메뉴 건너뛰기




Volumn 43, Issue 42, 2004, Pages 13404-13415

Global and local dynamics of the U1A Polyadenylation Inhibition Element (PIE) RNA and PIE RNA-U1A complexes

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; DATA REDUCTION; FLUORESCENCE; MATHEMATICAL MODELS; MOLECULAR STRUCTURE; PROTEINS;

EID: 6344294088     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049117g     Document Type: Article
Times cited : (12)

References (34)
  • 1
    • 0023478466 scopus 로고
    • cDNA cloning of the human U1 snRNA-associated A protein: Extensive homology between U1 and U2 snRNP-associated proteins
    • Sillikens, P. T. G., Habets, W. J., Beijer, R. P., and van Venrooij, W. J. (1987) cDNA cloning of the human U1 snRNA-associated A protein: Extensive homology between U1 and U2 snRNP-associated proteins, EMBO J. 6, 3841-3848.
    • (1987) EMBO J. , vol.6 , pp. 3841-3848
    • Sillikens, P.T.G.1    Habets, W.J.2    Beijer, R.P.3    Van Venrooij, W.J.4
  • 2
    • 0024851833 scopus 로고
    • Identification of the RNA binding segment of human U1A protein and definition of its binding site on U1 snRNA
    • Scherly, D., Boelens, W., van Venrooij, W. J., Dathan, N. A., and Mattaj, I. W. (1989) Identification of the RNA binding segment of human U1A protein and definition of its binding site on U1 snRNA, EMBO J. 8, 4163-4170.
    • (1989) EMBO J. , vol.8 , pp. 4163-4170
    • Scherly, D.1    Boelens, W.2    Van Venrooij, W.J.3    Dathan, N.A.4    Mattaj, I.W.5
  • 3
    • 0025221731 scopus 로고
    • Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A
    • Nagai, K., Oubridge, C., Jessen, T. H., Li, J., and Evans, P. R. (1990) Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A, Nature 348, 515-520.
    • (1990) Nature , vol.348 , pp. 515-520
    • Nagai, K.1    Oubridge, C.2    Jessen, T.H.3    Li, J.4    Evans, P.R.5
  • 4
    • 0030845289 scopus 로고    scopus 로고
    • Tertiary structure of RBD2 and backbone dynamics of RBD1 and RBD2 of the human U1A protein determined by NMR spectroscopy
    • Lu, J., and Hall, K. B. (1997) Tertiary structure of RBD2 and backbone dynamics of RBD1 and RBD2 of the human U1A protein determined by NMR spectroscopy, Biochemistry 36, 10393-10405.
    • (1997) Biochemistry , vol.36 , pp. 10393-10405
    • Lu, J.1    Hall, K.B.2
  • 5
    • 0028965970 scopus 로고
    • An RBD that does not bind RNA: NMR secondary structure determination and biochemical properties of the C-terminal RNA binding domain from the human U1A protein
    • Lu, J., and Hall, K. B. (1995) An RBD that does not bind RNA: NMR secondary structure determination and biochemical properties of the C-terminal RNA binding domain from the human U1A protein, J. Mol. Biol. 247, 739-752.
    • (1995) J. Mol. Biol. , vol.247 , pp. 739-752
    • Lu, J.1    Hall, K.B.2
  • 6
    • 0032858726 scopus 로고    scopus 로고
    • Global and local dynamics of the human U1A protein determined by tryptophan fluorescence
    • Jean, J. M., Clerte, C., and Hall, K. B. (1999) Global and local dynamics of the human U1A protein determined by tryptophan fluorescence, Protein Sci. 8, 2110-2120.
    • (1999) Protein Sci. , vol.8 , pp. 2110-2120
    • Jean, J.M.1    Clerte, C.2    Hall, K.B.3
  • 8
    • 0028173689 scopus 로고
    • The human U1A snRNP protein regulates polyadenylation via a direct interaction with poly(A) polymerase
    • Gunderson, S. I., Beyer, K., Martin, G., Keller, W., Boelens, W. C., and Mattaj, I. A. (1994) The human U1A snRNP protein regulates polyadenylation via a direct interaction with poly(A) polymerase, Cell 76, 531-541.
