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Volumn 70, Issue 1, 2008, Pages 1-18

Structural bioinformatics analysis of enzymes involved in the biosynthesis pathway of the hypermodified nucleoside ms2io6A37 in tRNA

Author keywords

Enzymes acting on RNA; Fold recognition; Molecular evolution; Protein structure prediction; Remote homology; RNA modification

Indexed keywords

6 N (3,3 DIMETHYLALLYL)ADENOSINE; ADENOSINE; ALKANE; CARBOXYLIC ACID; ENZYME; FERRITIN; FLAVODOXIN; HYDROXYLASE MIAE; METHANE MONOOXYGENASE; METHYLTHIOTRANSFERASE MIAB; N6 (4 HYDROXYISOPENTENYL) 2 THIOMETHYLADENOSINE; N6 ISOPENTENYL 2 THIOMETHYLADENOSINE; NUCLEOSIDE; NUCLEOSIDE TRIPHOSPHATASE; PRENYLTRANSFERASE MIAA; PROTEIN; PROTEIN TRAM; TRANSFER RNA; UNCLASSIFIED DRUG; URIDINE;

EID: 37349028282     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21640     Document Type: Article
Times cited : (40)

References (84)
  • 3
    • 0021731924 scopus 로고
    • On the biological significance of modified nucleosides in tRNA
    • Kersten H. On the biological significance of modified nucleosides in tRNA. Prog Nucleic Acid Res Mol Biol 1984;31:59-114.
    • (1984) Prog Nucleic Acid Res Mol Biol , vol.31 , pp. 59-114
    • Kersten, H.1
  • 4
    • 0029169650 scopus 로고
    • Genetic dissection of synthesis and function of modified nucleosides in bacterial transfer RNA
    • Bjork GR. Genetic dissection of synthesis and function of modified nucleosides in bacterial transfer RNA. Prog Nucleic Acid Res Mol Biol 1995;50:263-338.
    • (1995) Prog Nucleic Acid Res Mol Biol , vol.50 , pp. 263-338
    • Bjork, G.R.1
  • 6
    • 0022424144 scopus 로고
    • Nucleotide 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, Soll D, Cedergren R. Nucleotide sequences of two serine tRNAs with a GGA anticodon: the structure-function relationships in the serine family of E. coli tRNAs. Nucleic Acids Res 1985;13:5697-5706.
    • (1985) Nucleic Acids Res , vol.13 , pp. 5697-5706
    • Grosjean, H.1    Nicoghosian, K.2    Haumont, E.3    Soll, D.4    Cedergren, R.5
  • 7
    • 0020491144 scopus 로고
    • cis 2-Methylthioribosylzeatin (ms2io6A) is present in the transfer RNA of Salmonella typhimurium, but not Escherichia coli
    • Buck M, McCloskey JA, Basile B, Ames BN. cis 2-Methylthioribosylzeatin (ms2io6A) is present in the transfer RNA of Salmonella typhimurium, but not Escherichia coli. Nucleic Acids Res 1982;10:5649-5662.
    • (1982) Nucleic Acids Res , vol.10 , pp. 5649-5662
    • Buck, M.1    McCloskey, J.A.2    Basile, B.3    Ames, B.N.4
  • 9
    • 0014194905 scopus 로고
    • Cytokinins in the soluble RNA of plant tissues
    • Hall RH, Csonka L, David H, McLennan B. Cytokinins in the soluble RNA of plant tissues. Science 1967;156:69-71.
    • (1967) Science , vol.156 , pp. 69-71
    • Hall, R.H.1    Csonka, L.2    David, H.3    McLennan, B.4
  • 11
    • 9144220291 scopus 로고    scopus 로고
    • MiaB protein is a bifunctional radical-S-adenosylmethionine enzyme involved in thiolation and methylation of tRNA
    • Pierrel F, Douki T, Fontecave M, Atta M. MiaB protein is a bifunctional radical-S-adenosylmethionine enzyme involved in thiolation and methylation of tRNA. J Biol Chem 2004;279:47555-47563.
