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Volumn 2, Issue 6, 2010, Pages 366-374

Crystal structure of Mj1640/DUF358 protein reveals a putative SPOUT-class RNA methyltransferase

Author keywords

DUF358; SPOUT class RNA methyltransferase; X ray structure

Indexed keywords

ARCHAEAL PROTEIN; METHYLTRANSFERASE; RNA; S ADENOSYLMETHIONINE;

EID: 79951483622     PISSN: 16742788     EISSN: 17594685     Source Type: Journal    
DOI: 10.1093/jmcb/mjq034     Document Type: Article
Times cited : (11)

References (20)
  • 1
    • 0037526102 scopus 로고    scopus 로고
    • 1G37)methyltransferase: Insights into tRNA recognition
    • DOI 10.1093/emboj/cdg269
    • 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. (Pubitemid 36712357)
    • (2003) EMBO Journal , vol.22 , Issue.11 , 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
  • 2
    • 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. (Pubitemid 33121215)
    • (2002) Journal of Molecular Microbiology and Biotechnology , vol.4 , Issue.1 , pp. 71-75
    • Anantharam, V.1    Koonin, E.V.2    Aravind, L.3
  • 3
    • 33344476204 scopus 로고    scopus 로고
    • Identification and characterization of RsmE, the founding member of a new RNA base methyltransferase family
    • DOI 10.1261/rna.2283106
    • Basturea, G. N., Rudd, K. E., and Deutscher, M. P. (2006). Identification and characterization of RsmE, the founding member of a new RNA base methyltransferase family. RNA 12, 426-434. (Pubitemid 43290870)
    • (2006) RNA , vol.12 , Issue.3 , pp. 426-434
    • Basturea, G.N.1    Rudd, K.E.2    Deutscher, M.P.3
  • 4
    • 34748874591 scopus 로고    scopus 로고
    • Distinct Determinants of tRNA Recognition by the TrmD and Trm5 Methyl Transferases
    • DOI 10.1016/j.jmb.2007.08.010, PII S0022283607010819
    • 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. (Pubitemid 47488397)
    • (2007) Journal of Molecular Biology , vol.373 , Issue.3 , pp. 623-632
    • Christian, T.1    Hou, Y.-M.2
  • 5
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • DOI 10.1016/S0076-6879(97)76075-0
    • Doublié, S. (1997). Preparation of selenomethionyl proteins for phase determination. Meth. Enzymol. 276, 523-530. (Pubitemid 27085620)
    • (1997) Methods in Enzymology , vol.276 , pp. 523-530
    • Doublie, S.1
  • 7
    • 0141704142 scopus 로고    scopus 로고
    • Functional assignment based on structural analysis: Crystal structure of the yggJ protein (HI0303) of Haemophilus influenzae reveals an RNA methyltransferase with a deep trefoil knot
    • DOI 10.1002/prot.10510
    • Forouhar, F., Shen, J., Xiao, R., Acton, T. B., Montelione, G. T., and Tong, L. (2003). Functional assignment based on structural analysis: crystal structure of the yggJ protein (HI0303) of Haemophilus influenzae reveals an RNA methyltransferase with a deep trefoil knot. Proteins 53, 329-332. (Pubitemid 37193829)
    • (2003) Proteins: Structure, Function and Genetics , vol.53 , Issue.2 , pp. 329-332
    • Forouhar, F.1    Shen, J.2    Xiao, R.3    Acton, T.B.4    Montelione, G.T.5    Tong, L.6
  • 8
    • 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
  • 9
    • 39149096592 scopus 로고    scopus 로고
    • The yeast ribosome synthesis factor Emg1 is a novel member of the superfamily of alpha/beta knot fold methyltransferases
    • DOI 10.1093/nar/gkm1074
    • Leulliot, N., Bohnsack, M. T., Graille, M., Tollervey, D., and Van Tilbeurgh, H. (2008). The yeast ribosome synthesis factor Emg1 is a novel member of the superfamily of alpha/beta knot fold methyltransferases. Nucleic Acids Res. 36, 629-639. (Pubitemid 351255435)
    • (2008) Nucleic Acids Research , vol.36 , Issue.2 , pp. 629-639
    • Leulliot, N.1    Bohnsack, M.T.2    Graille, M.3    Tollervey, D.4    Van tilbeurgh, H.5
  • 10
    • 33644927702 scopus 로고    scopus 로고
    • Pumping RNA: Nuclear bodybuilding along the RNP pipeline
    • Matera, A. G., and Shpargel, K. B. (2006). Pumping RNA: nuclear bodybuilding along the RNP pipeline. Curr. Opin. Cell Biol. 18, 317-324.
    • (2006) Curr. Opin. Cell. Biol. , vol.18 , pp. 317-324
    • Matera, A.G.1    Shpargel, K.B.2
  • 11
    • 55849109584 scopus 로고    scopus 로고
    • The epigenetics of rRNA genes: From molecular to chromosome biology
    • McStay, B., and Grummt, I. (2008). The epigenetics of rRNA genes: from molecular to chromosome biology. Annu. Rev. Cell Dev. Biol. 24, 131-157.
