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Volumn 7, Issue 4, 2000, Pages 329-335

The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; POLYADENYLIC ACID; POLYNUCLEOTIDE ADENYLYLTRANSFERASE; PROTEIN U1A; RNA BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 0034070741     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/74101     Document Type: Article
Times cited : (126)

References (35)
  • 1
  • 2
    • 0027471377 scopus 로고
    • The human U1 snRNP-specific U1A protein inhibits polyadenylation of its own pre-mRNA
    • Boelens, W.C. et al. The human U1 snRNP-specific U1A protein inhibits polyadenylation of its own pre-mRNA. Cell 72, 881-892 (1993).
    • (1993) Cell , vol.72 , pp. 881-892
    • Boelens, W.C.1
  • 3
    • 0027453554 scopus 로고
    • A complex secondary structure in U1A pre-mRNA that binds two molecules of U1A protein is required for regulation of polyadenylation
    • van Gelder, C.W.G. et al. A complex secondary structure in U1A pre-mRNA that binds two molecules of U1A protein is required for regulation of polyadenylation. EMBO J. 12, 5191-5200 (1993).
    • (1993) EMBO J. , vol.12 , pp. 5191-5200
    • Van Gelder, C.W.G.1
  • 4
    • 0028173689 scopus 로고
    • The Human U1A snRNP Protein Regulates Polyadenylation via a Direct Interaction with Poly(A) Polymerase
    • Gunderson, S.I. et al. The Human U1A snRNP Protein Regulates Polyadenylation via a Direct Interaction with Poly(A) Polymerase. Cell 76, 531-541 (1994).
    • (1994) Cell , vol.76 , pp. 531-541
    • Gunderson, S.I.1
  • 5
    • 0031004560 scopus 로고    scopus 로고
    • Involvement of the carboxy terminus of vertebrate poly a polymerase in U1A autoregulation and in the coupling of splicing and polyadenylation
    • Gunderson, S.I., Vagner, S., Polycarpou-Schwarz, M. & Mattaj, I.W. Involvement of the carboxy terminus of vertebrate poly A polymerase in U1A autoregulation and in the coupling of splicing and polyadenylation. Genes S Dev. 11, 761-773 (1997).
    • (1997) Genes S Dev. , vol.11 , pp. 761-773
    • Gunderson, S.I.1    Vagner, S.2    Polycarpou-Schwarz, M.3    Mattaj, I.W.4
  • 6
    • 0033215058 scopus 로고    scopus 로고
    • Last but not least: Regulated poly(A) tail formation
    • Barabino, S.M.L & Keller, W. Last but not least: regulated poly(A) tail formation. Cell 99, 9-11 (1999).
    • (1999) Cell , vol.99 , pp. 9-11
    • Barabino, S.M.L.1    Keller, W.2
  • 7
    • 0031860374 scopus 로고    scopus 로고
    • RNA Recognition by RNP proteins during RNA processing and maturation
    • Varani, G. & Nagai, K. RNA Recognition by RNP proteins during RNA processing and maturation. Ann. Rev. Biophys. Biomol. Struct. 27,407-445 (1998).
    • (1998) Ann. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 407-445
    • Varani, G.1    Nagai, K.2
  • 8
    • 0029920331 scopus 로고    scopus 로고
    • Specificity of ribonucleoprotein interaction determined by RNA folding during complex formation
    • Allain, F.-H.T. et al. Specificity of ribonucleoprotein interaction determined by RNA folding during complex formation. Nature 380, 645-650 (1996).
    • (1996) Nature , vol.380 , pp. 645-650
    • Allain, F.-H.T.1
  • 9
    • 0030755124 scopus 로고    scopus 로고
    • Structural Basis of the RNA binding specificity of human U1A protein
    • Allain, F.H.-T., Howe, P.W.A., Neuhaus, D. & Varani, G. Structural Basis of the RNA binding specificity of human U1A protein. EMBO J. 16, 5764-5774 (1997).
