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Volumn 39, Issue 4, 2011, Pages 1538-1553

Structural basis for the dual RNA-recognition modes of human Tra2-β RRM

Author keywords

[No Author keywords available]

Indexed keywords

SERINE ARGININE RICH PROTEIN; TRANSFORMER2 BETA PROTEIN; UNCLASSIFIED DRUG;

EID: 79952324952     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkq854     Document Type: Article
Times cited : (63)

References (49)
  • 1
    • 14644431487 scopus 로고    scopus 로고
    • Broad Specificity of SR (Serine{plus 45 degree rule}Arginine) Proteins in the Regulation of Alternative Splicing of Pre-Messenger RNA
    • DOI 10.1016/S0079-6603(04)78002-2, PII S0079660304780022
    • Bourgeois, C.F., Lejeune, F. and Stevenin, J. (2004) Broad specificity of SR (serine/arginine) proteins in the regulation of alternative splicing of pre-messenger RNA. Prog. Nucleic Acid Res. Mol. Biol., 78, 37-88. (Pubitemid 39753917)
    • (2004) Progress in Nucleic Acid Research and Molecular Biology , vol.78 , pp. 37-88
    • Bourgeois, C.F.1    Lejeune, F.2    Stevenin, J.3
  • 2
    • 1842635464 scopus 로고    scopus 로고
    • Regulation of alternative RNA splicing by exon definition and exon sequences in viral and mammalian gene expression
    • Zheng, Z.M. (2004) Regulation of alternative RNA splicing by exon definition and exon sequences in viral and mammalian gene expression. J. Biomed. Sci., 11, 278-294.
    • (2004) J. Biomed. Sci. , vol.11 , pp. 278-294
    • Zheng, Z.M.1
  • 3
    • 0026756495 scopus 로고
    • Binding of the Drosophila transformer and transformer-2 proteins to the regulatory elements of doublesex primary transcript for sex-specific RNA processing
    • Inoue, K., Hoshijima, K., Higuchi, I., Sakamoto, H. and Shimura, Y. (1992) Binding of the Drosophila transformer and transformer-2 proteins to the regulatory elements of doublesex primary transcript for sex-specific RNA processing. Proc. Natl Acad. Sci. USA, 89, 8092-8096.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 8092-8096
    • Inoue, K.1    Hoshijima, K.2    Higuchi, I.3    Sakamoto, H.4    Shimura, Y.5
  • 4
    • 1542330117 scopus 로고    scopus 로고
    • Tra2β, SF2/ASF and SRp30c modulate the function of an exonic splicing enhancer in exon 10 of tau pre-mRNA
    • DOI 10.1111/j.1356-9597.2004.00709.x
    • Kondo, S., Yamamoto, N., Murakami, T., Okumura, M., Mayeda, A. and Imaizumi, K. (2004) Tra2b, SF2/ASF and SRp30c modulate the function of an exonic splicing enhancer in exon 10 of tau pre-mRNA. Genes Cells, 9, 121-130. (Pubitemid 38312956)
    • (2004) Genes to Cells , vol.9 , Issue.2 , pp. 121-130
    • Kondo, S.1    Yamamoto, N.2    Murakami, T.3    Okumura, M.4    Mayeda, A.5    Imaizumi, K.6
  • 5
    • 34548145188 scopus 로고    scopus 로고
    • Molecular mechanisms of spinal muscular atrophy
    • DOI 10.1177/0883073807305787
    • Sumner, C.J. (2007) Molecular mechanisms of spinal muscular atrophy. J. Child. Neurol., 22, 979-989. (Pubitemid 47308312)
    • (2007) Journal of Child Neurology , vol.22 , Issue.8 , pp. 979-989
    • Sumner, C.J.1
  • 8
    • 0025367075 scopus 로고
    • 0 splice site selection by activating proximal sites
    • 0 splice site selection by activating proximal sites. Cell, 62, 35-42.
    • (1990) Cell , vol.62 , pp. 35-42
    • Krainer, A.R.1    Conway, G.C.2    Kozak, D.3
  • 9
    • 0025827463 scopus 로고
    • Primary structure of the human splicing factor ASF reveals similarities with Drosophila regulators
    • Ge, H., Zuo, P. and Manley, J.L. (1991) Primary structure of the human splicing factor ASF reveals similarities with Drosophila regulators. Cell, 66, 373-382. (Pubitemid 121001374)
    • (1991) Cell , vol.66 , Issue.2 , pp. 373-382
    • Ge, H.1    Zuo, P.2    Manley, J.L.3
  • 10
    • 0032478506 scopus 로고    scopus 로고
    • Human Tra2 proteins are sequence-specific activators of pre-mRNA splicing
