메뉴 건너뛰기




Volumn 42, Issue 22, 2014, Pages 13911-13919

Solution structure of the YTH domain in complex with N6-methyladenosine RNA: A reader of methylated RNA

Author keywords

[No Author keywords available]

Indexed keywords

6 N METHYLADENINE; 6 N METHYLADENOSINE; ADENOSINE; GUANINE; N(6)-METHYLADENOSINE; NERVE PROTEIN; PROTEIN BINDING; RNA; RNA BINDING PROTEIN; YT521 PROTEIN, RAT;

EID: 84927593761     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gku1116     Document Type: Article
Times cited : (180)

References (42)
  • 2
    • 84898814417 scopus 로고    scopus 로고
    • Gene expression regulation mediated through reversible m6A RNA methylation
    • Fu, Y., Dominissini, D., Rechavi, G. and He, C. (2014) Gene expression regulation mediated through reversible m6A RNA methylation. Nat. Rev. Genet., 15, 293-306.
    • (2014) Nat. Rev. Genet. , vol.15 , pp. 293-306
    • Fu, Y.1    Dominissini, D.2    Rechavi, G.3    He, C.4
  • 3
    • 84899586607 scopus 로고    scopus 로고
    • The dynamic epitranscriptome: N6-methyladenosine and gene expression control
    • Meyer, K. D. and Jaffrey, S. R. (2014) The dynamic epitranscriptome: N6-methyladenosine and gene expression control. Nat. Rev. Mol. Cell. Biol, 15, 313-326.
    • (2014) Nat. Rev. Mol. Cell. Biol , vol.15 , pp. 313-326
    • Meyer, K.D.1    Jaffrey, S.R.2
  • 4
    • 42249110521 scopus 로고    scopus 로고
    • FTO: The first gene contributing to common forms of human obesity
    • Loos, R. J. and Bouchard, C. (2008) FTO: the first gene contributing to common forms of human obesity. Obes. Rev., 9, 246-250.
    • (2008) Obes. Rev. , vol.9 , pp. 246-250
    • Loos, R.J.1    Bouchard, C.2
  • 9
  • 10
    • 84862649489 scopus 로고    scopus 로고
    • Comprehensive analysis of mRNA methylation reveals enrichment in 3' UTRs and near stop codons
    • Meyer, K. D., Saletore, Y, Zumbo, P., Elemento, O., Mason, C. E. and Jaffrey, S. R. (2012) Comprehensive analysis of mRNA methylation reveals enrichment in 3' UTRs and near stop codons. Cell, 149, 1635-1646.
    • (2012) Cell , vol.149 , pp. 1635-1646
    • Meyer, K.D.1    Saletore, Y.2    Zumbo, P.3    Elemento, O.4    Mason, C.E.5    Jaffrey, S.R.6
  • 13
    • 84893310526 scopus 로고    scopus 로고
    • N (6)-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) N (6)-methyladenosine modification destabilizes developmental regulators in embryonic stem cells. Nat. Cell Biol., 16, 191-198.
    • (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
  • 14
    • 0032739144 scopus 로고    scopus 로고
    • The interaction and colocalization of Sam68 with the splicing-associated factor YT521-B in nuclear dots is regulated by the Src family kinase p59 (fyn)
    • Hartmann, A. M., Nayler, O., Schwaiger, F. W., Obermeier, A. and Stamm, S. (1999) The interaction and colocalization of Sam68 with the splicing-associated factor YT521-B in nuclear dots is regulated by the Src family kinase p59 (fyn). Mol. Biol. Cell, 10, 3909-3926.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3909-3926
    • Hartmann, A.M.1    Nayler, O.2    Schwaiger, F.W.3    Obermeier, A.4    Stamm, S.5
  • 15
    • 0031882856 scopus 로고    scopus 로고
    • Cloning of a gene, YT521, for a novel RNA splicing-related protein induced by hypoxia/reoxygenation
    • Imai, Y, Matsuo, N, Ogawa, S., Tohyama, M. and Takagi, T (1998) Cloning of a gene, YT521, for a novel RNA splicing-related protein induced by hypoxia/reoxygenation. Brain Res. Mol. Brain Res., 53, 33-40.
    • (1998) Brain Res. Mol. Brain Res. , vol.53 , pp. 33-40
    • Imai, Y.1    Matsuo, N.2    Ogawa, S.3    Tohyama, M.4    Takagi, T.5
  • 19
    • 80055028381 scopus 로고    scopus 로고
