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Volumn 7, Issue , 2006, Pages

The yfhQ gene of Escherichia coli encodes a tRNA:Cm32/Um32 methyltransferase

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BACTERIAL PROTEIN; BACTERIAL RNA; ESCHERICHIA COLI PROTEIN; METHYLTRANSFERASE; PROTEIN LAST; PROTEIN YBEA; PROTEIN YFHQ; PROTEIN YIBK; S ADENOSYLMETHIONINE; TRANSFER RNA; UNCLASSIFIED DRUG;

EID: 33748711082     PISSN: 14712199     EISSN: 14712199     Source Type: Journal    
DOI: 10.1186/1471-2199-7-23     Document Type: Article
Times cited : (41)

References (38)
  • 1
    • 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
  • 2
    • 0001918945 scopus 로고    scopus 로고
    • Location and distribution of modified nucleotides in tRNA
    • In Edited by: Grosjean H, Benne P, Washington: ASM Press
    • Auffinger P, Westhof E: Location and distribution of modified nucleotides in tRNA. In Modification and editing of RNA Edited by: Grosjean H, Benne P, Washington: ASM Press; 1998:569-576.
    • (1998) Modification and Editing of RNA , pp. 569-576
    • Auffinger, P.1    Westhof, E.2
  • 3
    • 0037439213 scopus 로고    scopus 로고
    • tRNA transfers to the limelight
    • Hopper AK, Phizicky EM: tRNA transfers to the limelight. Genes Dev 2003, 17(2):162-180.
    • (2003) Genes Dev , vol.17 , Issue.2 , pp. 162-180
    • Hopper, A.K.1    Phizicky, E.M.2
  • 4
    • 3042731061 scopus 로고    scopus 로고
    • Bioinformatics-guided identification and experimental characterization of novel RNA methyltransferases
    • In Edited by: Bujnicki JM. Berlin: Springer-Verlag
    • Bujnicki JM, Droogmans L, Grosjean H, Purushothaman SK, Lapeyre B: Bioinformatics-guided identification and experimental characterization of novel RNA methyltransferases. In Practical Bioinformatics Volume 15. Edited by: Bujnicki JM. Berlin: Springer-Verlag; 2004:139-168.
    • (2004) Practical Bioinformatics Volume 15 , pp. 139-168
    • Bujnicki, J.M.1    Droogmans, L.2    Grosjean, H.3    Purushothaman, S.K.4    Lapeyre, B.5
  • 6
    • 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
    • Bujnicki JM, Oudjama Y, Roovers M, Owczarek S, Caillet J, Droogmans L: Identification of a bifunctional enzyme MnmC involved in the biosynthesis of a hypermodified uridine in the wobble position of tRNA. Rna 2004, 10(8):1236-1242.
    • (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
  • 7
    • 0033302662 scopus 로고    scopus 로고
    • 6-adenine DNA methylation
    • 6-adenine DNA methylation. In Silica Biol 1999, 1(4):175-182.
    • (1999) Silico Biol , vol.1 , Issue.4 , pp. 175-182
    • Bujnicki, J.M.1
  • 8
    • 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(7):1427-1464.
    • (2002) Nucleic Acids Res , vol.30 , Issue.7 , pp. 1427-1464
    • Anantharaman, V.1    Koonin, E.V.2    Aravind, L.3
  • 9
    • 0036132209 scopus 로고    scopus 로고
    • SPOUT: A class of methyltransferases that includes spoU and trmD RNA methylase superfamilies, and novel superfamilies of predicted prokaryotic RNA methylases
    • Anantharaman V, Koonin EV, Aravind L: SPOUT: a class of methyltransferases that includes spoU and trmD RNA methylase superfamilies, and novel superfamilies of predicted prokaryotic RNA methylases. J Mol Microbiol Biotechnol 2002, 4(1):71-75.