    • DOI 10.1016/S0092-8674(00)81153-8
    • Tacke, R., Tohyama, M., Ogawa, S. and Manley, J.L. (1998) Human Tra2 proteins are sequence-specific activators of pre-mRNA splicing. Cell, 93, 139-148. (Pubitemid 28173559)
    • (1998) Cell , vol.93 , Issue.1 , pp. 139-148
    • Tacke, R.1    Tohyama, M.2    Ogawa, S.3    Manley, J.L.4
  • 12
    • 0028990057 scopus 로고
    • The RNP domain: A sequence-specific RNA-binding domain involved in processing and transport of RNA
    • Nagai, K., Oubridge, C., Ito, N., Avis, J. and Evans, P. (1995) The RNP domain: a sequence-specific RNA-binding domain involved in processing and transport of RNA. Trends Biochem. Sci., 20, 235-240.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 235-240
    • Nagai, K.1    Oubridge, C.2    Ito, N.3    Avis, J.4    Evans, P.5
  • 17
    • 3042737403 scopus 로고    scopus 로고
    • U2AF homology motifs: Protein recognition in the RRM world
    • DOI 10.1101/gad.1206204
    • Kielkopf, C.L., Lucke, S. and Green, M.R. (2004) U2AF homology motifs: protein recognition in the RRM world. Genes Dev., 18, 1513-1526. (Pubitemid 38868903)
    • (2004) Genes and Development , vol.18 , Issue.13 , pp. 1513-1526
    • Kielkopf, C.L.1    Lucke, S.2    Green, M.R.3
  • 19
    • 0032923295 scopus 로고    scopus 로고
    • Cell-free production and stable-isotope labeling of milligram quantities of proteins
    • DOI 10.1016/S0014-5793(98)01620-2, PII S0014579398016202
    • Kigawa, T., Yabuki, T., Yoshida, Y., Tsutsui, M., Ito, Y., Shibata, T. and Yokoyama, S. (1999) Cell-free production and stable-isotope labeling of milligram quantities of proteins. FEBS Lett., 442, 15-19. (Pubitemid 29065369)
    • (1999) FEBS Letters , vol.442 , Issue.1 , pp. 15-19
    • Kigawa, T.1    Yabuki, T.2    Yoshida, Y.3    Tsutsui, M.4    Ito, Y.5    Shibata, T.6    Yokoyama, S.7
  • 21
    • 0028019827 scopus 로고
    • Multidimensional nuclear magnetic resonance methods for protein studies
    • DOI 10.1016/S0959-440X(94)90173-2
    • Bax, A. (1994) Multidimensional nuclear magnetic resonance methods for protein studies. Curr. Opin. Struct. Biol., 4, 738-744. (Pubitemid 24325294)
    • (1994) Current Opinion in Structural Biology , vol.4 , Issue.5 , pp. 738-744
    • Bax, A.1
  • 22
    • 0030624544 scopus 로고    scopus 로고
    • NMR methods for the study of protein structure and dynamics
    • Kay, L.E. (1997) NMR methods for the study of protein structure and dynamics. Biochem. Cell Biol., 75, 1-15. (Pubitemid 127733122)
    • (1997) Biochemistry and Cell Biology , vol.75 , Issue.1 , pp. 1-15
    • Kay, L.E.1
  • 23
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J. and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR, 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 24
    • 4644259437 scopus 로고    scopus 로고
    • Using NMRView to visualize and analyze the NMR spectra of macromolecules
    • Johnson, B.A. (2004) Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol. Biol., 278, 313-352.
    • (2004) Methods Mol. Biol. , vol.278 , pp. 313-352
    • Johnson, B.A.1
  • 25
    • 34547923673 scopus 로고    scopus 로고
    • KUJIRA, a package of integrated modules for systematic and interactive analysis of NMR data directed to high-throughput NMR structure studies
    • DOI 10.1007/s10858-007-9175-5
    • Kobayashi, N., Iwahara, J., Koshiba, S., Tomizawa, T., Tochio, N., Guntert, P., Kigawa, T. and Yokoyama, S. (2007) KUJIRA, a package of integrated modules for systematic and interactive analysis of NMR data directed to high-throughput NMR structure studies. J. Biomol. NMR, 39, 31-52. (Pubitemid 47249693)
    • (2007) Journal of Biomolecular NMR , vol.39 , Issue.1 , pp. 31-52
    • Kobayashi, N.1    Iwahara, J.2    Koshiba, S.3    Tomizawa, T.4    Tochio, N.5    Guntert, P.6    Kigawa, T.7    Yokoyama, S.8
  • 26
    • 33845555707 scopus 로고
