9
    • Gehrke, C. W., and Kuo, K. C. (1989) Ribonucleoside analysis by reversed-phase high-performance liquid chromatography. J. Chromatogr. 471, 3-36 (Pubitemid 19144813)
    • (1989) Journal of Chromatography , vol.471 , pp. 3-36
    • Gehrke, C.W.1    Kuo, K.C.2
  • 34
    • 0038374971 scopus 로고    scopus 로고
    • Many paths to methyltransfer: A chronicle of convergence
    • DOI 10.1016/S0968-0004(03)00090-2
    • Schubert, H. L., Blumenthal, R. M., and Cheng, X. (2003) Many paths to methyltransfer. A chronicle of convergence. Trends Biochem. Sci. 28, 329-335 (Pubitemid 36776296)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.6 , pp. 329-335
    • Schubert, H.L.1    Blumenthal, R.M.2    Cheng, X.3
  • 36
    • 20044392729 scopus 로고    scopus 로고
    • A 'gain of function' mutation in a protein mediates production of novel modified nucleosides
    • DOI 10.1038/sj.emboj.7600666
    • Chen, P., Crain, P. F., Näsvall, S. J., Pomerantz, S. C., and Björk, G. R. (2005) A "gain of function" mutation in a protein mediates production of novel modified nucleosides. EMBO J. 24, 1842-1851 (Pubitemid 40769503)
    • (2005) EMBO Journal , vol.24 , Issue.10 , pp. 1842-1851
    • Chen, P.1    Crain, P.F.2    Nasvall, S.J.3    Pomerantz, S.C.4    Bjork, G.R.5
  • 37
    • 0016219098 scopus 로고
    • Replacement of ribothymidine by 5-methyl-2-thiouridine in sequence GT psi C in tRNA of an extreme thermophile
    • Watanabe, K., Oshima, T., Saneyoshi, M., and Nishimura, S. (1974) Replacement of ribothymidine by 5-methyl-2-thiouridine in sequence GT psi C in tRNA of an extreme thermophile. FEBS Lett. 43, 59-63
    • (1974) FEBS Lett. , vol.43 , pp. 59-63
    • Watanabe, K.1    Oshima, T.2    Saneyoshi, M.3    Nishimura, S.4
  • 38
    • 0028272470 scopus 로고
    • The role of posttranscriptional modification in stabilization of transfer RNA from hyperthermophiles
    • DOI 10.1021/bi00191a014
    • Kowalak, J. A., Dalluge, J. J., McCloskey, J. A., and Stetter, K. O. (1994) The role of post-transcriptional modification in stabilization of transfer RNA from hyperthermophiles. Biochemistry 33, 7869-7876 (Pubitemid 24223805)
    • (1994) Biochemistry , vol.33 , Issue.25 , pp. 7869-7876
    • Kowalak, J.A.1    Dalluge, J.J.2    McCloskey, J.A.3    Stetter, K.O.4
  • 39
    • 33744946077 scopus 로고    scopus 로고
    • Identification of two tRNA thiolation genes required for cell growth at extremely high temperatures
    • DOI 10.1074/jbc.M511675200
    • Shigi, N., Sakaguchi, Y., Suzuki, T., and Watanabe, K. (2006) Identification of two tRNA thiolation genes required for cell growth at extremely high temperatures. J. Biol. Chem. 281, 14296-14306 (Pubitemid 43848358)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.20 , pp. 14296-14306
    • Shigi, N.1    Sakaguchi, Y.2    Suzuki, T.3    Watanabe, K.4
  • 40
    • 34648840096 scopus 로고    scopus 로고
    • Comparative RNomics and Modomics in mollicutes: Prediction of gene function and evolutionary implications
    • DOI 10.1080/15216540701604632, PII 781871696
    • de Crécy-Lagard, V., Marck, C., Brochier-Armanet, C., and Grosjean, H. (2007) Comparative RNomics and modomics in Mollicutes. Prediction of gene function and evolutionary implications. IUBMB Life 59, 634-658 (Pubitemid 47463915)
    • (2007) IUBMB Life , vol.59 , Issue.10 , pp. 634-658
    • De Crecy-Lagard, V.1    Marck, C.2    Brochier-Armanet, C.3    Grosjean, H.4
  • 41
    • 80755169463 scopus 로고    scopus 로고
    • Human mitochondrial tRNAs. Biogenesis, function, structural aspects, and diseases
    • Suzuki, T., and Nagao, A. (2011) Human mitochondrial tRNAs. Biogenesis, function, structural aspects, and diseases. Annu. Rev. Genet. 45, 299-329
    • (2011) Annu. Rev. Genet. , vol.45 , pp. 299-329
    • Suzuki, T.1    Nagao, A.2
  • 44
    • 0023046558 scopus 로고
    • A single tRNA (gua-nine)- Methyltransferase from Tetrahymena with both mono- and dimethylating activity
    • Reinhart, M. P., Lewis, J. M., and Leboy, P. S. (1986) A single tRNA (gua-nine)- methyltransferase from Tetrahymena with both mono- and dimethylating activity. Nucleic Acids Res. 14, 1131-1148
    • (1986) Nucleic Acids Res. , vol.14 , pp. 1131-1148
    • Reinhart, M.P.1    Lewis, J.M.2    Leboy, P.S.3
  • 45
    • 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
  • 50
    • 80053415582 scopus 로고    scopus 로고
    • Substrate tRNA recognition mechanism of a multisite-specific tRNA methyltransferase, Aquifex aeolicus Trm1, based on the X-ray crystal structure
    • Awai, T., Ochi, A., Ihsanawati, Sengoku, T., Hirata, A., Bessho, Y., Yokoyama, S., and Hori, H. (2011) Substrate tRNA recognition mechanism of a multisite-specific tRNA methyltransferase, Aquifex aeolicus Trm1, based on the X-ray crystal structure. J. Biol. Chem. 286, 35236-35246
    • (2011) J. Biol. Chem. , vol.286 , pp. 35236-35246
    • Awai, T.1    Ochi, A.2    Ihsanawati3    Sengoku, T.4    Hirata, A.5    Bessho, Y.6    Yokoyama, S.7    Hori, H.8
  • 51
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • DOI 10.1093/bioinformatics/15.4.305
    • Gouet, P., Courcelle, E., Stuart, D. I., and Métoz, F. (1999) ESPript. Analysis of multiple sequence alignments in PostScript. Bioinformatics 15, 305-308 (Pubitemid 29213756)
    • (1999) Bioinformatics , vol.15 , Issue.4 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 52


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.