    • (1997) EMBO J. , vol.16 , pp. 5764-5774
    • Allain, F.H.-T.1    Howe, P.W.A.2    Neuhaus, D.3    Varani, G.4
  • 10
    • 0000711201 scopus 로고
    • Overcoming the ambiguity problem encountered in the analysis of nuclear Overhauser magnetic resonance spectra of symmetric dimer proteins
    • Folkers, P.J.M., Folmer, R.H.A., Konings, R.N.H. & Hilbers, C.W. Overcoming the ambiguity problem encountered in the analysis of nuclear Overhauser magnetic resonance spectra of symmetric dimer proteins. J. Am. Chem. Soc. 115, 3798-3799(1993).
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 3798-3799
    • Folkers, P.J.M.1    Folmer, R.H.A.2    Konings, R.N.H.3    Hilbers, C.W.4
  • 11
    • 0033544709 scopus 로고    scopus 로고
    • Changes in sidechain and backbone dynamics identify determinants of specificity in RNA recognition by human U1A protein
    • Mittermaier, A., Varani, L., Muhandiram, D.R., Kay, L.E. & Varani, G. Changes in sidechain and backbone dynamics identify determinants of specificity in RNA recognition by human U1A protein. J. Mol. Biol. 294, 967-979 (1999).
    • (1999) J. Mol. Biol. , vol.294 , pp. 967-979
    • Mittermaier, A.1    Varani, L.2    Muhandiram, D.R.3    Kay, L.E.4    Varani, G.5
  • 12
    • 0030612833 scopus 로고    scopus 로고
    • Attenuation of T2 relaxation by mutual cancellation by dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • Pervushin, K., Riek, R., Wider, G. & Wüthrich, K. Attenuation of T2 relaxation by mutual cancellation by dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc. Natl. Acad. Sci. USA 94, 12366-12371 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wüthrich, K.4
  • 13
    • 0030808350 scopus 로고    scopus 로고
    • Methods for Measurement of intermolecular NOEs by multinuclear NMR spectroscopy: Application to a bacteriophage λ N-peptide/boxb RNA complex
    • Zwhalen, C. et al. Methods for Measurement of intermolecular NOEs by multinuclear NMR spectroscopy: application to a bacteriophage λ N-peptide/boxb RNA complex. J. Am. Chem. Soc. 119, 6711-6721 (1997).
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 6711-6721
    • Zwhalen, C.1
  • 14
    • 0031585990 scopus 로고    scopus 로고
    • Characterization of long-range structure in the denatured state of Staphyloccocal nuclease. I. Paramagnetic relaxation enhancement by nitroxide spin labels
    • Gillespie, J.R. & Shortle, D. Characterization of long-range structure in the denatured state of Staphyloccocal nuclease. I. Paramagnetic relaxation enhancement by nitroxide spin labels. J. Mol. Biol. 268,158-169 (1997).
    • (1997) J. Mol. Biol. , vol.268 , pp. 158-169
    • Gillespie, J.R.1    Shortle, D.2
  • 15
    • 0032576150 scopus 로고    scopus 로고
    • A new method to detect long-range protein-RNA contacts: NMR detection of electron-proton relaxation induced by nitroxide spin-labeled RNA
    • Ramos, A. & Varani, G. A new method to detect long-range protein-RNA contacts: NMR detection of electron-proton relaxation induced by nitroxide spin-labeled RNA. J. Am. Chem. Soc. 120,10992-10993 (1998).
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 10992-10993
    • Ramos, A.1    Varani, G.2
  • 16
    • 0031637533 scopus 로고    scopus 로고
    • Determination of the NMR structure of the complex between U1A protein and its RNA polyadenylation inhibition element
    • Howe, P.W.A., Allain, F.H.-T., Varani, G. & Neuhaus, D. Determination of the NMR structure of the complex between U1A protein and its RNA polyadenylation inhibition element. J. Biomol. NMR 11, 59-84(1998).
    • (1998) J. Biomol. NMR , vol.11 , pp. 59-84
    • Howe, P.W.A.1    Allain, F.H.-T.2    Varani, G.3    Neuhaus, D.4
  • 17
    • 0029082529 scopus 로고
    • Structure of the P1 helix from group I self splicing introns
    • Allain, F.H.-T. & Varani, G. Structure of the P1 helix from group I self splicing introns. J. Mol. Biol. 250, 333-353 (1995).