    • (2002) J Mol Microbiol Biotechnol , vol.4 , Issue.1 , pp. 71-75
    • Anantharaman, V.1    Koonin, E.V.2    Aravind, L.3
  • 10
    • 0038374971 scopus 로고    scopus 로고
    • Many paths to methyltransfer: A chronicle of convergence
    • Schubert HL, Blumenthal RM, Cheng X: Many paths to methyltransfer: a chronicle of convergence. Trends Biochem Sci 2003, 28(6):329-335.
    • (2003) Trends Biochem Sci , vol.28 , Issue.6 , pp. 329-335
    • Schubert, H.L.1    Blumenthal, R.M.2    Cheng, X.3
  • 11
    • 0034596029 scopus 로고    scopus 로고
    • The FtsJ/RrmJ heat shock protein of Escherichia coli is a 23 Sribosomal RNA methyltransferase
    • Caldas T, Binet E, Bouloc P, Costa A, Desgres J, Richarme G: The FtsJ/RrmJ heat shock protein of Escherichia coli is a 23 Sribosomal RNA methyltransferase. J Biol Chem 2000, 275(22):16414-16419.
    • (2000) J Biol Chem , vol.275 , Issue.22 , pp. 16414-16419
    • Caldas, T.1    Binet, E.2    Bouloc, P.3    Costa, A.4    Desgres, J.5    Richarme, G.6
  • 13
    • 1842404152 scopus 로고    scopus 로고
    • The spoU gene of Escherichia, coli, the fourth gene of the spoT operon, is essential for tRNA (Gm 18) 2′-O-methyltransferase activity
    • Persson BC, Jager G, Gustafsson C: The spoU gene of Escherichia, coli, the fourth gene of the spoT operon, is essential for tRNA (Gm 18) 2′-O-methyltransferase activity. Nucleic Acids Res 1997, 25(20):4093-4097.
    • (1997) Nucleic Acids Res , vol.25 , Issue.20 , pp. 4093-4097
    • Persson, B.C.1    Jager, G.2    Gustafsson, C.3
  • 14
    • 1842607227 scopus 로고    scopus 로고
    • Deep knot structure for construction of active site and cofactor binding site of tRNA modification enzyme
    • Nureki O, Watanabe K, Fukai S, Ishii R, Endo Y, Hori H, Yokoyama S: Deep knot structure for construction of active site and cofactor binding site of tRNA modification enzyme. Structure (Camb) 2004, 12(4):593-602.
    • (2004) Structure (Camb) , vol.12 , Issue.4 , pp. 593-602
    • Nureki, O.1    Watanabe, K.2    Fukai, S.3    Ishii, R.4    Endo, Y.5    Hori, H.6    Yokoyama, S.7
  • 15
    • 0037007220 scopus 로고    scopus 로고
    • Trm7p catalyses the formation of two 2′-O-methylriboses in yeast tRNA anticodon loop
    • Pintard L, Lecointe F, Bujnicki JM, Bonnerot C, Grosjean H, Lapeyre B: Trm7p catalyses the formation of two 2′-O-methylriboses in yeast tRNA anticodon loop. Embo J 2002, 21(7):1811-1820.
    • (2002) Embo J , vol.21 , Issue.7 , pp. 1811-1820
    • Pintard, L.1    Lecointe, F.2    Bujnicki, J.M.3    Bonnerot, C.4    Grosjean, H.5    Lapeyre, B.6
  • 16
    • 0037413674 scopus 로고    scopus 로고
    • Molecular phylogenetics of the RrmJ/fibrillarin superfamily of ribose 2′-O-methyltransferases
    • Feder M, Pas J, Wyrwicz LS, Bujnicki JM: Molecular phylogenetics of the RrmJ/fibrillarin superfamily of ribose 2′-O-methyltransferases. Gene 2003, 302(1-2):129-138.