    • The fission yeast RNA binding protein Mmi1 regulates meiotic genes by controlling intron specific splicing and polyadenylation coupled RNA turnover
    • Chen, H. M., Futcher, B. and Leatherwood, J. (2011) The fission yeast RNA binding protein Mmi1 regulates meiotic genes by controlling intron specific splicing and polyadenylation coupled RNA turnover. PLoS One, 6, e26804.
    • (2011) PLoS One , vol.6 , pp. e26804
    • Chen, H.M.1    Futcher, B.2    Leatherwood, J.3
  • 20
    • 0030808350 scopus 로고    scopus 로고
    • Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy: Application to a bacteriophage lambda N-peptide/boxB RNA complex
    • Zwahlen, C, Legault, P, Vincent, S. J. F, Greenblatt, J., Konrat, R. and Kay, L. E. (1997) Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy: Application to a bacteriophage lambda N-peptide/boxB RNA complex. J. Am. Chem. Soc, 119, 6711-6721.
    • (1997) J. Am. Chem. Soc , vol.119 , pp. 6711-6721
    • Zwahlen, C.1    Legault, P.2    Vincent, S.J.F.3    Greenblatt, J.4    Konrat, R.5    Kay, L.E.6
  • 21
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann, T, Guntert, P and Wuthrich, K. (2002) Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J. Mol. Biol, 319, 209-227.
    • (2002) J. Mol. Biol , vol.319 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 22
    • 0036873589 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS
    • Herrmann, T, Guntert, P and Wuthrich, K. (2002) Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS. J. Biomol NMR, 24, 171-189.
    • (2002) J. Biomol NMR , vol.24 , pp. 171-189
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 23
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • Guntert, P (2004) Automated NMR structure calculation with CYANA. Methods Mol. Biol, 278, 353-378.
    • (2004) Methods Mol. Biol , vol.278 , pp. 353-378
    • Guntert, P.1
  • 24
    • 68349093958 scopus 로고    scopus 로고
    • TALOS plus: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • Shen, Y, Delaglio, F, Cornilescu, G. and Bax, A. (2009) TALOS plus: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J. Biomol. NMR, 44, 213-223.
    • (2009) J. Biomol. NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 26
    • 0029633186 scopus 로고
    • Amber, a package of computer-programs for applying molecular mechanics, normal-mode analysis, molecular-dynamics and free-energy calculations to simulate the structural and energetic properties of molecules
    • Pearlman, DA., Case, DA., Caldwell, J. W., Ross, W. S., Cheatham, TE., Debolt, S., Ferguson, D, Seibel, G and Kollman, P (1995) Amber, a package of computer-programs for applying molecular mechanics, normal-mode analysis, molecular-dynamics and free-energy calculations to simulate the structural and energetic properties of molecules. Comput. Phys. Commun., 91, 1-41.
    • (1995) Comput. Phys. Commun. , vol.91 , pp. 1-41
    • Pearlman, D.A.1    Case, D.A.2    Caldwell, J.W.3    Ross, W.S.4    Cheatham, T.E.5    Debolt, S.6    Ferguson, D.7    Seibel, G.8    Kollman, P.9
  • 28
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R. A., Rullmannn, J. A., MacArthur, M. W., Kaptein, R. and Thornton, J. M. (1996) AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR, 8, 477-486.
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 29
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M. and Wuthrich, K. (1996) MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graphics, 14, 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 30
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR: An automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations
    • Dolinsky, TJ., Nielsen, J. E., McCammon, J. A. and Baker, NA. (2004) PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations. Nucleic Acids Res., 32, W665-W667.
    • (2004) Nucleic Acids Res. , vol.32 , pp. W665-W667
    • Dolinsky, T.J.1    Nielsen, J.E.2    McCammon, J.A.3    Baker, N.A.4
  • 31
    • 0035964342 scopus 로고    scopus 로고
    • Electrostatics of nanosystems: Application to microtubules and the ribosome
    • Baker, NA., Sept, D., Joseph, S., Holst, M. J. and McCammon, J. A. (2001) Electrostatics of nanosystems: application to microtubules and the ribosome. Proc. Natl. Acad. Sci. USA, 98, 10037-10041.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10037-10041
    • Baker, N.A.1    Sept, D.2    Joseph, S.3    Holst, M.J.4    McCammon, J.A.5
  • 32
    • 34548180540 scopus 로고    scopus 로고
    • Scaffold-independent analysis of RNA-protein interactions: The Nova-1 KH3-RNA complex
    • Beuth, B., Garcia-Mayoral, M. F, Taylor, I. A. and Ramos, A. (2007) Scaffold-independent analysis of RNA-protein interactions: the Nova-1 KH3-RNA complex. J. Am. Chem. Soc, 129, 10205-10210.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 10205-10210
    • Beuth, B.1    Garcia-Mayoral, M.F.2    Taylor, I.A.3    Ramos, A.4
  • 33
    • 65449188232 scopus 로고    scopus 로고
    • Jalview Version 2 - A multiple sequence alignment editor and analysis workbench
    • Waterhouse, A. M., Procter, J. B., Martin, D. M., Clamp, M. and Barton, G. J. (2009) Jalview Version 2-a multiple sequence alignment editor and analysis workbench. Bioinformatics, 25, 1189-1191.
    • (2009) Bioinformatics , vol.25 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.3    Clamp, M.4    Barton, G.J.5
  • 35
  • 36
    • 8444236034 scopus 로고    scopus 로고
    • A new scoring function and associated statistical significance for structure alignment by CE
    • Jia, Y, Dewey, TG, Shindyalov, IN. and Bourne, PE. (2004) A new scoring function and associated statistical significance for structure alignment by CE. J. Comput. Biol, 11, 787-799.
    • (2004) J. Comput. Biol , vol.11 , pp. 787-799
    • Jia, Y.1    Dewey, T.G.2    Shindyalov, I.N.3    Bourne, P.E.4
  • 37
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov, IN. and Bourne, PE. (1998) Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Eng., 11, 739-747.
    • (1998) Protein Eng. , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 38
    • 84907235997 scopus 로고    scopus 로고
    • Molecular basis for the recognition of methylated adenines in RNA by the eukaryotic YTH domain
    • Luo, S. and Tong, L. (2014) Molecular basis for the recognition of methylated adenines in RNA by the eukaryotic YTH domain. Proc Natl. Acad. Sci. U. S. A., 111, 13834-13839.
    • (2014) Proc Natl. Acad. Sci. U. S. A. , vol.111 , pp. 13834-13839
    • Luo, S.1    Tong, L.2
  • 40
    • 84897446590 scopus 로고    scopus 로고
    • Crystal structures of the novel cytosolic 5'-nucleotidase IIIB explain its preference for m7GMP
    • Monecke, T, Buschmann, J, Neumann, P, Wahle, E. and Ficner, R. (2014) Crystal structures of the novel cytosolic 5'-nucleotidase IIIB explain its preference for m7GMP. PLoS One, 9, e90915.
    • (2014) PLoS One , vol.9 , pp. e90915
    • Monecke, T.1    Buschmann, J.2    Neumann, P.3    Wahle, E.4    Ficner, R.5
  • 41
    • 84878944044 scopus 로고    scopus 로고
    • Readout of epigenetic modifications
    • Patel, D. J. and Wang, Z. (2013) Readout of epigenetic modifications. Annu. Rev. Biochem., 82, 81-118.
    • (2013) Annu. Rev. Biochem. , vol.82 , pp. 81-118
    • Patel, D.J.1    Wang, Z.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.