    • (1995) J. Mol. Biol. , vol.250 , pp. 333-353
    • Allain, F.H.-T.1    Varani, G.2
  • 18
    • 0032999204 scopus 로고    scopus 로고
    • Refinement of the structure of protein-RNA complexes by residual dipolar coupling analysis
    • Bayer, P., Varani, L. & Varani, G. Refinement of the structure of protein-RNA complexes by residual dipolar coupling analysis. J. Biomol. NMR 14,149-155 (1999).
    • (1999) J. Biomol. NMR , vol.14 , pp. 149-155
    • Bayer, P.1    Varani, L.2    Varani, G.3
  • 19
    • 0030585191 scopus 로고    scopus 로고
    • Two structurally different RNA molecules are bound by the spliceosomal protein U1A using the same recognition strategy
    • Jovine, L., Oubridge, C., Avis, J.M. & Nagai, K. Two structurally different RNA molecules are bound by the spliceosomal protein U1A using the same recognition strategy. Structure 4, 621-631 (1996).
    • (1996) Structure , vol.4 , pp. 621-631
    • Jovine, L.1    Oubridge, C.2    Avis, J.M.3    Nagai, K.4
  • 20
    • 0033056554 scopus 로고    scopus 로고
    • Multiprotein-DNA complexes in transcriptional regulation
    • Wolberger, C. Multiprotein-DNA complexes in transcriptional regulation. Ann. Rev. Biophys. Biomol. Struct. 28, 29-56 (1999).
    • (1999) Ann. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 29-56
    • Wolberger, C.1
  • 21
    • 0028828745 scopus 로고
    • Crystal structure of the MATa1/MATo2 homeodomain heterodimer bound to DNA
    • Li, T, Stark, M.R., Johnson, A.D. & Wolberger, C Crystal structure of the MATa1/MATo2 homeodomain heterodimer bound to DNA. Science 270, 262-269 (1995).
    • (1995) Science , vol.270 , pp. 262-269
    • Li, T.1    Stark, M.R.2    Johnson, A.D.3    Wolberger, C.4
  • 22
    • 0028142407 scopus 로고
    • Heterodimerization of the yeast homeodomain transcriptional regulator a2 and a1 induces an interfacial helix in a2
    • Phillips, C.L., Stark, M.R., Johnson, A.D. & Dahlquist, F.W. Heterodimerization of the yeast homeodomain transcriptional regulator a2 and a1 induces an interfacial helix in a2. Biochemistry 33, 9294-9302 (1994).
    • (1994) Biochemistry , vol.33 , pp. 9294-9302
    • Phillips, C.L.1    Stark, M.R.2    Johnson, A.D.3    Dahlquist, F.W.4
  • 23
    • 0033043229 scopus 로고    scopus 로고
    • Conformattonal consequences of binding of U1A protein to the 3' untranslated region of its pre-mRNA
    • Grainger, R.J., Norman, D.G. & Lilley, D.M.J. Conformattonal consequences of binding of U1A protein to the 3' untranslated region of its pre-mRNA. J. Mol. Biol. 288, 585-594 (1999).
    • (1999) J. Mol. Biol. , vol.288 , pp. 585-594
    • Grainger, R.J.1    Norman, D.G.2    Lilley, D.M.J.3
  • 24
    • 0028021493 scopus 로고
    • Interaction between two homeodomain proteins is specified by a short C-terminal tail
    • Stark, M.R. & Johnson, A.D. Interaction between two homeodomain proteins is specified by a short C-terminal tail. Nature 371, 429-432 (1994).
    • (1994) Nature , vol.371 , pp. 429-432
    • Stark, M.R.1    Johnson, A.D.2
  • 25
    • 0033999614 scopus 로고    scopus 로고
    • 14 Residues of the U1 snRNP-specific U1A protein is involved in homodimerization, cooperative RNA binding and inhibition of polyadenylation
    • in the press
    • Klein Gunnewiek, J.M.T. et al. 14 Residues of the U1 snRNP-specific U1A protein is involved in homodimerization, cooperative RNA binding and inhibition of polyadenylation. Mol. Cell Biol. in the press (2000).
    • (2000) Mol. Cell Biol.
    • Klein Gunnewiek, J.M.T.1
  • 26
    • 0028326761 scopus 로고
    • New insights into the auxiliary domains of eukaryotic RNA binding proteins
    • Biamonti, G. & Riva, S. New insights into the auxiliary domains of eukaryotic RNA binding proteins. FEBS Lett. 340, 1-8 (1994).
