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Volumn 42, Issue 1, 2014, Pages 509-525

Crystal structure of tRNA m1G9 methyltransferase Trm10: Insight into the catalytic mechanism and recognition of tRNA substrate

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE; PROTEIN TRM10; S ADENOSYLHOMOCYSTEINE; TRANSFER RNA METHYLTRANSFERASE; UNCLASSIFIED DRUG; HOMODIMER; METHYLTRANSFERASE; MONOMER; SPOUT PROTEIN; TRANSFER RNA; TRM10 PROTEIN;

EID: 84891757846     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkt869     Document Type: Article
Times cited : (43)

References (71)
  • 1
    • 0029169650 scopus 로고
    • Genetic dissection of synthesis and function of modified nucleosides in bacterial transfer-Rna
    • Bjork, G.R. (1995) Genetic dissection of synthesis and function of modified nucleosides in bacterial transfer-Rna. Prog. Nucleic Acid Res., 50, 263-338
    • (1995) Prog. Nucleic Acid Res , vol.50 , pp. 263-338
    • Bjork, G.R.1
  • 2
    • 1242309517 scopus 로고    scopus 로고
    • Decoding the genome: A modified view
    • Agris, P.F. (2004) Decoding the genome: A modified view. Nucleic Acids Res., 32, 223-238
    • (2004) Nucleic Acids Res , vol.32 , pp. 223-238
    • Agris, P.F.1
  • 4
    • 32644447756 scopus 로고    scopus 로고
    • Post-Transcriptional nucleotide modification and alternative folding of RNA
    • Helm, M. (2006) Post-Transcriptional nucleotide modification and alternative folding of RNA. Nucleic Acids Res., 34, 721-733
    • (2006) Nucleic Acids Res , vol.34 , pp. 721-733
    • Helm, M.1
  • 5
    • 42149137980 scopus 로고    scopus 로고
    • TRNA's modifications bring order to gene expression
    • Gustilo, E.M., Vendeix, F.A. and Agris, P.F. (2008) tRNA's modifications bring order to gene expression. Curr. Opin. Microbiol., 11, 134-140
    • (2008) Curr. Opin. Microbiol , vol.11 , pp. 134-140
    • Gustilo, E.M.1    Vendeix, F.A.2    Agris, P.F.3
  • 6
    • 84871436566 scopus 로고    scopus 로고
    • Transfer RNA modifications: Nature's combinatorial chemistry playground
    • Wiley Interdiscip
    • Jackman, J.E. and Alfonzo, J.D. (2013) Transfer RNA modifications: Nature's combinatorial chemistry playground. Wiley Interdiscip. Rev. RNA, 4, 35-48
    • (2013) Rev. RNA , vol.4 , pp. 35-48
    • Jackman, J.E.1    Alfonzo, J.D.2
  • 7
    • 0344923796 scopus 로고    scopus 로고
    • Structural alterations of the tRNA(m1G37)methyltransferase from Salmonella typhimurium affect tRNA substrate specificity
    • Li, J.N. and Bjork, G.R. (1999) Structural alterations of the tRNA(m1G37)methyltransferase from Salmonella typhimurium affect tRNA substrate specificity. RNA, 5, 395-408
    • (1999) RNA , vol.5 , pp. 395-408
    • Li, J.N.1    Bjork, G.R.2
  • 9
    • 2542429274 scopus 로고    scopus 로고
    • Distinct origins of tRNA(m1G37) methyltransferase
    • Christian, T., Evilia, C., Williams, S. and Hou, Y.M. (2004) Distinct origins of tRNA(m1G37) methyltransferase. J. Mol. Biol., 339, 707-719
    • (2004) J. Mol. Biol , vol.339 , pp. 707-719
    • Christian, T.1    Evilia, C.2    Williams, S.3    Hou, Y.M.4
  • 10
    • 0037407933 scopus 로고    scopus 로고
    • Identification of the yeast gene encoding the tRNA m1G methyltransferase responsible for modification at position 9