    • (1994) Cell , vol.76 , pp. 531-541
    • Gunderson, S.I.1    Beyer, K.2    Martin, G.3    Keller, W.4    Boelens, W.C.5    Mattaj, I.A.6
  • 9
    • 0031004560 scopus 로고    scopus 로고
    • Involvement of the carboxyl terminus of vertebrate poly(A) polymerase in U1A autoregulation and the coupling of splicing and polyadenylation
    • Gunderson, S. I., Vagner, S., Polycarpou-Schwarz, M., and Mattaj, I. W. (1997) Involvement of the carboxyl terminus of vertebrate poly(A) polymerase in U1A autoregulation and the coupling of splicing and polyadenylation, Genes Dev. 11, 761-773.
    • (1997) Genes Dev. , vol.11 , pp. 761-773
    • Gunderson, S.I.1    Vagner, S.2    Polycarpou-Schwarz, M.3    Mattaj, I.W.4
  • 11
    • 0031576340 scopus 로고    scopus 로고
    • Severe axial bending of RNA introduced by the U1A binding element present in the 3′ untranslated region of the U1A mRNA
    • Grainger, R. J., Murchie, A. I. H., Norman, D. G., and Lilley, D. M. J. (1997) Severe axial bending of RNA introduced by the U1A binding element present in the 3′ untranslated region of the U1A mRNA, J. Mol. Biol. 273, 84-92.
    • (1997) J. Mol. Biol. , vol.273 , pp. 84-92
    • Grainger, R.J.1    Murchie, A.I.H.2    Norman, D.G.3    Lilley, D.M.J.4
  • 12
    • 0033043229 scopus 로고    scopus 로고
    • Binding of U1A protein to the 3′ untranslated region of its pre-mRNA
    • Grainger, R. J., Norman, D. G., and Lilley, D. M. J. (1999) Binding of U1A protein to the 3′ untranslated region of its pre-mRNA, J. Mol. Biol. 288, 585-594.
    • (1999) J. Mol. Biol. , vol.288 , pp. 585-594
    • Grainger, R.J.1    Norman, D.G.2    Lilley, D.M.J.3
  • 13
    • 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., Allain, F. H., Varani, G., and Neuhaus, D. (1998) Determination of the NMR structure of the complex between U1A protein and its RNA polyadenylation inhibition element, J. Biomol. NMR 11, 59-84.
    • (1998) J. Biomol. NMR , vol.11 , pp. 59-84
    • Howe, P.W.1    Allain, F.H.2    Varani, G.3    Neuhaus, D.4
  • 14
    • 0030069826 scopus 로고    scopus 로고
    • Structure of polyadenylation regulatory element of the human U1A pre-mRNA 3′-untranslated region and interaction with the U1A protein
    • Gubser, C. C., and Varani, G. (1996) Structure of polyadenylation regulatory element of the human U1A pre-mRNA 3′-untranslated region and interaction with the U1A protein, Biochemistry 35, 2253-2260.
    • (1996) Biochemistry , vol.35 , pp. 2253-2260
    • Gubser, C.C.1    Varani, G.2
  • 15
    • 0033999614 scopus 로고    scopus 로고
    • Fourteen residues of the U1 snRNP-specific U1A protein are required for homodimerization, cooperative RNA binding, and inhibition of polyadenylation
    • Klein Gunnewiek, J. M., Hussein, R. I., van Aarssen, Y., Palacios, D., de Jong, R., van Venrooij, W. J., and Gunderson, S. I. (2000) Fourteen residues of the U1 snRNP-specific U1A protein are required for homodimerization, cooperative RNA binding, and inhibition of polyadenylation, Mol. Cell. Biol. 20, 2209-2217.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2209-2217
    • Klein Gunnewiek, J.M.1    Hussein, R.I.2    Van Aarssen, Y.3    Palacios, D.4    De Jong, R.5    Van Venrooij, W.J.6    Gunderson, S.I.7
  • 16
    • 0034691238 scopus 로고    scopus 로고
    • Spatial Orientation and dynamics of the U1A proteins in the U1A-UTR complex
    • Clerte, C., and Hall, K. B. (2000) Spatial Orientation and dynamics of the U1A proteins in the U1A-UTR complex, Biochemistry 39, 7320-7329.