    • (2003) Gene , vol.302 , Issue.1-2 , pp. 129-138
    • Feder, M.1    Pas, J.2    Wyrwicz, L.S.3    Bujnicki, J.M.4
  • 18
    • 0029832294 scopus 로고    scopus 로고
    • Identification of new RNA modifying enzymes by iterative genome search using known modifying enzymes as probes
    • Gustafsson C, Reid R, Greene PJ, Santi DV: Identification of new RNA modifying enzymes by iterative genome search using known modifying enzymes as probes. Nucleic Acids Res 1996, 24(19):3756-3762.
    • (1996) Nucleic Acids Res , vol.24 , Issue.19 , pp. 3756-3762
    • Gustafsson, C.1    Reid, R.2    Greene, P.J.3    Santi, D.V.4
  • 19
    • 0036774065 scopus 로고    scopus 로고
    • The structure of the RlmB 23S rRNA methyltransferase reveals a new methyltransferase fold with a unique knot
    • Michel G, Sauve V, Larocque P, Li Y, Matte A, Cygler M: The structure of the RlmB 23S rRNA methyltransferase reveals a new methyltransferase fold with a unique knot. Structure (Camb) 2002, 10:1303-1315.
    • (2002) Structure (Camb) , vol.10 , pp. 1303-1315
    • Michel, G.1    Sauve, V.2    Larocque, P.3    Li, Y.4    Matte, A.5    Cygler, M.6
  • 22
    • 24044464543 scopus 로고    scopus 로고
    • Functional analysis of 1440 Escherichia coli genes using the combination of knock-out library and phenotype microarrays
    • Ito M, Baba T, Mori H: Functional analysis of 1440 Escherichia coli genes using the combination of knock-out library and phenotype microarrays. Metab Eng 2005, 7(4):318-327.
    • (2005) Metab Eng , vol.7 , Issue.4 , pp. 318-327
    • Ito, M.1    Baba, T.2    Mori, H.3
  • 23
    • 0037375572 scopus 로고    scopus 로고
    • Structure of the YibK methyltransferase from Haemophilus influenzae (H10766): A cofactor bound at a site formed by a knot
    • Lim K, Zhang H, Tempczyk A, Krajewski W, Bonander N, Toedt J, Howard A, Eisenstein E, Herzberg O: Structure of the YibK methyltransferase from Haemophilus influenzae (H10766): a cofactor bound at a site formed by a knot. Proteins 2003, 51(1):56-67.
    • (2003) Proteins , vol.51 , Issue.1 , pp. 56-67
    • Lim, K.1    Zhang, H.2    Tempczyk, A.3    Krajewski, W.4    Bonander, N.5    Toedt, J.6    Howard, A.7    Eisenstein, E.8    Herzberg, O.9
  • 24
    • 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(13):3305-3307.
    • (2003) Nucleic Acids Res , vol.31 , Issue.13 , pp. 3305-3307
    • Kurowski, M.A.1    Bujnicki, J.M.2
  • 25
    • 9644281537 scopus 로고    scopus 로고
    • Structure and function of the antibiotic resistance-mediating methyltransferase AviRb from Streptomyces viridochromogenes
    • Mosbacher TG, Bechthold A, Schulz GE: Structure and function of the antibiotic resistance-mediating methyltransferase AviRb from Streptomyces viridochromogenes. J Mol Biol 2005, 345(3):535-545.
    • (2005) J Mol Biol , vol.345 , Issue.3 , pp. 535-545
    • Mosbacher, T.G.1    Bechthold, A.2    Schulz, G.E.3
  • 26
    • 0242362160 scopus 로고    scopus 로고
    • 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
    • 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.
    • (2003) Proteins , vol.53 , Issue.SUPPL. 6 , pp. 369-379
    • Kosinski, J.1    Cymerman, I.A.2    Feder, M.3    Kurowski, M.A.4    Sasin, J.M.5    Bujnicki, J.M.6
  • 28
    • 15444370839 scopus 로고    scopus 로고
    • Roles of conserved amino acid, sequence motifsin the SpoU (TrmH) RNA methyltransferase family
    • Watanabe K, Nureki O, Fukai S, Ishii R, Okamoto H, Yokoyama S, Endo Y, Hori H: Roles of conserved amino acid, sequence motifsin the SpoU (TrmH) RNA methyltransferase family. J Biol Chem 2005, 280(11):10368-10377.
