메뉴 건너뛰기




Volumn 11, Issue 3, 2016, Pages 575-582

Structural Chemistry of Human RNA Methyltransferases

Author keywords

[No Author keywords available]

Indexed keywords

RNA METHYLTRANSFERASE; TRANSFER RNA METHYLTRANSFERASE;

EID: 84961682996     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/acschembio.5b00781     Document Type: Review
Times cited : (60)

References (44)
  • 1
    • 84924917866 scopus 로고    scopus 로고
    • RNA methyltransferases involved in 5′ cap biosynthesis
    • Byszewska, M., Smietanski, M., Purta, E., and Bujnicki, J. M. (2014) RNA methyltransferases involved in 5′ cap biosynthesis RNA Biol. 11, 1597-1607 10.1080/15476286.2015.1004955
    • (2014) RNA Biol. , vol.11 , pp. 1597-1607
    • Byszewska, M.1    Smietanski, M.2    Purta, E.3    Bujnicki, J.M.4
  • 3
    • 84922394767 scopus 로고    scopus 로고
    • Dynamic RNA modifications in posttranscriptional regulation
    • Wang, X. and He, C. (2014) Dynamic RNA modifications in posttranscriptional regulation Mol. Cell 56, 5-12 10.1016/j.molcel.2014.09.001
    • (2014) Mol. Cell , vol.56 , pp. 5-12
    • Wang, X.1    He, C.2
  • 4
    • 77958519530 scopus 로고    scopus 로고
    • Enzymology of RNA cap synthesis
    • Ghosh, A. and Lima, C. D. (2010) Enzymology of RNA cap synthesis Wiley Interdiscip Rev. RNA 1, 152-172 10.1002/wrna.19
    • (2010) Wiley Interdiscip Rev. RNA , vol.1 , pp. 152-172
    • Ghosh, A.1    Lima, C.D.2
  • 5
    • 81355150889 scopus 로고    scopus 로고
    • RAM/Fam103a1 is required for mRNA cap methylation
    • Gonatopoulos-Pournatzis, T., Dunn, S., Bounds, R., and Cowling, V. H. (2011) RAM/Fam103a1 is required for mRNA cap methylation Mol. Cell 44, 585-596 10.1016/j.molcel.2011.08.041
    • (2011) Mol. Cell , vol.44 , pp. 585-596
    • Gonatopoulos-Pournatzis, T.1    Dunn, S.2    Bounds, R.3    Cowling, V.H.4
  • 7
    • 77958508457 scopus 로고    scopus 로고
    • Characterization of hMTr1, a human Cap1 2′-O-ribose methyltransferase
    • Belanger, F., Stepinski, J., Darzynkiewicz, E., and Pelletier, J. (2010) Characterization of hMTr1, a human Cap1 2′-O-ribose methyltransferase J. Biol. Chem. 285, 33037-33044 10.1074/jbc.M110.155283
    • (2010) J. Biol. Chem. , vol.285 , pp. 33037-33044
    • Belanger, F.1    Stepinski, J.2    Darzynkiewicz, E.3    Pelletier, J.4
  • 8
    • 67651159060 scopus 로고    scopus 로고
    • Structural basis for m7G-cap hypermethylation of small nuclear, small nucleolar and telomerase RNA by the dimethyltransferase TGS1
    • Monecke, T., Dickmanns, A., and Ficner, R. (2009) Structural basis for m7G-cap hypermethylation of small nuclear, small nucleolar and telomerase RNA by the dimethyltransferase TGS1 Nucleic Acids Res. 37, 3865-3877 10.1093/nar/gkp249
    • (2009) Nucleic Acids Res. , vol.37 , pp. 3865-3877
    • Monecke, T.1    Dickmanns, A.2    Ficner, R.3
  • 10
    • 84867553154 scopus 로고    scopus 로고
    • Human RNA methyltransferase BCDIN3D regulates microRNA processing