    • (1994) FEBS Lett. , vol.340 , pp. 1-8
    • Biamonti, G.1    Riva, S.2
  • 27
    • 0027753933 scopus 로고
    • Analysis of the RNA-recognition motif and RS and RGG domains: Conservation in metazoan pre-mRNA splicing factors
    • Birney, E., Kumar, S. & Krainer, A.R. Analysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factors. Nucleic Acids Res. 21, 5803-5816(1993).
    • (1993) Nucleic Acids Res. , vol.21 , pp. 5803-5816
    • Birney, E.1    Kumar, S.2    Krainer, A.R.3
  • 28
    • 0002123344 scopus 로고    scopus 로고
    • Preparation of RNA-protein complexes for X-ray crystallography and NMR
    • (ed. Smith, C.) Oxford University Press
    • Price, S.R., Oubridge, C, Varani, G. & Nagai, K. Preparation of RNA-protein complexes for X-ray crystallography and NMR. In RNA-Protein Interaction: Practical Approach (ed. Smith, C.) (Oxford University Press, 1998), p. 48-72.
    • (1998) RNA-Protein Interaction: Practical Approach , pp. 48-72
    • Price, S.R.1    Oubridge, C.2    Varani, G.3    Nagai, K.4
  • 29
    • 0029338320 scopus 로고
    • Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (FHSQC) detection scheme that avoids water saturation
    • Mori, S., Abeygunawardana, C, O'Neil Johnson, M. & van Zijl, P.C.M. Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (FHSQC) detection scheme that avoids water saturation. J. Mag. Res. B 108, 94-98 (1995).
    • (1995) J. Mag. Res. B , vol.108 , pp. 94-98
    • Mori, S.1    Abeygunawardana, C.2    O'Neil Johnson, M.3    Van Zijl, P.C.M.4
  • 30
    • 45149138663 scopus 로고
    • Comparison of different modes of two-dimensional reverse-correlation NMR for the study of proteins
    • Bax, A., Ikura, M., Kay, L.E., Torchia, D.A. & Tschudin, R. Comparison of different modes of two-dimensional reverse-correlation NMR for the study of proteins. J. Mag. Res. 86, 304-318 (1990).
    • (1990) J. Mag. Res. , vol.86 , pp. 304-318
    • Bax, A.1    Ikura, M.2    Kay, L.E.3    Torchia, D.A.4    Tschudin, R.5
  • 31
    • 0030207171 scopus 로고    scopus 로고
    • An optimized 3D NOESY-HSQC
    • Talluri, S. & Wagner, G. An optimized 3D NOESY-HSQC. J. Mag. Res. B 112, 200-205 (1996).
    • (1996) J. Mag. Res. B , vol.112 , pp. 200-205
    • Talluri, S.1    Wagner, G.2
  • 32
    • 0031585992 scopus 로고    scopus 로고
    • Characterization of long-range structure in the denatured state of Staphyloccocal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures
    • Gillespie, J.R. & Shortle, D. Characterization of long-range structure in the denatured state of Staphyloccocal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures. J. Mol. Biol. 268, 170-184 (1997).
    • (1997) J. Mol. Biol. , vol.268 , pp. 170-184
    • Gillespie, J.R.1    Shortle, D.2
  • 33
    • 0342723737 scopus 로고    scopus 로고
    • RNA Recognition by a Staufen double-stranded RNA binding domain
    • in the press
    • Ramos, A. et al. RNA Recognition by a Staufen double-stranded RNA binding domain. EMBO J. in the press (2000).
    • (2000) EMBO J.
    • Ramos, A.1
  • 34
    • 0001083043 scopus 로고    scopus 로고
    • Treatment of NOE constraints involving equivalent or nonstereoassigned protons in calculations of biomacromolecular structures
    • Fletcher, CM., Jones, D.N.M., Diamond, R. & Neuhaus, D. Treatment of NOE constraints involving equivalent or nonstereoassigned protons in calculations of biomacromolecular structures. J. Biomol. NMR 8, 292-310 (1996).
    • (1996) J. Biomol. NMR , vol.8 , pp. 292-310
    • Fletcher, C.M.1    Jones, D.N.M.2    Diamond, R.3    Neuhaus, D.4


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