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Volumn 8, Issue 7, 2009, Pages 1516-1526

Multiple motif scanning to identify methyltransferases from the yeast proteome

Author keywords

[No Author keywords available]

Indexed keywords

METHYLTRANSFERASE; PROTEOME;

EID: 70449498766     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M900025-MCP200     Document Type: Article
Times cited : (60)

References (30)
  • 2
    • 0031569882 scopus 로고    scopus 로고
    • Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine
    • Djordjevic, S., and Stock, A. M. (1997) Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine. Structure 5, 545-558 (Pubitemid 27191230)
    • (1997) Structure , vol.5 , Issue.4 , pp. 545-558
    • Djordjevic, S.1    Stock, A.M.2
  • 3
    • 0036917889 scopus 로고    scopus 로고
    • SAM (dependent) I AM: The S-adenosylmethionine-dependent methyltransferase fold
    • Martin, J. L., and McMillan, F. M. (2002) SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold. Curr. Opin. Struct. Biol. 12, 783-793
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 783-793
    • Martin, J.L.1    McMillan, F.M.2
  • 4
    • 0028956315 scopus 로고
    • Universal catalytic domain structure of AdoMet-dependent methyltransferases
    • Schluckebier, G., O'Gara, M., Saenger, W., and Cheng, X. (1995) Universal catalytic domain structure of AdoMet-dependent methyltransferases. J. Mol. Biol. 247, 16-20
    • (1995) J. Mol. Biol. , vol.247 , pp. 16-20
    • Schluckebier, G.1    O'Gara, M.2    Saenger, W.3    Cheng, X.4
  • 5
    • 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
  • 6
    • 1642284876 scopus 로고    scopus 로고
    • Automated identification of putative methyltransferases from genomic open reading frames
    • Katz, J. E., Dlakić, M., and Clarke, S. (2003) Automated identification of putative methyltransferases from genomic open reading frames. Mol. Cell. Proteomics 2, 525-540
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 525-540
    • Katz, J.E.1    Dlakić, M.2    Clarke, S.3
  • 7
    • 0028179364 scopus 로고
    • Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes
    • Kagan, R. M., and Clarke, S. (1994) Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes. Arch. Biochem. Biophys. 310, 417-427
    • (1994) Arch. Biochem. Biophys. , vol.310 , pp. 417-427
    • Kagan, R.M.1    Clarke, S.2
  • 8
    • 0033534476 scopus 로고    scopus 로고
    • S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase
    • Niewmierzycka, A., and Clarke, S. (1999) S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase. J. Biol. Chem. 274, 814-824
    • (1999) J. Biol. Chem. , vol.274 , pp. 814-824
    • Niewmierzycka, A.1    Clarke, S.2
  • 9
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • DOI 10.1093/nar/gki408
    • Söding, J., Biegert, A., and Lupas, A. N. (2005) The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res. 33, W244-248 (Pubitemid 44529917)
    • (2005) Nucleic Acids Research , vol.33 , Issue.WEB. SERV. ISS
    • Soding, J.1    Biegert, A.2    Lupas, A.N.3
  • 10
    • 3042818018 scopus 로고    scopus 로고
    • The international protein index: An integrated database for proteomics experiments
    • DOI 10.1002/pmic.200300721
    • Kersey, P. J., Duarte, J., Williams, A., Karavidopoulou, Y., Bimey, E., and Apweiler, R. (2004) The International Protein Index: an integrated database for proteomics experiments. Proteomics 4, 1985-1988 (Pubitemid 38880363)
    • (2004) Proteomics , vol.4 , Issue.7 , pp. 1985-1988
    • Kersey, P.J.1    Duarte, J.2    Williams, A.3    Karavidopoulou, Y.4    Birney, E.5    Apweiler, R.6
  • 12
    • 0030612472 scopus 로고    scopus 로고
    • Structure of Pvull DNA-(cytosine N4) methyltransferase, an example of domain permutation and protein fold assignment
    • DOI 10.1093/nar/25.14.2702
    • Gong, W., O'Gara, M., Blumenthal, R. M., and Cheng, X. (1997) Structure of Pvu II DNA-(cytosine N4) methyltransferase, an example of domain permutation and protein fold assignment. Nucleic Acids Res. 25, 2702-2715 (Pubitemid 27299782)