    • (2004) J Biol Chem , vol.279 , pp. 47555-47563
    • Pierrel, F.1    Douki, T.2    Fontecave, M.3    Atta, M.4
  • 12
    • 0032725978 scopus 로고    scopus 로고
    • Identification of the miaB gene, involved in methylthiolation of isopentenylated A37 derivatives in the tRNA of Salmonella typhimurium and Escherichia coli
    • Esberg B, Leung HC, Tsui HC, Bjork GR, Winkler ME. Identification of the miaB gene, involved in methylthiolation of isopentenylated A37 derivatives in the tRNA of Salmonella typhimurium and Escherichia coli. J Bacteriol 1999;181:7256-7265.
    • (1999) J Bacteriol , vol.181 , pp. 7256-7265
    • Esberg, B.1    Leung, H.C.2    Tsui, H.C.3    Bjork, G.R.4    Winkler, M.E.5
  • 13
    • 0027131291 scopus 로고
    • Isolation of the gene (miaE) encoding the hydroxylase involved in the synthesis of 2-methylthio-cis-ribozeatin in tRNA of Salmonella typhimurium and characterization of mutants
    • Persson BC, Bjork GR. Isolation of the gene (miaE) encoding the hydroxylase involved in the synthesis of 2-methylthio-cis-ribozeatin in tRNA of Salmonella typhimurium and characterization of mutants. J Bacteriol 1993;175:7776-7785.
    • (1993) J Bacteriol , vol.175 , pp. 7776-7785
    • Persson, B.C.1    Bjork, G.R.2
  • 14
    • 0021256993 scopus 로고
    • A modified nucleotide in tRNA as a possible regulator of aerobiosis: Synthesis of cis-2-methyl-thioribosylzeatin in the tRNA of Salmonella
    • Buck M, Ames BN. A modified nucleotide in tRNA as a possible regulator of aerobiosis: synthesis of cis-2-methyl-thioribosylzeatin in the tRNA of Salmonella. Cell 1984;36:523-531.
    • (1984) Cell , vol.36 , pp. 523-531
    • Buck, M.1    Ames, B.N.2
  • 15
    • 0028986353 scopus 로고
    • 6A) present next to the anticodon contributes to the decoding efficiency of the tRNA
    • 6A) present next to the anticodon contributes to the decoding efficiency of the tRNA. J Bacteriol 1995;177:1967-1975.
    • (1995) J Bacteriol , vol.177 , pp. 1967-1975
    • Esberg, B.1    Bjork, G.R.2
  • 16
    • 0018179979 scopus 로고
    • Isopentenyladenosine deficient tRNA from an antisuppressor mutant of Saccharomyces cerevisiae
    • Laten H, Gorman J, Bock RM. Isopentenyladenosine deficient tRNA from an antisuppressor mutant of Saccharomyces cerevisiae. Nucleic Acids Res 1978;5:4329-4342.
    • (1978) Nucleic Acids Res , vol.5 , pp. 4329-4342
    • Laten, H.1    Gorman, J.2    Bock, R.M.3
  • 17
    • 0020489739 scopus 로고
    • Iron mediated methylthiolation of tRNA as a regulator of operon expression in Escherichia coli
    • Buck M, Griffiths E. Iron mediated methylthiolation of tRNA as a regulator of operon expression in Escherichia coli. Nucleic Acids Res 1982;10:2609-2624.
    • (1982) Nucleic Acids Res , vol.10 , pp. 2609-2624
    • Buck, M.1    Griffiths, E.2
  • 18
    • 0022655673 scopus 로고
    • Pleiotropic effects induced by modification deficiency next to the anticodon of tRNA from Salmonella typhimurium LT2
    • Ericson JU, Bjork GR. Pleiotropic effects induced by modification deficiency next to the anticodon of tRNA from Salmonella typhimurium LT2. J Bacteriol 1986;166:1013-1021.