    • Jackman, J.E., Montange, R.K., Malik, H.S. and Phizicky, E.M. (2003) Identification of the yeast gene encoding the tRNA m1G methyltransferase responsible for modification at position 9. RNA, 9, 574-585
    • (2003) RNA , vol.9 , pp. 574-585
    • Jackman, J.E.1    Montange, R.K.2    Malik, H.S.3    Phizicky, E.M.4
  • 11
    • 41649102484 scopus 로고    scopus 로고
    • Evidence that tRNA modifying enzymes are important in vivo targets for 5-fluorouracil in yeast
    • Gustavsson, M. and Ronne, H. (2008) Evidence that tRNA modifying enzymes are important in vivo targets for 5-fluorouracil in yeast. RNA, 14, 666-674
    • (2008) RNA , vol.14 , pp. 666-674
    • Gustavsson, M.1    Ronne, H.2
  • 12
    • 79960967666 scopus 로고    scopus 로고
    • Variants in SUP45 and TRM10 underlie natural variation in translation termination efficiency in Saccharomyces cerevisiae
    • Torabi, N. and Kruglyak, L. (2011) Variants in SUP45 and TRM10 underlie natural variation in translation termination efficiency in Saccharomyces cerevisiae. Plos Genet., 7, e1002211
    • (2011) Plos Genet , vol.7
    • Torabi, N.1    Kruglyak, L.2
  • 13
    • 84871194226 scopus 로고    scopus 로고
    • A subcomplex of human mitochondrial RNase P is a bifunctional methyltransferase- extensive moonlighting in mitochondrial tRNA biogenesis
    • Vilardo, E., Nachbagauer, C., Buzet, A., Taschner, A., Holzmann, J. and Rossmanith, W. (2012) A subcomplex of human mitochondrial RNase P is a bifunctional methyltransferase- extensive moonlighting in mitochondrial tRNA biogenesis. Nucleic Acids Res., 40, 11583-11593
    • (2012) Nucleic Acids Res , vol.40 , pp. 11583-11593
    • Vilardo, E.1    Nachbagauer, C.2    Buzet, A.3    Taschner, A.4    Holzmann, J.5    Rossmanith, W.6
  • 14
    • 0032052242 scopus 로고    scopus 로고
    • The presence of modified nucleotides is required for cloverleaf folding of a human mitochondrial tRNA
    • Helm, M., Brule, H., Degoul, F., Cepanec, C., Leroux, J.P., Giege, R. and Florentz, C. (1998) The presence of modified nucleotides is required for cloverleaf folding of a human mitochondrial tRNA. Nucleic Acids Res., 26, 1636-1643
    • (1998) Nucleic Acids Res , vol.26 , pp. 1636-1643
    • Helm, M.1    Brule, H.2    Degoul, F.3    Cepanec, C.4    Leroux, J.P.5    Giege, R.6    Florentz, C.7
  • 15
    • 71549158173 scopus 로고    scopus 로고
    • Stereochemical mechanisms of tRNA methyltransferases
    • Hou, Y.M. and Perona, J.J. (2010) Stereochemical mechanisms of tRNA methyltransferases. FEBS Lett., 584, 278-286
    • (2010) FEBS Lett , vol.584 , pp. 278-286
    • Hou, Y.M.1    Perona, J.J.2
  • 17
    • 0038374971 scopus 로고    scopus 로고
    • Many paths to methyltransfer: A chronicle of convergence
    • Schubert, H.L., Blumenthal, R.M. and Cheng, X. (2003) Many paths to methyltransfer: A chronicle of convergence. Trends Biochem. Sci., 28, 329-335
    • (2003) Trends Biochem. Sci , vol.28 , pp. 329-335
    • Schubert, H.L.1    Blumenthal, R.M.2    Cheng, X.3
  • 18
    • 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, E.V. and Aravind, L. (2002) 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., 4, 71-75
    • (2002) J. Mol. Microbiol. Biotechnol , vol.4 , pp. 71-75
    • Anantharaman, V.1    Koonin, E.V.2    Aravind, L.3
  • 19
    • 34648820435 scopus 로고    scopus 로고