    • Xhemalce, B., Robson, S. C., and Kouzarides, T. (2012) Human RNA methyltransferase BCDIN3D regulates microRNA processing Cell 151, 278-288 10.1016/j.cell.2012.08.041
    • (2012) Cell , vol.151 , pp. 278-288
    • Xhemalce, B.1    Robson, S.C.2    Kouzarides, T.3
  • 11
    • 34548366485 scopus 로고    scopus 로고
    • The mouse homolog of HEN1 is a potential methylase for Piwi-interacting RNAs
    • Kirino, Y. and Mourelatos, Z. (2007) The mouse homolog of HEN1 is a potential methylase for Piwi-interacting RNAs RNA 13, 1397-1401 10.1261/rna.659307
    • (2007) RNA , vol.13 , pp. 1397-1401
    • Kirino, Y.1    Mourelatos, Z.2
  • 12
    • 84919836468 scopus 로고    scopus 로고
    • RNA epigenetics
    • Liu, N. and Pan, T. (2015) RNA epigenetics Transl Res. 165, 28-35 10.1016/j.trsl.2014.04.003
    • (2015) Transl Res. , vol.165 , pp. 28-35
    • Liu, N.1    Pan, T.2
  • 13
    • 84893310526 scopus 로고    scopus 로고
    • N6-methyladenosine modification destabilizes developmental regulators in embryonic stem cells
    • Wang, Y., Li, Y., Toth, J. I., Petroski, M. D., Zhang, Z., and Zhao, J. C. (2014) N6-methyladenosine modification destabilizes developmental regulators in embryonic stem cells Nat. Cell Biol. 16, 191-198 10.1038/ncb2902
    • (2014) Nat. Cell Biol. , vol.16 , pp. 191-198
    • Wang, Y.1    Li, Y.2    Toth, J.I.3    Petroski, M.D.4    Zhang, Z.5    Zhao, J.C.6
  • 16
    • 84930621650 scopus 로고    scopus 로고
    • N(6)-methyladenosine Modulates Messenger RNA Translation Efficiency
    • Wang, X., Zhao, B. S., Roundtree, I. A., Lu, Z., Han, D., Ma, H., Weng, X., Chen, K., Shi, H., and He, C. (2015) N(6)-methyladenosine Modulates Messenger RNA Translation Efficiency Cell 161, 1388-1399 10.1016/j.cell.2015.05.014
    • (2015) Cell , vol.161 , pp. 1388-1399
    • Wang, X.1    Zhao, B.S.2    Roundtree, I.A.3    Lu, Z.4    Han, D.5    Ma, H.6    Weng, X.7    Chen, K.8    Shi, H.9    He, C.10
  • 18
    • 84924072927 scopus 로고    scopus 로고
    • N(6)-methyladenosine-dependent RNA structural switches regulate RNA-protein interactions
    • Liu, N., Dai, Q., Zheng, G., He, C., Parisien, M., and Pan, T. (2015) N(6)-methyladenosine-dependent RNA structural switches regulate RNA-protein interactions Nature 518, 560-564 10.1038/nature14234
    • (2015) Nature , vol.518 , pp. 560-564
    • Liu, N.1    Dai, Q.2    Zheng, G.3    He, C.4    Parisien, M.5    Pan, T.6
  • 20
    • 38549164687 scopus 로고    scopus 로고
    • The 3D rRNA modification maps database: With interactive tools for ribosome analysis
    • Piekna-Przybylska, D., Decatur, W. A., and Fournier, M. J. (2008) The 3D rRNA modification maps database: with interactive tools for ribosome analysis Nucleic Acids Res. 36, D178-183 10.1093/nar/gkm855
    • (2008) Nucleic Acids Res. , vol.36 , pp. D178-D183
    • Piekna-Przybylska, D.1    Decatur, W.A.2    Fournier, M.J.3
  • 21
    • 0037125235 scopus 로고    scopus 로고
    • Modification of rRNA as a 'quality control mechanism' in ribosome biogenesis
    • Song, X. and Nazar, R. N. (2002) Modification of rRNA as a 'quality control mechanism' in ribosome biogenesis FEBS Lett. 523, 182-186 10.1016/S0014-5793(02)02986-1