    • (1986) J Bacteriol , vol.166 , pp. 1013-1021
    • Ericson, J.U.1    Bjork, G.R.2
  • 19
    • 0023369964 scopus 로고
    • Effects of miaA on translation and growth rates
    • Diaz I, Pedersen S, Kurland CG. Effects of miaA on translation and growth rates. Mol Gen Genet 1987;208:373-376.
    • (1987) Mol Gen Genet , vol.208 , pp. 373-376
    • Diaz, I.1    Pedersen, S.2    Kurland, C.G.3
  • 20
    • 1842376275 scopus 로고    scopus 로고
    • The modified nucleoside 2-methylthio-N6-isopentenyladenosine in tRNA of Shigella flexneri is required for expression of virulence genes
    • Durand JM, Bjork GR, Kuwae A, Yoshikawa M, Sasakawa C. The modified nucleoside 2-methylthio-N6-isopentenyladenosine in tRNA of Shigella flexneri is required for expression of virulence genes. J Bacteriol 1997;179:5777-5782.
    • (1997) J Bacteriol , vol.179 , pp. 5777-5782
    • Durand, J.M.1    Bjork, G.R.2    Kuwae, A.3    Yoshikawa, M.4    Sasakawa, C.5
  • 21
    • 0026531622 scopus 로고
    • Mutation of the miaA gene of Agrobacterium tumefaciens results in reduced vir gene expression
    • Gray J, Wang J, Gelvin SB. Mutation of the miaA gene of Agrobacterium tumefaciens results in reduced vir gene expression. J Bacteriol 1992;174:1086-1098.
    • (1992) J Bacteriol , vol.174 , pp. 1086-1098
    • Gray, J.1    Wang, J.2    Gelvin, S.B.3
  • 22
    • 0014674092 scopus 로고
    • Role of modifications in tyrosine transfer RNA: A modified base affecting ribosome binding
    • Gefter ML, Russell RL. Role of modifications in tyrosine transfer RNA: a modified base affecting ribosome binding. J Mol Biol 1969;39:145-157.
    • (1969) J Mol Biol , vol.39 , pp. 145-157
    • Gefter, M.L.1    Russell, R.L.2
  • 23
    • 0022344630 scopus 로고
    • Temperature jump relaxation studies on the interactions between transfer RNAs with complementary anticodons. The effect of modified bases adjacent to the anticodon triplet
    • Houssier C, Grosjean H. Temperature jump relaxation studies on the interactions between transfer RNAs with complementary anticodons. The effect of modified bases adjacent to the anticodon triplet. J Biomol Struct Dyn 1985;3:387-408.
    • (1985) J Biomol Struct Dyn , vol.3 , pp. 387-408
    • Houssier, C.1    Grosjean, H.2
  • 24
    • 0000036468 scopus 로고
    • Presence of the hypermodified nucleotide N6-(delta 2-isopentenyl)-2-methylthioadenosine prevents codon misreading by Escherichia coli phenylalanyl-transfer RNA
    • Wilson RK, Roe BA. Presence of the hypermodified nucleotide N6-(delta 2-isopentenyl)-2-methylthioadenosine prevents codon misreading by Escherichia coli phenylalanyl-transfer RNA. Proc Natl Acad Sci USA 1989;86:409-413.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 409-413
    • Wilson, R.K.1    Roe, B.A.2
  • 25
    • 0035801515 scopus 로고    scopus 로고
    • Improvement of reading frame maintenance is a common function for several tRNA modifications
    • Urbonavicius J, Qian Q, Durand JM, Hagervall TG, Bjork GR. Improvement of reading frame maintenance is a common function for several tRNA modifications. Embo J 2001;20:4863-4873.
    • (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
  • 26
    • 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 ME, Nikonowicz EP. Solution conformations of unmodified and A(37)N(6)-dimethylallyl modified anticodon stem-loops of Escherichia coli tRNA(Phe). J Mol Biol 2002;319:1015-1034.