    • Structural and evolutionary bioinformatics of the SPOUT superfamily of methyltransferases
    • Tkaczuk, K.L., Dunin-Horkawicz, S., Purta, E. and Bujnicki, J.M. (2007) Structural and evolutionary bioinformatics of the SPOUT superfamily of methyltransferases. BMC Bioinformatics, 8, 73
    • (2007) BMC Bioinformatics , vol.8 , pp. 73
    • Tkaczuk, K.L.1    Dunin-Horkawicz, S.2    Purta, E.3    Bujnicki, J.M.4
  • 20
    • 78049370805 scopus 로고    scopus 로고
    • New archaeal methyltransferases forming 1-methyladenosine or 1-methyladenosine and 1-methylguanosine at position 9 of tRNA
    • Kempenaers, M., Roovers, M., Oudjama, Y., Tkaczuk, K.L., Bujnicki, J.M. and Droogmans, L. (2010) New archaeal methyltransferases forming 1-methyladenosine or 1-methyladenosine and 1-methylguanosine at position 9 of tRNA. Nucleic Acids Res., 38, 6533-6543
    • (2010) Nucleic Acids Res , vol.38 , pp. 6533-6543
    • Kempenaers, M.1    Roovers, M.2    Oudjama, Y.3    Tkaczuk, K.L.4    Bujnicki, J.M.5    Droogmans, L.6
  • 21
    • 54549088876 scopus 로고    scopus 로고
    • RNase P without RNA: Identification and functional reconstitution of the human mitochondrial tRNA processing enzyme
    • Holzmann, J., Frank, P., Loffler, E., Bennett, K.L., Gerner, C. and Rossmanith, W. (2008) RNase P without RNA: Identification and functional reconstitution of the human mitochondrial tRNA processing enzyme. Cell, 135, 462-474
    • (2008) Cell , vol.135 , pp. 462-474
    • Holzmann, J.1    Frank, P.2    Loffler, E.3    Bennett, K.L.4    Gerner, C.5    Rossmanith, W.6
  • 24
  • 27
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Method Enzymol., 276, 307-326
    • (1997) Method Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 29
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. and Cowtan, K. (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr. D, 60, 2126-2132
    • (2004) Acta Crystallogr , vol.D60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 30
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G.N., Vagin, A.A. and Dodson, E.J. (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D, 53, 240-255
    • (1997) Acta Crystallogr , vol.D53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 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
    • 34548801413 scopus 로고    scopus 로고
    • Detection of enzymatic activity of transfer RNA modification enzymes using radiolabeled tRNA substrates
    • Grosjean, H., Droogmans, L., Roovers, M. and Keith, G. (2007) Detection of enzymatic activity of transfer RNA modification enzymes using radiolabeled tRNA substrates. Methods Enzymol., 425, 55-101
    • (2007) Methods Enzymol , vol.425 , pp. 55-101
    • Grosjean, H.1    Droogmans, L.2    Roovers, M.3    Keith, G.4
  • 33
    • 84934441519 scopus 로고    scopus 로고
    • High-purity enzymatic synthesis of sitespecifically modified tRNA
    • Hou, Y.M. (2012) High-purity enzymatic synthesis of sitespecifically modified tRNA. Methods Mol. Biol., 941, 195-212
    • (2012) Methods Mol. Biol , vol.941 , pp. 195-212
    • Hou, Y.M.1
  • 36
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-Transform methods using perceptual criteria
    • Svergun, D.I. (1992) Determination of the regularization parameter in indirect-Transform methods using perceptual criteria. J. Appl. Crystallogr., 25, 495-503