    • (2008) Annu. Rev. Cell. Dev. Biol. , vol.24 , pp. 131-157
    • McStay, B.1    Grummt, I.2
  • 13
    • 1842607227 scopus 로고    scopus 로고
    • Deep knot structure for construction of active site and cofactor binding site of tRNA modification enzyme
    • DOI 10.1016/j.str.2004.03.003, PII S0969212604000838
    • 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. (Pubitemid 38447162)
    • (2004) Structure , 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
  • 14
    • 77950589659 scopus 로고    scopus 로고
    • Flexible recognition of the tRNA G18 methylation target site by TrmH methyltransferase through first binding and induced fit processes
    • Ochi, A., Makabe, K., Kuwajima, K., and Hori, H. (2010). Flexible recognition of the tRNA G18 methylation target site by TrmH methyltransferase through first binding and induced fit processes. J. Biol. Chem. 285, 9018-9029.
    • (2010) J. Biol. Chem. , vol.285 , pp. 9018-9029
    • Ochi, A.1    Makabe, K.2    Kuwajima, K.3    Hori, H.4
  • 15
    • 52949120327 scopus 로고    scopus 로고
    • YbeA is the m3Psi methyltransferase RlmH that targets nucleotide 1915 in 23S rRNA
    • Purta, E., Kaminska, K. H., Kasprzak, J. M., Bujnicki, J. M., and Douthwaite, S. (2008). YbeA is the m3Psi methyltransferase RlmH that targets nucleotide 1915 in 23S rRNA. RNA 14, 2234-2244.
    • (2008) RNA , vol.14 , pp. 2234-2244
    • Purta, E.1    Kaminska, K.H.2    Kasprzak, J.M.3    Bujnicki, J.M.4    Douthwaite, S.5
  • 16
    • 41149170790 scopus 로고    scopus 로고
    • The crystal structure of Nep1 reveals an extended SPOUT-class methyltransferase fold and a pre-organized SAM-binding site
    • DOI 10.1093/nar/gkm1172
    • Taylor, A. B., Meyer, B., Leal, B. Z., Kötter, P., Schirf, V., Demeler, B., Hart, P. J., Entian, K. D., and Wöhnert, J. (2008). The crystal structure of Nep1 reveals an extended SPOUT-class methyltransferase fold and a pre-organized SAM-binding site. Nucleic Acids Res. 36, 1542-1554. (Pubitemid 351426107)
    • (2008) Nucleic Acids Research , vol.36 , Issue.5 , pp. 1542-1554
    • Taylor, A.B.1    Meyer, B.2    Leal, B.Z.3    Kotter, P.4    Schirf, V.5    Demeler, B.6    Hart, P.J.7    Entian, K.-D.8    Wohnert, J.9
  • 17
    • 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, 73-103.
    • (2007) BMC Bioinformatics , vol.8 , pp. 73-103
    • Tkaczuk, K.L.1    Dunin-Horkawicz, S.2    Purta, E.3    Bujnicki, J.M.4
  • 18
    • 15444370839 scopus 로고    scopus 로고
    • Roles of conserved amino acid sequence motifs in the SpoU (TrmH) RNA methyltransferase family
    • DOI 10.1074/jbc.M411209200
    • Watanabe, K., Nureki, O., Fukai, S., Ishii, R., Okamoto, H., Yokoyama, S., Endo, Y., and Hori, H. (2005). Roles of conserved amino acid sequence motifs in the SpoU (TrmH) RNA methyltransferase family. J. Biol. Chem. 280, 10368-10377. (Pubitemid 40395893)
    • (2005) Journal of Biological Chemistry , 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
  • 19
    • 33845919828 scopus 로고    scopus 로고
    • Functional categorization of the conserved basic amino acid residues in TrmH (tRNA (Gm18) methyltansferase) enzymes
    • DOI 10.1074/jbc.M606141200
    • Watanabe, K., Nureki, O., Fukai, S., Endo, Y., and Hori, H. (2006). Functional categorization of the conserved basic amino acid residues in TrmH (tRNA (Gm18) methyltransferase) enzymes. J. Biol. Chem. 281, 34630-34639. (Pubitemid 46036669)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.45 , pp. 34630-34639
    • Watanabe, K.1    Nureki, O.2    Fukai, S.3    Endo, Y.4    Hori, H.5
  • 20
    • 77952314717 scopus 로고    scopus 로고
    • The ribosome assembly factor Nep1 responsible for Bowen-conradi syndrome is a pseudouridine-N1-specific methyltransferase
    • Wurm, J. P., Meyer, B., Bahr, U., Held, M., Frolow, O., Kötter, P., Engels, J. W., Heckel, A., Karas, M., Entian, K. D., et al. (2010). The ribosome assembly factor Nep1 responsible for Bowen-Conradi syndrome is a pseudouridine-N1-specific methyltransferase. Nucleic Acids Res. 38, 2387-2398.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 2387-2398
    • Wurm, J.P.1    Meyer, B.2    Bahr, U.3    Held, M.4    Frolow, O.5    Kötter, P.6    Engels, J.W.7    Heckel, A.8    Karas, M.9    Entian, K.D.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.