    • (2002) J Mol Biol , vol.319 , pp. 1015-1034
    • Cabello-Villegas, J.1    Winkler, M.E.2    Nikonowicz, E.P.3
  • 29
    • 0034732888 scopus 로고    scopus 로고
    • Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: Essential elements for recognition of tRNA substrates within the anticodon stem-loop
    • Soderberg T, Poulter CD. Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: essential elements for recognition of tRNA substrates within the anticodon stem-loop. Biochemistry 2000;39:6546-6553.
    • (2000) Biochemistry , vol.39 , pp. 6546-6553
    • Soderberg, T.1    Poulter, C.D.2
  • 30
    • 0035852848 scopus 로고    scopus 로고
    • Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: Site-directed mutagenesis of highly conserved residues
    • Soderberg T, Poulter CD. Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: site-directed mutagenesis of highly conserved residues. Biochemistry 2001;40:1734-1740.
    • (2001) Biochemistry , vol.40 , pp. 1734-1740
    • Soderberg, T.1    Poulter, C.D.2
  • 31
    • 0035282866 scopus 로고    scopus 로고
    • Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: Functional characterization using new analysis and information visualization methods
    • Sofia HJ, Chen G, Hetzler BG, Reyes-Spindola JF, Miller NE. Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods. Nucleic Acids Res 2001;29:1097-1106.
    • (2001) Nucleic Acids Res , vol.29 , pp. 1097-1106
    • Sofia, H.J.1    Chen, G.2    Hetzler, B.G.3    Reyes-Spindola, J.F.4    Miller, N.E.5
  • 34
    • 33750001271 scopus 로고    scopus 로고
    • MUMMALS: Multiple sequence alignment improved by using hidden Markov models with local structural information
    • Pei J, Grishin NV. MUMMALS: multiple sequence alignment improved by using hidden Markov models with local structural information. Nucleic Acids Res 2006;34:4364-4374.
    • (2006) Nucleic Acids Res , vol.34 , pp. 4364-4374
    • Pei, J.1    Grishin, N.V.2
  • 35
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: Integrated software for Molecular Evolutionary Genetics Analysis and sequence alignment
    • Kumar S, Tamura K, Nei M. MEGA3: Integrated software for Molecular Evolutionary Genetics Analysis and sequence alignment. Brief Bioinform 2004;5:150-163.
    • (2004) Brief Bioinform , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 37
    • 0043123216 scopus 로고    scopus 로고
    • GeneSilico protein structure prediction meta-server
    • Kurowski MA, Bujnicki JM. GeneSilico protein structure prediction meta-server. Nucleic Acids Res 2003;31:3305-3307.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3305-3307
    • Kurowski, M.A.1    Bujnicki, J.M.2
  • 38
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin LJ, Bryson K, Jones DT. The PSIPRED protein structure prediction server. Bioinformatics 2000;16:404-405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 40
    • 0033933636 scopus 로고    scopus 로고
    • Cascaded multiple classifiers for secondary structure prediction
    • Ouali M, King RD. Cascaded multiple classifiers for secondary structure prediction. Protein Sci 2000;9:1162-1176.
    • (2000) Protein Sci , vol.9 , pp. 1162-1176
    • Ouali, M.1    King, R.D.2
  • 41
    • 4043052866 scopus 로고    scopus 로고
    • Accurate prediction of solvent accessibility using neural networks-based regression
    • Adamczak R, Porollo A, Meller J. Accurate prediction of solvent accessibility using neural networks-based regression. Proteins 2004;56:753-767.
    • (2004) Proteins , vol.56 , pp. 753-767
    • Adamczak, R.1    Porollo, A.2    Meller, J.3
  • 42
    • 0034663597 scopus 로고    scopus 로고
    • Application of multiple sequence alignment profiles to improve protein secondary structure prediction
    • Cuff JA, Barton GJ. Application of multiple sequence alignment profiles to improve protein secondary structure prediction. Proteins 2000;40:502-511.