    • (1997) Nucleic Acids Research , vol.25 , Issue.14 , pp. 2702-2715
    • Gong, W.1    O'Gara, M.2    Blumenthal, R.M.3    Cheng, X.4
  • 13
    • 0038629269 scopus 로고    scopus 로고
    • Structures along the catalytic pathway of PrmC/HemK, an N5-glutamine AdoMet-dependent methyltransferase
    • Schubert, H. L., Phillips, J. D., and Hill, C. P. (2003) Structures along the catalytic pathway of PrmC/HemK, an N5-glutamine AdoMet-dependent methyltransferase. Biochemistry 42, 5592-5599
    • (2003) Biochemistry , vol.42 , pp. 5592-5599
    • Schubert, H.L.1    Phillips, J.D.2    Hill, C.P.3
  • 14
    • 34547829268 scopus 로고    scopus 로고
    • Functional specialization of domains tandemly duplicated within 16S rRNA methyltransferase RsmC
    • DOI 10.1093/nar/gkm411
    • Sunita, S., Purta, E., Durawa, M., Tkaczuk, K. L., Swaathi, J., Bujnicki, J. M., and Sivaraman, J. (2007) Functional specialization of domains tandemly duplicated within 16S rRNA methyltransferase RsmC. Nucleic Acids Res. 35, 4264-4274 (Pubitemid 47244581)
    • (2007) Nucleic Acids Research , vol.35 , Issue.13 , pp. 4264-4274
    • Sunita, S.1    Purta, E.2    Durawa, M.3    Tkaczuk, K.L.4    Swaathi, J.5    Bujnicki, J.M.6    Sivaraman, J.7
  • 15
    • 3042513877 scopus 로고    scopus 로고
    • Structural characterization and comparative phylogenetic analysis of Escherichia coli HemK, a protein (N5)-glutamine methyltransferase
    • Yang, Z., Shipman, L., Zhang, M., Anton, B. P., Roberts, R. J., and Cheng, X. (2004) Structural characterization and comparative phylogenetic analysis of Escherichia coli HemK, a protein (N5)-glutamine methyltransferase. J. Mol. Biol. 340, 695-706
    • (2004) J. Mol. Biol. , vol.340 , pp. 695-706
    • Yang, Z.1    Shipman, L.2    Zhang, M.3    Anton, B.P.4    Roberts, R.J.5    Cheng, X.6
  • 16
    • 0028010888 scopus 로고
    • Hhal methyltransferase flips its target base out of the DNA helix
    • DOI 10.1016/0092-8674(94)90342-5
    • Klimasauskas, S., Kumar, S., Roberts, R. J., and Cheng, X. (1994) Hhal methyltransferase flips its target base out of the DNA helix. Cell 76, 357-369 (Pubitemid 24046697)
    • (1994) Cell , vol.76 , Issue.2 , pp. 357-369
    • Klimasauskas, S.1    Kumar, S.2    Roberts, R.J.3    Cheng, X.4
  • 17
    • 0034679591 scopus 로고    scopus 로고
    • Crystal structure of the conserved core of protein arginine methyltransferase PRMT3
    • Zhang, X., Zhou, L., and Cheng, X. (2000) Crystal structure of the conserved core of protein arginine methyltransferase PRMT3. EMBO J. 19, 3509-3519 (Pubitemid 30462110)
    • (2000) EMBO Journal , vol.19 , Issue.14 , pp. 3509-3519
    • Zhang, X.1    Zhou, L.2    Cheng, X.3
  • 18
    • 33747823564 scopus 로고    scopus 로고
    • MEME: Discovering and analyzing DNA and protein sequence motifs
    • DOI 10.1093/nar/gkl198
    • Bailey, T. L., Williams, N., Misleh, C., and Li, W. W. (2006) MEME: discovering and analyzing DNA and protein sequence motifs. Nucleic Acids Res. 34, W369-373 (Pubitemid 44529795)
    • (2006) Nucleic Acids Research , vol.34 , Issue.WEB. SERV. ISS
    • Bailey, T.L.1    Williams, N.2    Misleh, C.3    Li, W.W.4
  • 19
    • 0031877016 scopus 로고    scopus 로고
    • Combining evidence using p-values: Application to sequence homology searches
    • Bailey, T. L., and Gribskov, M. (1998) Combining evidence using p-values: application to sequence homology searches. Bioinformatics 14, 48-54
    • (1998) Bioinformatics , vol.14 , pp. 48-54
    • Bailey, T.L.1    Gribskov, M.2
  • 21
    • 0027497266 scopus 로고
    • The Escherichia coli cysG gene encodes the multifunctional protein, siroheme synthase
    • DOI 10.1016/0014-5793(93)80438-Z
    • Spencer, J. B., Stolowich, N. J., Roessner, C. A., and Scott, A. I. (1993) The Escherichia coli cysG gene encodes the multifunctional protein, siroheme synthase. FEBS Lett. 335, 57-60 (Pubitemid 23347735)
    • (1993) FEBS Letters , vol.335 , Issue.1 , pp. 57-60
    • Spencer, J.B.1    Stolowich, N.J.2    Roessner, C.A.3    Scott, A.I.4
  • 22
    • 0031039128 scopus 로고    scopus 로고