    • (1992) J. Appl. Crystallogr , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 37
    • 75649147383 scopus 로고    scopus 로고
    • Determination of the molecular weight of proteins in solution from a single small-Angle X-ray scattering measurement on a relative scale
    • Fischer, H., Neto, M.D., Napolitano, H.B., Polikarpov, I. and Craievich, A.F. (2010) Determination of the molecular weight of proteins in solution from a single small-Angle X-ray scattering measurement on a relative scale. J. Appl. Crystallogr., 43, 101-109
    • (2010) J. Appl. Crystallogr , vol.43 , pp. 101-109
    • Fischer, H.1    Neto, M.D.2    Napolitano, H.B.3    Polikarpov, I.4    Craievich, A.F.5
  • 38
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun, D.I., Petoukhov, M.V. and Koch, M.H.J. (2001) Determination of domain structure of proteins from X-ray solution scattering. Biophys. J., 80, 2946-2953
    • (2001) Biophys. J. , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.J.3
  • 39
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- And low-resolution structural models
    • Kozin, M.B. and Svergun, D.I. (2001) Automated matching of high- And low-resolution structural models. J. Appl. Crystallogr., 34, 33-41
    • (2001) J. Appl. Crystallogr , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 40
  • 43
    • 78049370805 scopus 로고    scopus 로고
    • New archaeal methyltransferases forming 1-methyladenosine or 1- methyladenosine and 1-methylguanosine at position 9 of tRNA
    • Kempenaers, M., Roovers, M., Oudjama, Y., Tkaczuk, K.L., Bujnicki, J.M. and Droogmans, L. (2010) New archaeal methyltransferases forming 1-methyladenosine or 1- methyladenosine and 1-methylguanosine at position 9 of tRNA. Nucleic Acids Res., 38, 6533-6543
    • (2010) Nucleic Acids Res , vol.38 , pp. 6533-6543
    • Kempenaers, M.1    Roovers, M.2    Oudjama, Y.3    Tkaczuk, K.L.4    Bujnicki, J.M.5    Droogmans, L.6
  • 44
    • 34748874591 scopus 로고    scopus 로고
    • Distinct determinants of tRNA recognition by the TrmD and Trm5 methyl transferases
    • Christian, T. and Hou, Y.M. (2007) Distinct determinants of tRNA recognition by the TrmD and Trm5 methyl transferases. J. Mol. Biol., 373, 623-632
    • (2007) J. Mol. Biol , vol.373 , pp. 623-632
    • Christian, T.1    Hou, Y.M.2
  • 45
    • 84880683872 scopus 로고    scopus 로고
    • Unexpected expansion of tRNA substrate recognition by the yeast m1G9 methyltransferase Trm10
    • Swinehart, W.E., Henderson, J.C. and Jackman, J.E. (2013) Unexpected expansion of tRNA substrate recognition by the yeast m1G9 methyltransferase Trm10. RNA, 19, 1137-1146
    • (2013) RNA , vol.19 , pp. 1137-1146
    • Swinehart, W.E.1    Henderson, J.C.2    Jackman, J.E.3
  • 46
    • 78649649697 scopus 로고    scopus 로고
    • Mechanism of N-methylation by the tRNA m1G37 methyltransferase Trm5
    • Christian, T., Lahoud, G., Liu, C., Hoffmann, K., Perona, J.J. and Hou, Y.M. (2010) Mechanism of N-methylation by the tRNA m1G37 methyltransferase Trm5. RNA, 16, 2484-2492
    • (2010) RNA , vol.16 , pp. 2484-2492
    • Christian, T.1    Lahoud, G.2    Liu, C.3    Hoffmann, K.4    Perona, J.J.5    Hou, Y.M.6
  • 47
    • 77953808683 scopus 로고    scopus 로고