    • (2000) Biochemistry , vol.39 , pp. 7320-7329
    • Clerte, C.1    Hall, K.B.2
  • 18
    • 0033795017 scopus 로고    scopus 로고
    • Anomalous fluorescence enhancement of Cy3 and cy3.5 versus anomalous fluorescence loss of Cy5 and Cy7 upon covalent linking to IgG and noncovalent binding to avidin
    • Gruber, H. J., Hahn, C. D., Kada, G., Riener, C. K., Harms, G. S., Ahrer, W., Dax, T. G., and Knaus, H. G. (2000) Anomalous fluorescence enhancement of Cy3 and cy3.5 versus anomalous fluorescence loss of Cy5 and Cy7 upon covalent linking to IgG and noncovalent binding to avidin, Bioconjugate Chem. 11, 696-704.
    • (2000) Bioconjugate Chem. , vol.11 , pp. 696-704
    • Gruber, H.J.1    Hahn, C.D.2    Kada, G.3    Riener, C.K.4    Harms, G.S.5    Ahrer, W.6    Dax, T.G.7    Knaus, H.G.8
  • 19
    • 0026718393 scopus 로고
    • Parameter estimation by least-squares methods
    • Johnson, M. L., and Faunt, L. M. (1992) Parameter estimation by least-squares methods, Methods Enzymol 210, 1-37.
    • (1992) Methods Enzymol , vol.210 , pp. 1-37
    • Johnson, M.L.1    Faunt, L.M.2
  • 21
    • 0016502735 scopus 로고
    • Distribution of end-to-end distances of oligopeptides in solution as estimated by energy transfer
    • Haas, E., Wilchek, M., Katchalski-Katzir, E., and Steinberg, I. Z. (1975) Distribution of end-to-end distances of oligopeptides in solution as estimated by energy transfer, Proc. Natl. Acad. Sci. U.S.A. 72, 1807-1811.
    • (1975) Proc. Natl. Acad. Sci. U.S.A. , vol.72 , pp. 1807-1811
    • Haas, E.1    Wilchek, M.2    Katchalski-Katzir, E.3    Steinberg, I.Z.4
  • 22
    • 0024632497 scopus 로고
    • The effect of a distribution of separations upon intramolecular distances in biopolymers, as determined by radiationless energy transfer
    • Albaugh, S., Lan, J. Q., and Steiner, R. F. (1989) The effect of a distribution of separations upon intramolecular distances in biopolymers, as determined by radiationless energy transfer, Biophys. Chem. 33, 71-76.
    • (1989) Biophys. Chem. , vol.33 , pp. 71-76
    • Albaugh, S.1    Lan, J.Q.2    Steiner, R.F.3
  • 23
    • 0025887737 scopus 로고
    • Interterminal distance and flexibility of a triantennary glycopeptide as measured by resonance energy transfer
    • Rice, K. G., Wu, R. G., Brand, L., and Lee, Y. C. (1991) Interterminal distance and flexibility of a triantennary glycopeptide as measured by resonance energy transfer, Biochemistry 30, 6646-6655.
    • (1991) Biochemistry , vol.30 , pp. 6646-6655
    • Rice, K.G.1    Wu, R.G.2    Brand, L.3    Lee, Y.C.4
  • 24
    • 0025929570 scopus 로고
    • Fluorescence techniques for studying protein structure
    • Eftink, M. R. (1991) Fluorescence techniques for studying protein structure, Methods Biochem. Anal. 35, 127-205.