    • Exchangeable proton NMR without base-line distortion using new strong-pulse sequences
    • Pierre Plateau, M.G. (1982) Exchangeable proton NMR without base-line distortion, using new strong-pulse sequences. J. Am. Chem. Soc., 104, 7310-7311.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 7310-7311
    • Pierre Plateau, M.G.1
  • 28
    • 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
    • DOI 10.1016/S0022-2836(02)00241-3
    • 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. (Pubitemid 34729497)
    • (2002) Journal of Molecular Biology , vol.319 , Issue.1 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 29
    • 58849162221 scopus 로고    scopus 로고
    • Automated structure determination from NMR spectra
    • Guntert, P. (2009) Automated structure determination from NMR spectra. Eur. Biophys. J., 38, 129-143.
    • (2009) Eur. Biophys. J. , vol.38 , pp. 129-143
    • Guntert, P.1
  • 30
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • DOI 10.1006/jmbi.1997.1284
    • Guntert, P., Mumenthaler, C. and Wuthrich, K. (1997) Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol., 273, 283-298. (Pubitemid 27460230)
    • (1997) Journal of Molecular Biology , vol.273 , Issue.1 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 31
    • 0027236528 scopus 로고
    • The high-resolution, three-dimensional solution structure of human interleukin-4 determined by multidimensional heteronuclear magnetic resonance spectroscopy
    • Powers, R., Garrett, D.S., March, C.J., Frieden, E.A., Gronenborn, A.M. and Clore, G.M. (1993) The high-resolution, three-dimensional solution structure of human interleukin-4 determined by multidimensional heteronuclear magnetic resonance spectroscopy. Biochemistry, 32, 6744-6762. (Pubitemid 23217146)
    • (1993) Biochemistry , vol.32 , Issue.26 , pp. 6744-6762
    • Powers, R.1    Garrett, D.S.2    March, C.J.3    Frieden, E.A.4    Gronenborn, A.M.5    Clore, G.M.6
  • 35
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • DOI 10.1016/0263-7855(96)00009-4
    • Koradi, R., Billeter, M. and Wuthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph., 14, 51-55, 29-32. (Pubitemid 26152976)
    • (1996) Journal of Molecular Graphics , vol.14 , Issue.1 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 36
    • 41149169592 scopus 로고    scopus 로고
    • NELF-E RRM undergoes major structural changes in flexible protein regions on target RNA binding
    • DOI 10.1021/bi702429m
    • Rao, J.N., Schweimer, K., Wenzel, S., Wohrl, B.M. and Rosch, P. (2008) NELF-E RRM undergoes major structural changes in flexible protein regions on target RNA binding. Biochemistry, 47, 3756-3761. (Pubitemid 351431365)
    • (2008) Biochemistry , vol.47 , Issue.12 , pp. 3756-3761
    • Rao, J.N.1    Schweimer, K.2    Wenzel, S.3    Wohrl, B.M.4    Rosch, P.5
  • 37
    • 33750997616 scopus 로고    scopus 로고
    • Protein-RNA interactions: Exploring binding patterns with a three-dimensional superposition analysis of high resolution structures
    • DOI 10.1093/bioinformatics/btl470
    • Morozova, N., Allers, J., Myers, J. and Shamoo, Y. (2006) Protein-RNA interactions: exploring binding patterns with a three-dimensional superposition analysis of high resolution structures. Bioinformatics, 22, 2746-2752. (Pubitemid 44742394)
    • (2006) Bioinformatics , vol.22 , Issue.22 , pp. 2746-2752
    • Morozova, N.1    Myers, J.2    Shamoo, Y.3
  • 38
    • 0033591465 scopus 로고    scopus 로고
    • Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure
    • DOI 10.1006/jmbi.1999.2700
    • Mathews, D.H., Sabina, J., Zuker, M. and Turner, D.H. (1999) Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure. J. Mol. Biol., 288, 911-940. (Pubitemid 29248642)
    • (1999) Journal of Molecular Biology , vol.288 , Issue.5 , pp. 911-940