    • Control of catalytic cycle by a pair of analogous tRNA modification enzymes
    • Christian, T., Lahoud, G., Liu, C. and Hou, Y.M. (2010) Control of catalytic cycle by a pair of analogous tRNA modification enzymes. J. Mol. Biol., 400, 204-217
    • (2010) J. Mol. Biol , vol.400 , pp. 204-217
    • Christian, T.1    Lahoud, G.2    Liu, C.3    Hou, Y.M.4
  • 48
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm, L. and Rosenstrom, P. (2010) Dali server: Conservation mapping in 3D. Nucleic Acids Res., 38, W545-W549
    • (2010) Nucleic Acids Res , vol.38
    • Holm, L.1    Rosenstrom, P.2
  • 49
    • 0037375572 scopus 로고    scopus 로고
    • Structure of the YibK methyltransferase from Haemophilus influenzae (HI0766): 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. and Herzberg, O. (2003) Structure of the YibK methyltransferase from Haemophilus influenzae (HI0766): A cofactor bound at a site formed by a knot. Proteins, 51, 56-67
    • (2003) Proteins , vol.51 , 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
  • 50
    • 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. and Yokoyama, S. (2004) Deep knot structure for construction of active site and cofactor binding site of tRNA modification enzyme. Structure, 12, 593-602
    • (2004) Structure , vol.12 , pp. 593-602
    • Nureki, O.1    Watanabe, K.2    Fukai, S.3    Ishii, R.4    Endo, Y.5    Hori, H.6    Yokoyama, S.7
  • 51
    • 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, R., Li, Y., Matte, A. and Cygler, M. (2002) The structure of the RlmB 23S rRNA methyltransferase reveals a new methyltransferase fold with a unique knot. Structure, 10, 1303-1315
    • (2002) Structure , vol.10 , pp. 1303-1315
    • Michel, G.1    Sauve, V.2    Larocque, R.3    Li, Y.4    Matte, A.5    Cygler, M.6
  • 52
    • 0037526102 scopus 로고    scopus 로고
    • Crystal structure of tRNA(m1G37)methyltransferase: Insights into tRNA recognition
    • Ahn, H.J., Kim, H.W., Yoon, H.J., Lee, B.I., Suh, S.W. and Yang, J.K. (2003) Crystal structure of tRNA(m1G37)methyltransferase: Insights into tRNA recognition. EMBO J., 22, 2593-2603
    • (2003) EMBO J. , vol.22 , pp. 2593-2603
    • Ahn, H.J.1    Kim, H.W.2    Yoon, H.J.3    Lee, B.I.4    Suh, S.W.5    Yang, J.K.6
  • 53
    • 0036206498 scopus 로고    scopus 로고
    • Identification and characterization of tRNA (Gm18) methyltransferase from Thermus thermophilus HB8: Domain structure and conserved amino acid sequence motifs
    • Hori, H., Suzuki, T., Sugawara, K., Inoue, Y., Shibata, T., Kuramitsu, S., Yokoyama, S., Oshima, T. and Watanabe, K. (2002) Identification and characterization of tRNA (Gm18) methyltransferase from Thermus thermophilus HB8: Domain structure and conserved amino acid sequence motifs. Genes Cells, 7, 259-272
    • (2002) Genes Cells , vol.7 , pp. 259-272
    • Hori, H.1    Suzuki, T.2    Sugawara, K.3    Inoue, Y.4    Shibata, T.5    Kuramitsu, S.6    Yokoyama, S.7    Oshima, T.8    Watanabe, K.9
  • 55
    • 84872081024 scopus 로고    scopus 로고
    • Characterization of the Staphylococcus aureus rRNA methyltransferase encoded by orfX, the gene containing the staphylococcal chromosome Cassette mec (SCCmec) insertion site