    • (1991) Methods Biochem. Anal. , vol.35 , pp. 127-205
    • Eftink, M.R.1
  • 26
    • 13344269017 scopus 로고
    • Solution conformations of a biantennary glycopeptide and a series of its exoglycosidase products from sequential trimming of sugar residues
    • Wu, P., Lee, K. B., Lee, Y. C., and Brand, L. (1991) Solution conformations of a biantennary glycopeptide and a series of its exoglycosidase products from sequential trimming of sugar residues, J. Biol. Chem. 271, 1470-1474.
    • (1991) J. Biol. Chem. , vol.271 , pp. 1470-1474
    • Wu, P.1    Lee, K.B.2    Lee, Y.C.3    Brand, L.4
  • 27
    • 0025790430 scopus 로고
    • Interaction of DNA with the Klenow fragment of DNA polymerase I studied by time-resolved fluorescence spectroscopy
    • Guest, C. R., Hochstrasser, R. A., Dupuy, C. G., Allen, D. J., Benkovic, S. J., and Millar, D. P. (1991) Interaction of DNA with the Klenow fragment of DNA polymerase I studied by time-resolved fluorescence spectroscopy, Biochemistry 30, 8759-8770.
    • (1991) Biochemistry , vol.30 , pp. 8759-8770
    • Guest, C.R.1    Hochstrasser, R.A.2    Dupuy, C.G.3    Allen, D.J.4    Benkovic, S.J.5    Millar, D.P.6
  • 28
    • 0035793105 scopus 로고    scopus 로고
    • 2-Aminopurine fluorescence quenching and lifetimes: Role of bases stacking
    • Jean, J. M., and Hall, K. B. (2001) 2-Aminopurine fluorescence quenching and lifetimes: Role of bases stacking, Proc. Natl. Acad. Sci. U.S.A. 98, 37-41.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 37-41
    • Jean, J.M.1    Hall, K.B.2
  • 29
    • 1242274330 scopus 로고    scopus 로고
    • A guide to ions and RNA structure
    • Draper, D. E. (2004) A guide to ions and RNA structure, RNA 10, 335-343.
    • (2004) RNA , vol.10 , pp. 335-343
    • Draper, D.E.1
  • 30
    • 0030476302 scopus 로고    scopus 로고
    • Thermodynamic comparison of the salt dependence of natural RNA hairpins and RNA hairpins with nonnucleotide spacers
    • Williams, D. J., and Hall, K. B. (1996) Thermodynamic comparison of the salt dependence of natural RNA hairpins and RNA hairpins with nonnucleotide spacers, Biochemistry 35, 14665-14670.
    • (1996) Biochemistry , vol.35 , pp. 14665-14670
    • Williams, D.J.1    Hall, K.B.2
  • 31
    • 0026713783 scopus 로고
    • Interaction of N-terminal domain of U1A protein with an RNA stem/loop
    • Hall, K. B., and Stump, W. T. (1992) Interaction of N-terminal domain of U1A protein with an RNA stem/loop, Nucleic Acids Res. 20, 4283-4290.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 4283-4290
    • Hall, K.B.1    Stump, W.T.2
  • 33
    • 0037028557 scopus 로고    scopus 로고
    • Structural analysis of metal ion ligation to nucleotides and nucleic acids using pulsed EPR spectroscopy
    • Hoogstraten, C. G., Grant, C. V., Horton, T. E., DeRose, V. J., and Britt, R. D. (2002) Structural analysis of metal ion ligation to nucleotides and nucleic acids using pulsed EPR spectroscopy, J. Am. Chem. Soc. 124, 834-842.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 834-842
    • Hoogstraten, C.G.1    Grant, C.V.2    Horton, T.E.3    DeRose, V.J.4    Britt, R.D.5
  • 34
    • 0034070741 scopus 로고    scopus 로고
    • 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
    • Varani, L., Gunderson, S. I., Mattaj, I. W., Kay, L. E., Neuhaus, D., and Varani, G. (2000) 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, Nat. Struct. Biol. 7, 329-335.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 329-335
    • Varani, L.1    Gunderson, S.I.2    Mattaj, I.W.3    Kay, L.E.4    Neuhaus, D.5    Varani, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.