    • (2002) FEBS Lett. , vol.523 , pp. 182-186
    • Song, X.1    Nazar, R.N.2
  • 22
    • 0036629250 scopus 로고    scopus 로고
    • RRNA modifications and ribosome function
    • Decatur, W. A. and Fournier, M. J. (2002) rRNA modifications and ribosome function Trends Biochem. Sci. 27, 344-351 10.1016/S0968-0004(02)02109-6
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 344-351
    • Decatur, W.A.1    Fournier, M.J.2
  • 23
    • 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 10.1093/nar/gkh185
    • (2004) Nucleic Acids Res. , vol.32 , pp. 223-238
    • Agris, P.F.1
  • 24
    • 84870152928 scopus 로고    scopus 로고
    • Biosynthesis and function of posttranscriptional modifications of transfer RNAs
    • El Yacoubi, B., Bailly, M., and de Crecy-Lagard, V. (2012) Biosynthesis and function of posttranscriptional modifications of transfer RNAs Annu. Rev. Genet. 46, 69-95 10.1146/annurev-genet-110711-155641
    • (2012) Annu. Rev. Genet. , vol.46 , pp. 69-95
    • El Yacoubi, B.1    Bailly, M.2    De Crecy-Lagard, V.3
  • 25
    • 84877088375 scopus 로고    scopus 로고
    • Transfer RNA post-transcriptional processing, turnover, and subcellular dynamics in the yeast Saccharomyces cerevisiae
    • Hopper, A. K. (2013) Transfer RNA post-transcriptional processing, turnover, and subcellular dynamics in the yeast Saccharomyces cerevisiae Genetics 194, 43-67 10.1534/genetics.112.147470
    • (2013) Genetics , vol.194 , pp. 43-67
    • Hopper, A.K.1
  • 27
    • 77649229290 scopus 로고    scopus 로고
    • Novel inhibitors of dengue virus methyltransferase: Discovery by in vitro-driven virtual screening on a desktop computer grid
    • Podvinec, M., Lim, S. P., Schmidt, T., Scarsi, M., Wen, D., Sonntag, L. S., Sanschagrin, P., Shenkin, P. S., and Schwede, T. (2010) Novel inhibitors of dengue virus methyltransferase: discovery by in vitro-driven virtual screening on a desktop computer grid J. Med. Chem. 53, 1483-1495 10.1021/jm900776m
    • (2010) J. Med. Chem. , vol.53 , pp. 1483-1495
    • Podvinec, M.1    Lim, S.P.2    Schmidt, T.3    Scarsi, M.4    Wen, D.5    Sonntag, L.S.6    Sanschagrin, P.7    Shenkin, P.S.8    Schwede, T.9
  • 30
    • 33646552414 scopus 로고    scopus 로고
    • The RNA methyltransferase Misu (NSun2) mediates Myc-induced proliferation and is upregulated in tumors
    • Frye, M. and Watt, F. M. (2006) The RNA methyltransferase Misu (NSun2) mediates Myc-induced proliferation and is upregulated in tumors Curr. Biol. 16, 971-981 10.1016/j.cub.2006.04.027
    • (2006) Curr. Biol. , vol.16 , pp. 971-981
    • Frye, M.1    Watt, F.M.2
  • 33
    • 84899524789 scopus 로고    scopus 로고
    • Long noncoding RNA ANRIL indicates a poor prognosis of gastric cancer and promotes tumor growth by epigenetically silencing of miR-99a/miR-449a