    • (2000) Proteins , vol.40 , pp. 502-511
    • Cuff, J.A.1    Barton, G.J.2
  • 43
    • 0142027795 scopus 로고    scopus 로고
    • Coupled prediction of protein secondary and tertiary structure
    • Meiler J, Baker D. Coupled prediction of protein secondary and tertiary structure. Proc Natl Acad Sci USA 2003;100:12105-12110.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 12105-12110
    • Meiler, J.1    Baker, D.2
  • 44
    • 0242362161 scopus 로고    scopus 로고
    • Combining local-structure, fold-recognition, and new fold methods for protein structure prediction
    • Karplus K, Karchin R, Draper J, Casper J, Mandel-Gutfreund Y, Diekhans M, Hughey R. Combining local-structure, fold-recognition, and new fold methods for protein structure prediction. Proteins 2003;53 (Suppl 6):491-496.
    • (2003) Proteins , vol.53 , Issue.SUPPL. 6 , pp. 491-496
    • Karplus, K.1    Karchin, R.2    Draper, J.3    Casper, J.4    Mandel-Gutfreund, Y.5    Diekhans, M.6    Hughey, R.7
  • 45
    • 0033997036 scopus 로고    scopus 로고
    • Comparison of sequence profiles. Strategies for structural predictions using sequence information
    • Rychlewski L, Jaroszewski L, Li W, Godzik A. Comparison of sequence profiles. Strategies for structural predictions using sequence information. Protein Sci 2000;9:232-241.
    • (2000) Protein Sci , vol.9 , pp. 232-241
    • Rychlewski, L.1    Jaroszewski, L.2    Li, W.3    Godzik, A.4
  • 46
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation using structural profiles in the program 3D-PSSM
    • Kelley LA, MacCallum RM, Sternberg MJ. Enhanced genome annotation using structural profiles in the program 3D-PSSM. J Mol Biol 2000;299:499-520.
    • (2000) J Mol Biol , vol.299 , pp. 499-520
    • Kelley, L.A.1    MacCallum, R.M.2    Sternberg, M.J.3
  • 47
    • 0035967880 scopus 로고    scopus 로고
    • FUGUE: Sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • Shi J, Blundell TL, Mizuguchi K. FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J Mol Biol 2001;310:243-257.
    • (2001) J Mol Biol , vol.310 , pp. 243-257
    • Shi, J.1    Blundell, T.L.2    Mizuguchi, K.3
  • 48
    • 0033537993 scopus 로고    scopus 로고
    • GenTHREADER: An efficient and reliable protein fold recognition method for genomic sequences
    • Jones DT. GenTHREADER: an efficient and reliable protein fold recognition method for genomic sequences. J Mol Biol 1999;287:797-815.
    • (1999) J Mol Biol , vol.287 , pp. 797-815
    • Jones, D.T.1
  • 49
    • 2542631929 scopus 로고    scopus 로고
    • Single-body residue-level knowledge-based energy score combined with sequence-profile and secondary structure information for fold recognition
    • Zhou H, Zhou Y. Single-body residue-level knowledge-based energy score combined with sequence-profile and secondary structure information for fold recognition. Proteins 2004;55:1005-1013.
    • (2004) Proteins , vol.55 , pp. 1005-1013
    • Zhou, H.1    Zhou, Y.2
  • 50
    • 28444454499 scopus 로고    scopus 로고
    • Pcons5: Combining consensus, structural evaluation and fold recognition scores
    • Wallner B, Elofsson A. Pcons5: combining consensus, structural evaluation and fold recognition scores. Bioinformatics 2005;21:4248-4254.
    • (2005) Bioinformatics , vol.21 , pp. 4248-4254
    • Wallner, B.1    Elofsson, A.2
  • 51
    • 30344467519 scopus 로고    scopus 로고
    • Generalized protein structure prediction based on combination of fold-recognition with de novo folding and evaluation of models
    • Kolinski A, Bujnicki JM. Generalized protein structure prediction based on combination of fold-recognition with de novo folding and evaluation of models. Proteins 2005;61 (Suppl 7):84-90.