    • Boundy, S., Safo, M.K., Wang, L., Musayev, F.N., O'Farrell, H.C., Rife, J.P. and Archer, G.L. (2013) Characterization of the Staphylococcus aureus rRNA methyltransferase encoded by orfX, the gene containing the staphylococcal chromosome Cassette mec (SCCmec) insertion site. J. Biol. Chem., 288, 132-140
    • (2013) J. Biol. Chem , vol.288 , pp. 132-140
    • Boundy, S.1    Safo, M.K.2    Wang, L.3    Musayev, F.N.4    O'Farrell, H.C.5    Rife, J.P.6    Archer, G.L.7
  • 57
    • 70349813956 scopus 로고    scopus 로고
    • Tertiary structure checkpoint at anticodon loop modification in tRNA functional maturation
    • Goto-Ito, S., Ito, T., Kuratani, M., Bessho, Y. and Yokoyama, S. (2009) Tertiary structure checkpoint at anticodon loop modification in tRNA functional maturation. Nat. Struct. Mol. Biol., 16, 1109-1115
    • (2009) Nat. Struct. Mol. Biol , vol.16 , pp. 1109-1115
    • Goto-Ito, S.1    Ito, T.2    Kuratani, M.3    Bessho, Y.4    Yokoyama, S.5
  • 58
    • 0027479161 scopus 로고
    • OB(oligonucleotide/oligosaccharide binding)- fold: Common structural and functional solution for nonhomologous sequences
    • Murzin, A.G. (1993) OB(oligonucleotide/oligosaccharide binding)- fold: Common structural and functional solution for nonhomologous sequences. EMBO J., 12, 861-867
    • (1993) EMBO J. , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 59
    • 0033046425 scopus 로고    scopus 로고
    • Novel predicted RNAbinding domains associated with the translation machinery
    • Aravind, L. and Koonin, E.V. (1999) Novel predicted RNAbinding domains associated with the translation machinery. J. Mol. Evol., 48, 291-302
    • (1999) J. Mol. Evol , vol.48 , pp. 291-302
    • Aravind, L.1    Koonin, E.V.2
  • 60
    • 0035312922 scopus 로고    scopus 로고
    • THUMP-A predicted RNAbinding domain shared by 4-Thiouridine pseudouridine synthases and RNA methylases
    • Aravind, L. and Koonin, E.V. (2001) THUMP-A predicted RNAbinding domain shared by 4-Thiouridine, pseudouridine synthases and RNA methylases. Trends Biochem. Sci., 26, 215-217
    • (2001) Trends Biochem. Sci , vol.26 , pp. 215-217
    • Aravind, L.1    Koonin, E.V.2
  • 61
    • 34548847733 scopus 로고    scopus 로고
    • Using circular dichroism spectra to estimate protein secondary structure
    • Greenfield, N.J. (2006) Using circular dichroism spectra to estimate protein secondary structure. Nat. Protoc., 1, 2876-2890
    • (2006) Nat. Protoc , vol.1 , pp. 2876-2890
    • Greenfield, N.J.1
  • 62
    • 0037677275 scopus 로고    scopus 로고
    • Protein concentration is not an absolute prerequisite for the determination of secondary structure from circular dichroism spectra: A new scaling method
    • Raussens, V., Ruysschaert, J.M. and Goormaghtigh, E. (2003) Protein concentration is not an absolute prerequisite for the determination of secondary structure from circular dichroism spectra: A new scaling method. Anal. Biochem., 319, 114-121
    • (2003) Anal. Biochem , vol.319 , pp. 114-121
    • Raussens, V.1    Ruysschaert, J.M.2    Goormaghtigh, E.3
  • 63
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. and Sander, C. (1983) Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers, 22, 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 64
    • 79953683436 scopus 로고    scopus 로고
    • Structural insight into the functional mechanism of Nep1/Emg1 N1-specific pseudouridine methyltransferase in ribosome biogenesis