    • Mathews, D.H.1    Sabina, J.2    Zuker, M.3    Turner, D.H.4
  • 39
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • DOI 10.1093/nar/gkg595
    • Zuker, M. (2003) Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res., 31, 3406-3415. (Pubitemid 37442169)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3406-3415
    • Zuker, M.1
  • 40
    • 30444446153 scopus 로고    scopus 로고
    • Molecular basis of RNA recognition by the human alternative splicing factor Fox-1
    • DOI 10.1038/sj.emboj.7600918, PII 7600918
    • Auweter, S.D., Fasan, R., Reymond, L., Underwood, J.G., Black, D.L., Pitsch, S. and Allain, F.H. (2006) Molecular basis of RNA recognition by the human alternative splicing factor Fox-1. EMBO J., 25, 163-173. (Pubitemid 43077305)
    • (2006) EMBO Journal , vol.25 , Issue.1 , pp. 163-173
    • Auweter, S.D.1    Fasan, R.2    Reymond, L.3    Underwood, J.G.4    Black, D.L.5    Pitsch, S.6    Allain, F.H.-T.7
  • 41
    • 0028004607 scopus 로고
    • Crystal structure at 1.92 A resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin
    • Oubridge, C., Ito, N., Evans, P.R., Teo, C.H. and Nagai, K. (1994) Crystal structure at 1.92 A resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin. Nature, 372, 432-438.
    • (1994) Nature , vol.372 , pp. 432-438
    • Oubridge, C.1    Ito, N.2    Evans, P.R.3    Teo, C.H.4    Nagai, K.5
  • 42
    • 0033134777 scopus 로고    scopus 로고
    • Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA
    • Ding, J., Hayashi, M.K., Zhang, Y., Manche, L., Krainer, A.R. and Xu, R.M. (1999) Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA. Genes Dev., 13, 1102-1115. (Pubitemid 29233142)
    • (1999) Genes and Development , vol.13 , Issue.9 , pp. 1102-1115
    • Ding, J.1    Hayashi, M.K.2    Zhang, Y.3    Manche, L.4    Krainer, A.R.5    Xu, R.-M.6
  • 45
    • 33750222859 scopus 로고    scopus 로고
    • Sequence-specific binding of single-stranded RNA: Is there a code for recognition?
    • DOI 10.1093/nar/gkl620
    • Auweter, S.D., Oberstrass, F.C. and Allain, F.H. (2006) Sequence-specific binding of single-stranded RNA: is there a code for recognition? Nucleic Acids Res., 34, 4943-4959. (Pubitemid 44605637)
    • (2006) Nucleic Acids Research , vol.34 , Issue.17 , pp. 4943-4959
    • Auweter, S.D.1    Oberstrass, F.C.2    Allain, F.H.-T.3
  • 46
    • 4444283116 scopus 로고    scopus 로고
    • Human UP1 as a model for understanding purine recognition in the family of proteins containing the RNA recognition motif (RRM)
    • DOI 10.1016/j.jmb.2004.07.029, PII S0022283604008563
    • Myers, J.C. and Shamoo, Y. (2004) Human UP1 as a model for understanding purine recognition in the family of proteins containing the RNA recognition motif (RRM). J. Mol. Biol., 342, 743-756. (Pubitemid 39165647)
    • (2004) Journal of Molecular Biology , vol.342 , Issue.3 , pp. 743-756
    • Myers, J.C.1    Shamoo, Y.2
  • 47
    • 77950192241 scopus 로고    scopus 로고
    • Structure and functional implications of a complex containing a segment of U6 RNA bound by a domain of Prp24
    • Martin-Tumasz, S., Reiter, N.J., Brow, D.A. and Butcher, S.E. (2010) Structure and functional implications of a complex containing a segment of U6 RNA bound by a domain of Prp24. RNA, 16, 792-804.
    • (2010) RNA , vol.16 , pp. 792-804
    • Martin-Tumasz, S.1    Reiter, N.J.2    Brow, D.A.3    Butcher, S.E.4
  • 48
    • 0033578927 scopus 로고    scopus 로고
    • Recognition of polyadenylate RNA by the poly(A)-binding protein
    • DOI 10.1016/S0092-8674(00)81517-2
    • Deo, R.C., Bonanno, J.B., Sonenberg, N. and Burley, S.K. (1999) Recognition of polyadenylate RNA by the poly(A)-binding protein. Cell, 98, 835-845. (Pubitemid 29446900)
    • (1999) Cell , vol.98 , Issue.6 , pp. 835-845
    • Deo, R.C.1    Bonanno, J.B.2    Sonenberg, N.3    Burley, S.K.4


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