    • (2005) Proteins , vol.61 , Issue.SUPPL. 7 , pp. 84-90
    • Kolinski, A.1    Bujnicki, J.M.2
  • 52
    • 0242362160 scopus 로고    scopus 로고
    • Kosinski J, Cymerman IA, Feder M, Kurowski MA, Sasin JM, Bujnicki JM. A Frankenstein's monster approach to comparative modeling: merging the finest fragments of Fold-Recognition models and iterative model refinement aided by 3D structure evaluation. Proteins 2003;53 (Suppl 6):369-379.
    • Kosinski J, Cymerman IA, Feder M, Kurowski MA, Sasin JM, Bujnicki JM. A "Frankenstein's monster" approach to comparative modeling: merging the finest fragments of Fold-Recognition models and iterative model refinement aided by 3D structure evaluation. Proteins 2003;53 (Suppl 6):369-379.
  • 54
    • 0347383758 scopus 로고    scopus 로고
    • Modeller: Generation and refinement of homologybased protein structure models
    • Fiser A, Sali A. Modeller: generation and refinement of homologybased protein structure models. Methods Enzymol 2003;374:461-491.
    • (2003) Methods Enzymol , vol.374 , pp. 461-491
    • Fiser, A.1    Sali, A.2
  • 55
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Luthy R, Bowie JU, Eisenberg D. Assessment of protein models with three-dimensional profiles. Nature 1992;356:83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 57
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L, Sander C. Protein structure comparison by alignment of distance matrices. J Mol Biol 1993;233:123-138.
    • (1993) J Mol Biol , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 59
    • 0037406141 scopus 로고    scopus 로고
    • Can correct protein models be identified?
    • Wallner B, Elofsson A. Can correct protein models be identified? Protein Sci 2003;12:1073-1086.
    • (2003) Protein Sci , vol.12 , pp. 1073-1086
    • Wallner, B.1    Elofsson, A.2
  • 62
    • 1642325936 scopus 로고    scopus 로고
    • Evolutionary history and higher order classification of AAA+ ATPases
    • Iyer LM, Leipe DD, Koonin EV, Aravind L. Evolutionary history and higher order classification of AAA+ ATPases. J Struct Biol 2004;146:11-31.
    • (2004) J Struct Biol , vol.146 , pp. 11-31
    • Iyer, L.M.1    Leipe, D.D.2    Koonin, E.V.3    Aravind, L.4
  • 63
    • 0142011067 scopus 로고    scopus 로고
    • Evolution and classification of P-loop kinases and related proteins
    • Leipe DD, Koonin EV, Aravind L. Evolution and classification of P-loop kinases and related proteins. J Mol Biol 2003;333:781-815.
    • (2003) J Mol Biol , vol.333 , pp. 781-815
    • Leipe, D.D.1    Koonin, E.V.2    Aravind, L.3
  • 64
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • Leipe DD, Wolf YI, Koonin EV, Aravind L. Classification and evolution of P-loop GTPases and related ATPases. J Mol Biol 2002;317:41-72.
    • (2002) J Mol Biol , vol.317 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 65
    • 0036529621 scopus 로고    scopus 로고
    • Comparative genomics and evolution of proteins involved in RNA metabolism
    • Anantharaman V, Koonin EV, Aravind L. Comparative genomics and evolution of proteins involved in RNA metabolism. Nucleic Acids Res 2002;30:1427-1464.
    • (2002) Nucleic Acids Res , vol.30 , pp. 1427-1464
    • Anantharaman, V.1    Koonin, E.V.2    Aravind, L.3
  • 66
    • 2542445427 scopus 로고    scopus 로고
    • ConSurf: Identification of functional regions in proteins by surface-mapping of phylogenetic information
    • Glaser F, Pupko T, Paz I, Bell RE, Bechor-Shental D, Martz E, Ben-Tal N. ConSurf: identification of functional regions in proteins by surface-mapping of phylogenetic information. Bioinformatics 2003;19:163-164.