    • (2005) J Biol Chem , vol.280 , Issue.11 , pp. 10368-10377
    • Watanabe, K.1    Nureki, O.2    Fukai, S.3    Ishii, R.4    Okamoto, H.5    Yokoyama, S.6    Endo, Y.7    Hori, H.8
  • 29
    • 37349087176 scopus 로고    scopus 로고
    • Conserved ribosomal RNA modification and their putative roles in ribosome biogenesis and translation
    • In Edited by: Grosjean H. Berlin-Heidelberg: Springer-Verlag
    • Lapeyre B: Conserved ribosomal RNA modification and their putative roles in ribosome biogenesis and translation. In Finetuning of RNA functions by modification and editing Volume 12. Edited by: Grosjean H. Berlin-Heidelberg: Springer-Verlag; 2005.
    • (2005) Finetuning of RNA Functions By Modification and Editing Volume 12
    • Lapeyre, B.1
  • 32
    • 2542429274 scopus 로고    scopus 로고
    • Distinct origins of tRNA(mlG37) methyltransferase
    • Christian T, Evilia C, Williams S, Hou YM: Distinct origins of tRNA(mlG37) methyltransferase. J Mol Biol 2004, 339(4):707-719.
    • (2004) J Mol Biol , vol.339 , Issue.4 , pp. 707-719
    • Christian, T.1    Evilia, C.2    Williams, S.3    Hou, Y.M.4
  • 33
    • 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, Chetouani F, Bachellerie JP: The yeast Saccharomyces cerevisiae YDL112w ORF encodes the putative 2′-O-ribose methyltransferase catalyzing the formation of Gm18 in tRNAs. Rna 1999, 5(1):66-81.
    • (1999) Rna , vol.5 , Issue.1 , pp. 66-81
    • Cavaille, J.1    Chetouani, F.2    Bachellerie, J.P.3
  • 34
    • 0035955465 scopus 로고    scopus 로고
    • 1 A58 methyltransferase family: Homology-based fold prediction and identification of new members from Eubacteria and Archaea
    • 1 A58 methyltransferase family: homology-based fold prediction and identification of new members from Eubacteria and Archaea. FEBS Lett 2001, 507(2):123-127.
    • (2001) FEBS Lett , vol.507 , Issue.2 , pp. 123-127
    • Bujnicki, J.M.1
  • 36
    • 0028239805 scopus 로고
    • Crystal structure of unmodifiedtRNA(GIn) complexed with glutaminyl-tRNA synthetase and ATP suggests a possible role for pseudo-uridines in stabilization of RNA structure
    • Arnez JG, Steitz TA: Crystal structure of unmodifiedtRNA(GIn) complexed with glutaminyl-tRNA synthetase and ATP suggests a possible role for pseudo-uridines in stabilization of RNA structure. Biochemistry 1994, 33(24):7560-7567.
    • (1994) Biochemistry , vol.33 , Issue.24 , pp. 7560-7567
    • Arnez, J.G.1    Steitz, T.A.2
  • 37
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama N, Woody RW: Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal Biochem 2000, 287(2):252-260.
    • (2000) Anal Biochem , vol.287 , Issue.2 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 38
    • 3142766402 scopus 로고    scopus 로고
    • Detection and quantification of modified nucleotides in RNA using thin-layer chromatography
    • Grosjean H, Keith G, Droogmans L: Detection and quantification of modified nucleotides; in RNA using thin-layer chromatography. Methods Mol Biol 2004, 265:357-391.
    • (2004) Methods Mol Biol , vol.265 , pp. 357-391
    • Grosjean, H.1    Keith, G.2    Droogmans, L.3


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