    • Zhang, E. B., Kong, R., Yin, D. D., You, L. H., Sun, M., Han, L., Xu, T. P., Xia, R., Yang, J. S., De, W., and Chen, J. (2014) Long noncoding RNA ANRIL indicates a poor prognosis of gastric cancer and promotes tumor growth by epigenetically silencing of miR-99a/miR-449a Oncotarget 5, 2276-2292 10.18632/oncotarget.1902
    • (2014) Oncotarget , vol.5 , pp. 2276-2292
    • Zhang, E.B.1    Kong, R.2    Yin, D.D.3    You, L.H.4    Sun, M.5    Han, L.6    Xu, T.P.7    Xia, R.8    Yang, J.S.9    De, W.10    Chen, J.11
  • 34
    • 84957922104 scopus 로고    scopus 로고
    • Long noncoding RNAs in cancer: From function to translation
    • Sahu, A., Singhal, U., and Chinnaiyan, A. (2015) Long noncoding RNAs in cancer: from function to translation Trends in Cancer 1, 93-109 10.1016/j.trecan.2015.08.010
    • (2015) Trends in Cancer , vol.1 , pp. 93-109
    • Sahu, A.1    Singhal, U.2    Chinnaiyan, A.3
  • 36
    • 0027536869 scopus 로고
    • Temperature-sensitive mutations demonstrate roles for yeast fibrillarin in pre-rRNA processing, pre-rRNA methylation, and ribosome assembly
    • Tollervey, D., Lehtonen, H., Jansen, R., Kern, H., and Hurt, E. C. (1993) Temperature-sensitive mutations demonstrate roles for yeast fibrillarin in pre-rRNA processing, pre-rRNA methylation, and ribosome assembly Cell 72, 443-457 10.1016/0092-8674(93)90120-F
    • (1993) Cell , vol.72 , pp. 443-457
    • Tollervey, D.1    Lehtonen, H.2    Jansen, R.3    Kern, H.4    Hurt, E.C.5
  • 37
    • 84868534809 scopus 로고    scopus 로고
    • Structure of the essential MTERF4:NSUN4 protein complex reveals how an MTERF protein collaborates to facilitate rRNA modification
    • Yakubovskaya, E., Guja, K. E., Mejia, E., Castano, S., Hambardjieva, E., Choi, W. S., and Garcia-Diaz, M. (2012) Structure of the essential MTERF4:NSUN4 protein complex reveals how an MTERF protein collaborates to facilitate rRNA modification Structure 20, 1940-1947 10.1016/j.str.2012.08.027
    • (2012) Structure , vol.20 , pp. 1940-1947
    • Yakubovskaya, E.1    Guja, K.E.2    Mejia, E.3    Castano, S.4    Hambardjieva, E.5    Choi, W.S.6    Garcia-Diaz, M.7
  • 38
    • 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 Bioinf. 8, 73 10.1186/1471-2105-8-73
    • (2007) BMC Bioinf. , vol.8 , pp. 73
    • Tkaczuk, K.L.1    Dunin-Horkawicz, S.2    Purta, E.3    Bujnicki, J.M.4
  • 39
    • 84938702956 scopus 로고    scopus 로고
    • Structural basis for methyl-donor-dependent and sequence-specific binding to tRNA substrates by knotted methyltransferase TrmD
    • Ito, T., Masuda, I., Yoshida, K., Goto-Ito, S., Sekine, S., Suh, S. W., Hou, Y. M., and Yokoyama, S. (2015) Structural basis for methyl-donor-dependent and sequence-specific binding to tRNA substrates by knotted methyltransferase TrmD Proc. Natl. Acad. Sci. U. S. A. 112, E4197-4205 10.1073/pnas.1422981112
    • (2015) Proc. Natl. Acad. Sci. U. S. A. , vol.112 , pp. E4197-E4205
    • Ito, T.1    Masuda, I.2    Yoshida, K.3    Goto-Ito, S.4    Sekine, S.5    Suh, S.W.6    Hou, Y.M.7    Yokoyama, S.8
  • 40
    • 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 10.1093/nar/gkq1131
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.