    • (2003) Bioinformatics , vol.19 , pp. 163-164
    • Glaser, F.1    Pupko, T.2    Paz, I.3    Bell, R.E.4    Bechor-Shental, D.5    Martz, E.6    Ben-Tal, N.7
  • 67
    • 0036882288 scopus 로고    scopus 로고
    • Analysis of protein-nucleic acid interactions by photochemical cross-linking and mass spectrometry
    • Steen H, Jensen ON. Analysis of protein-nucleic acid interactions by photochemical cross-linking and mass spectrometry. Mass Spectrom Rev 2002;21:163-182.
    • (2002) Mass Spectrom Rev , vol.21 , pp. 163-182
    • Steen, H.1    Jensen, O.N.2
  • 68
    • 0037236038 scopus 로고    scopus 로고
    • A top down approach to protein structural studies using chemical cross-linking and Fourier transform mass spectrometry
    • Kruppa GH, Schoeniger J, Young MM. A top down approach to protein structural studies using chemical cross-linking and Fourier transform mass spectrometry. Rapid Commun Mass Spectrom 2003;17:155-162.
    • (2003) Rapid Commun Mass Spectrom , vol.17 , pp. 155-162
    • Kruppa, G.H.1    Schoeniger, J.2    Young, M.M.3
  • 70
    • 0035853480 scopus 로고    scopus 로고
    • Anantharaman V, Koonin EV, Aravind L. TRAM, a predicted RNA-binding domain, common to tRNA uracil methylation and adenine thiolation enzymes. FEMS Microbiol Lett 2001;197:215-221.
    • Anantharaman V, Koonin EV, Aravind L. TRAM, a predicted RNA-binding domain, common to tRNA uracil methylation and adenine thiolation enzymes. FEMS Microbiol Lett 2001;197:215-221.
  • 71
    • 14844293080 scopus 로고    scopus 로고
    • A unique RNA Fold in the RumA-RNA-cofactor ternary complex contributes to substrate selectivity and enzymatic function
    • Lee TT, Agarwalla S, Stroud RM. A unique RNA Fold in the RumA-RNA-cofactor ternary complex contributes to substrate selectivity and enzymatic function. Cell 2005;120:599-611.
    • (2005) Cell , vol.120 , pp. 599-611
    • Lee, T.T.1    Agarwalla, S.2    Stroud, R.M.3
  • 72
    • 3242882336 scopus 로고    scopus 로고
    • AdoMet radical proteins-from structure to evolution - alignment of divergent protein sequences reveals strong secondary structure element conservation
    • Nicolet Y, Drennan CL. AdoMet radical proteins-from structure to evolution - alignment of divergent protein sequences reveals strong secondary structure element conservation. Nucleic Acids Res 2004;32:4015-4025.
    • (2004) Nucleic Acids Res , vol.32 , pp. 4015-4025
    • Nicolet, Y.1    Drennan, C.L.2
  • 73
    • 0037134469 scopus 로고    scopus 로고
    • Enzymatic modification of tRNAs: MiaB is an iron-sulfur protein
    • Pierrel F, Bjork GR, Fontecave M, Atta M. Enzymatic modification of tRNAs: MiaB is an iron-sulfur protein. J Biol Chem 2002;277:13367-13370.
    • (2002) J Biol Chem , vol.277 , pp. 13367-13370
    • Pierrel, F.1    Bjork, G.R.2    Fontecave, M.3    Atta, M.4
  • 74
    • 0033287696 scopus 로고    scopus 로고
    • B12 (cobalamin)-dependent enzymes
    • Marsh EN. Coenzyme B12 (cobalamin)-dependent enzymes. Essays Biochem 1999;34:139-154.
    • (1999) Essays Biochem , vol.34 , pp. 139-154
    • Coenzyme, M.E.N.1
  • 75
    • 0030589146 scopus 로고    scopus 로고
    • The structure of the C-terminal domain of methionine synthase: Presenting S-adenosylmethionine for reductive methylation of B12
    • Dixon MM, Huang S, Matthews RG, Ludwig M. The structure of the C-terminal domain of methionine synthase: presenting S-adenosylmethionine for reductive methylation of B12. Structure 1996;4:1263-1275.