    • Thomas, S.R., Keller, C.A., Szyk, A., Cannon, J.R. and Laronde- Leblanc, N.A. (2011) Structural insight into the functional mechanism of Nep1/Emg1 N1-specific pseudouridine methyltransferase in ribosome biogenesis. Nucleic Acids Res., 39, 2445-2457
    • (2011) Nucleic Acids Res , vol.39 , pp. 2445-2457
    • Thomas, S.R.1    Keller, C.A.2    Szyk, A.3    Cannon, J.R.4    Laronde-Leblanc, N.A.5
  • 65
    • 0034658247 scopus 로고    scopus 로고
    • A domain in the N-Terminal extension of class IIb eukaryotic aminoacyl-TRNA synthetases is important for tRNA binding
    • Frugier, M., Moulinier, L. and Giege, R. (2000) A domain in the N-Terminal extension of class IIb eukaryotic aminoacyl-TRNA synthetases is important for tRNA binding. EMBO J., 19, 2371-2380
    • (2000) EMBO J. , vol.19 , pp. 2371-2380
    • Frugier, M.1    Moulinier, L.2    Giege, R.3
  • 66
    • 84885173270 scopus 로고    scopus 로고
    • TRNA binding, positioning, and modification by the pseudouridine synthase Pus10
    • Kamalampeta, R., Keffer-Wilkes, L.C. and Kothe, U. (2013) tRNA binding, positioning, and modification by the pseudouridine synthase Pus10. J. Mol. Biol., 425, 3863-3874
    • (2013) J. Mol. Biol , vol.425 , pp. 3863-3874
    • Kamalampeta, R.1    Keffer-Wilkes, L.C.2    Kothe, U.3
  • 67
    • 0242331664 scopus 로고    scopus 로고
    • Structure of tRNA pseudouridine synthase TruB and its RNA complex: RNA recognition through a combination of rigid docking and induced fit
    • Pan, H., Agarwalla, S., Moustakas, D.T., Finer-Moore, J. and Stroud, R.M. (2003) Structure of tRNA pseudouridine synthase TruB and its RNA complex: RNA recognition through a combination of rigid docking and induced fit. Proc. Natl Acad. Sci. USA, 100, 12648-12653
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 12648-12653
    • Pan, H.1    Agarwalla, S.2    Moustakas, D.T.3    Finer-Moore, J.4    Stroud, R.M.5
  • 68
    • 0029828910 scopus 로고    scopus 로고
    • Expression of rat aspartyl-TRNA synthetase in Saccharomyces cerevisiae role of the nh2-Terminal polypeptide extension on enzyme activity and stability
    • Agou, F., Waller, J.P. and Mirande, M. (1996) Expression of rat aspartyl-TRNA synthetase in Saccharomyces cerevisiae. Role of the NH2-Terminal polypeptide extension on enzyme activity and stability. J. Biol. Chem., 271, 29295-29303
    • (1996) J. Biol. Chem , vol.271 , pp. 29295-29303
    • Agou, F.1    Waller, J.P.2    Mirande, M.3
  • 69
    • 59149107301 scopus 로고    scopus 로고
    • The human short-chain dehydrogenase/reductase (SDR) superfamily: A bioinformatics summary
    • Bray, J.E., Marsden, B.D. and Oppermann, U. (2009) The human short-chain dehydrogenase/reductase (SDR) superfamily: A bioinformatics summary. Chem. Biol. Interact., 178, 99-109
    • (2009) Chem. Biol. Interact , vol.178 , pp. 99-109
    • Bray, J.E.1    Marsden, B.D.2    Oppermann, U.3
  • 71
    • 0027184481 scopus 로고
    • A general two-metal-ion mechanism for catalytic RNA
    • Steitz, T.A. and Steitz, J.A. (1993) A general two-metal-ion mechanism for catalytic RNA. Proc. Natl Acad. Sci. USA, 90, 6498-6502
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6498-6502
    • Steitz, T.A.1    Steitz, J.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.