    • Spermidine biosynthesis in Saccharomyces cerevisae: Polyamine requirement of a null mutant of the SPE3 gene (spermidine synthase)
    • DOI 10.1016/S0378-1119(96)00660-9, PII S0378111996006609
    • Hamasaki-Katagiri, N., Tabor, C. W., and Tabor, H. (1997) Spermidine biosynthesis in Saccharomyces cerevisiae: polyamine requirement of a null mutant of the SPE3 gene (spermidine synthase). Gene 187, 35-43 (Pubitemid 27110432)
    • (1997) Gene , vol.187 , Issue.1 , pp. 35-43
    • Hamasaki-Katagiri, N.1    Tabor, C.W.2    Tabor, H.3
  • 23
    • 18344418431 scopus 로고    scopus 로고
    • Spermine is not essential for growth of Saccharomyces cerevisiae: Identification of the SPE4 gene (spermine synthase) and characterization of a spe4 deletion mutant
    • DOI 10.1016/S0378-1119(98)00027-4, PII S0378111998000274
    • Hamasaki-Katagiri, N., Katagiri, Y., Tabor, C. W., and Tabor, H. (1998) Spermine is not essential for growth of Saccharomyces cerevisiae: identification of the SPE4 gene (spermine synthase) and characterization of a spe4 deletion mutant. Gene 210, 195-201 (Pubitemid 28178414)
    • (1998) Gene , vol.210 , Issue.2 , pp. 195-201
    • Hamasaki-Katagiri, N.1    Katagiri, Y.2    Tabor, C.W.3    Tabor, H.4
  • 24
    • 33646778150 scopus 로고    scopus 로고
    • Biosynthesis of wybutosine, a hyper-modified nucleoside in eukaryotic phenylalanine tRNA
    • DOI 10.1038/sj.emboj.7601105, PII 7601105
    • Noma, A., Kirino, Y., Ikeuchi, Y., and Suzuki, T. (2006) Biosynthesis of wybutosine, a hyper-modified nucleoside in eukaryotic phenylalanine tRNA. EMBO J. 25, 2142-2154 (Pubitemid 43756230)
    • (2006) EMBO Journal , vol.25 , Issue.10 , pp. 2142-2154
    • Noma, A.1    Kirino, Y.2    Ikeuchi, Y.3    Suzuki, T.4
  • 25
    • 58149287683 scopus 로고    scopus 로고
    • In silico analysis of methyltransferases domains involved in biosynthesis of secondary metabolites
    • Ansari, M. Z., Sharma, J., Gokhale, R. S., and Mohanty, D. (2008) In silico analysis of methyltransferases domains involved in biosynthesis of secondary metabolites. BMC Bioinformatics 9, 454
    • (2008) BMC Bioinformatics , vol.9 , pp. 454
    • Ansari, M.Z.1    Sharma, J.2    Gokhale, R.S.3    Mohanty, D.4
  • 26
    • 46749130169 scopus 로고    scopus 로고
    • Identification of a novel N-terminal hydrophobic sequence that targets proteins to lipid droplets
    • DOI 10.1242/jcs.012013
    • Zehmer, J. K., Bartz, R., Liu, P., and Anderson, R. G. (2008) Identification of a novel N-terminal hydrophobic sequence that targets proteins to lipid droplets. J. Cell Sci. 121, 1852-1860 (Pubitemid 351943378)
    • (2008) Journal of Cell Science , vol.121 , Issue.11 , pp. 1852-1860
    • Zehmer, J.K.1    Bartz, R.2    Liu, P.3    Anderson, R.G.W.4
  • 27
    • 0345060040 scopus 로고    scopus 로고
    • Novel methyltransferase for modified uridine residues at the wobble position of tRNA
    • Kalhor, H. R., and Clarke, S. (2003) Novel methyltransferase for modified uridine residues at the wobble position of tRNA. Mol. Cell. Biol. 23, 9283-9292
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 9283-9292
    • Kalhor, H.R.1    Clarke, S.2
  • 28
    • 51149098989 scopus 로고    scopus 로고
    • The crystal structure of mammalian fatty acid synthase
    • Maier, T., Leibundgut, M., and Ban, N. (2008) The crystal structure of mammalian fatty acid synthase. Science 321, 1315-1322
    • (2008) Science , vol.321 , pp. 1315-1322
    • Maier, T.1    Leibundgut, M.2    Ban, N.3
  • 29
    • 5644261221 scopus 로고    scopus 로고
    • Structure of the conserved core of the yeast Dot1p, a nucleosomal histone H3 lysine 79 methyltransferase
    • Sawada, K., Yang, Z., Horton, J. R., Collins, R. E., Zhang, X., and Cheng, X. (2004) Structure of the conserved core of the yeast Dot1p, a nucleosomal histone H3 lysine 79 methyltransferase. J. Biol. Chem. 279, 43296-43306
    • (2004) J. Biol. Chem. , vol.279 , pp. 43296-43306
    • Sawada, K.1    Yang, Z.2    Horton, J.R.3    Collins, R.E.4    Zhang, X.5    Cheng, X.6


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