    • (1996) Structure , vol.4 , pp. 1263-1275
    • Dixon, M.M.1    Huang, S.2    Matthews, R.G.3    Ludwig, M.4
  • 76
    • 34247631048 scopus 로고    scopus 로고
    • Hernandez HL, Pierrel F, Elleingand E, Garcia-Serres R, Huynh BH, Johnson MK, Fontecave M, Atta M. MiaB, a bifunctional radical-S-adenosylmethionine enzyme involved in the thiolation and methylation of tRNA, contains two essential [4Fe-4S] clusters. Biochemistry 2007;46:5140-5147.
    • Hernandez HL, Pierrel F, Elleingand E, Garcia-Serres R, Huynh BH, Johnson MK, Fontecave M, Atta M. MiaB, a bifunctional radical-S-adenosylmethionine enzyme involved in the thiolation and methylation of tRNA, contains two essential [4Fe-4S] clusters. Biochemistry 2007;46:5140-5147.
  • 78
    • 0027913094 scopus 로고
    • Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane
    • Rosenzweig AC, Frederick CA, Lippard SJ, Nordlund P. Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane. Nature 1993;366:537-543.
    • (1993) Nature , vol.366 , pp. 537-543
    • Rosenzweig, A.C.1    Frederick, C.A.2    Lippard, S.J.3    Nordlund, P.4
  • 79
    • 0017847369 scopus 로고
    • Resolution of the methane mono-oxygenase of Methylococcus capsulatus (Bath) into three components. Purification and properties of component C, a flavoprotein
    • Colby J, Dalton H. Resolution of the methane mono-oxygenase of Methylococcus capsulatus (Bath) into three components. Purification and properties of component C, a flavoprotein. Biochem J 1978;171:461-468.
    • (1978) Biochem J , vol.171 , pp. 461-468
    • Colby, J.1    Dalton, H.2
  • 81
    • 0036802760 scopus 로고    scopus 로고
    • Soluble methane monooxygenase: Activation of dioxygen and methane
    • Kopp DA, Lippard SJ. Soluble methane monooxygenase: activation of dioxygen and methane. Curr Opin Chem Biol 2002;6:568-576.
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 568-576
    • Kopp, D.A.1    Lippard, S.J.2
  • 82
    • 1542377662 scopus 로고    scopus 로고
    • Dioxygen activation in methane monooxygenase: A theoretical study
    • Gherman BF, Baik MH, Lippard SJ, Friesner RA. Dioxygen activation in methane monooxygenase: a theoretical study. J Am Chem Soc 2004;126:2978-2990.
    • (2004) J Am Chem Soc , vol.126 , pp. 2978-2990
    • Gherman, B.F.1    Baik, M.H.2    Lippard, S.J.3    Friesner, R.A.4
  • 83
    • 12444307479 scopus 로고    scopus 로고
    • Substrate hydroxylation in methane monooxygenase: Quantitative modeling via mixed quantum mechanics/molecular mechanics techniques
    • Gherman BF, Lippard SJ, Friesner RA. Substrate hydroxylation in methane monooxygenase: quantitative modeling via mixed quantum mechanics/molecular mechanics techniques. J Am Chem Soc 2005;127:1025-1037.
    • (2005) J Am Chem Soc , vol.127 , pp. 1025-1037
    • Gherman, B.F.1    Lippard, S.J.2    Friesner, R.A.3
  • 84
    • 0017394040 scopus 로고
    • Zeatin ribonucleosides in the transfer ribonucleic acid of Rhizobium leguminosarum, Agrobacterium tumefaciens, Corynebacterium fascians, and Erwinia amylovora
    • Cherayil JD, Lipsett MN. Zeatin ribonucleosides in the transfer ribonucleic acid of Rhizobium leguminosarum, Agrobacterium tumefaciens, Corynebacterium fascians, and Erwinia amylovora. J Bacteriol 1977;131:741-744.
    • (1977) J Bacteriol , vol.131 , pp. 741-744
    • Cherayil, J.D.1    Lipsett, M.N.2


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