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Volumn 5, Issue 3, 1998, Pages 203-212

Solution structure of P22 transcriptional antitermination N peptide-box B RNA complex

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; RNA;

EID: 0031916834     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0398-203     Document Type: Article
Times cited : (93)

References (40)
  • 1
    • 0027296170 scopus 로고
    • Transcriptional antitermination
    • Greenblatt, J., Nodwell, J. R. & Mason, S. W. Transcriptional antitermination. Nature 364, 401-406 (1993).
    • (1993) Nature , vol.364 , pp. 401-406
    • Greenblatt, J.1    Nodwell, J.R.2    Mason, S.W.3
  • 2
    • 0027321585 scopus 로고
    • Control of transcription termination by RNA-binding proteins
    • Das, A. Control of transcription termination by RNA-binding proteins. Annu. rev. Biochem. 62, 893-930 (1993).
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 893-930
    • Das, A.1
  • 3
    • 0028842495 scopus 로고
    • Transcriptional antitermination: The λ paradigm updated
    • Friedman, D. I. & Court, D. L. Transcriptional antitermination: the λ paradigm updated. Mol. Microbiol. 18, 191-200 (1995).
    • (1995) Mol. Microbiol. , vol.18 , pp. 191-200
    • Friedman, D.I.1    Court, D.L.2
  • 4
    • 0029007110 scopus 로고
    • Bipartite function of a small RNA hairpin in transcription antitermination in bacteriophage λ
    • Chattopadhyay, S., Garcia-Mena, J., DeVito, J., Wolska, K. & Das, A. Bipartite function of a small RNA hairpin in transcription antitermination in bacteriophage λ. Proc Natl. Acad. Sci. USA 92, 4061-4065 (1995).
    • (1995) Proc Natl. Acad. Sci. USA , vol.92 , pp. 4061-4065
    • Chattopadhyay, S.1    Garcia-Mena, J.2    DeVito, J.3    Wolska, K.4    Das, A.5
  • 5
    • 0024434420 scopus 로고
    • Sequence-specific recognition of RNA hairpins by bacteriophage antiterminators requires a conserved arginine-rich motif
    • Lazinski, D., Grzadzielska, E. & Das, A. Sequence-specific recognition of RNA hairpins by bacteriophage antiterminators requires a conserved arginine-rich motif. Cell 59, 207-218 (1989).
    • (1989) Cell , vol.59 , pp. 207-218
    • Lazinski, D.1    Grzadzielska, E.2    Das, A.3
  • 6
    • 0030710554 scopus 로고    scopus 로고
    • Assembly of the N-dependent antitermination complex of phage λ: NusA and RNA bind independently to different unfolded domains of the N protein
    • Van Gilst, M. R. & von Hippel, P. H. Assembly of the N-dependent antitermination complex of phage λ: NusA and RNA bind independently to different unfolded domains of the N protein. J. Mol. Biol. 274, 160-173 (1997).
    • (1997) J. Mol. Biol. , vol.274 , pp. 160-173
    • Van Gilst, M.R.1    Von Hippel, P.H.2
  • 7
    • 0029048796 scopus 로고
    • Structural variety of arginine-rich RNA-binding peptides
    • Tan, R. & Frankel, A. D. Structural variety of arginine-rich RNA-binding peptides. Proc Natl. Acad. Sci. USA 92, 5282-5286 (1995).
    • (1995) Proc Natl. Acad. Sci. USA , vol.92 , pp. 5282-5286
    • Tan, R.1    Frankel, A.D.2
  • 8
    • 0031024660 scopus 로고    scopus 로고
    • Analysis of bacteriophage N protein and peptide binding to boxB RNA using polyacrylamide gel coelectrophoresis (PACE)
    • Cilley, C. D. & Williamson, J. R. Analysis of bacteriophage N protein and peptide binding to boxB RNA using polyacrylamide gel coelectrophoresis (PACE). RNA 3, 57-67 (1997).
    • (1997) RNA , vol.3 , pp. 57-67
    • Cilley, C.D.1    Williamson, J.R.2
  • 10
    • 0030596092 scopus 로고    scopus 로고
    • A network of heterogeneous hydrogen bonds in GNRA tetraloops
    • Jucker, F. M., Heus, H. A., Yip, P. F., Moors, E. H. & Pardi, A. A network of heterogeneous hydrogen bonds in GNRA tetraloops. J. Mol. Biol. 264, 968-980 (1996).
    • (1996) J. Mol. Biol. , vol.264 , pp. 968-980
    • Jucker, F.M.1    Heus, H.A.2    Yip, P.F.3    Moors, E.H.4    Pardi, A.5
  • 11
    • 0029820625 scopus 로고    scopus 로고
    • Crystal structure of a group 1 ribozyme domain: Principles of RNA packing
    • Cate, J. H. et al. Crystal structure of a group 1 ribozyme domain: principles of RNA packing. Science 273, 1678-1685 (1996).
    • (1996) Science , vol.273 , pp. 1678-1685
    • Cate, J.H.1
  • 12
    • 0028037302 scopus 로고
    • Model for an RNA tertiary interaction from the structure of an intermolecular complex between a GAAA tetraloop and an RNA helix
    • Pley, H., Flaherty, K. & McKay, D. Model for an RNA tertiary interaction from the structure of an intermolecular complex between a GAAA tetraloop and an RNA helix. Nature 372, 111-113 (1994).
    • (1994) Nature , vol.372 , pp. 111-113
    • Pley, H.1    Flaherty, K.2    McKay, D.3
  • 13
    • 0001750516 scopus 로고
    • Springer Advanced Texts in Chemistry (ed. Cantor, C. R.) Springer-Verlag, New York
    • Saenger, W. Principles of nucleic acid structure. In Springer Advanced Texts in Chemistry (ed. Cantor, C. R.) 118 (Springer-Verlag, New York; 1984).
    • (1984) Principles of Nucleic Acid Structure. , pp. 118
    • Saenger, W.1
  • 15
    • 0026651395 scopus 로고
    • Conformation of the TAR RNA-arginine complex by NMR spectroscope
    • Puglisi, J. D., Tan, R., Calnan, B. J., Frankel, A. D. & Williamson, J. R. Conformation of the TAR RNA-arginine complex by NMR spectroscope. Science 257, 76-80 (1992).
    • (1992) Science , vol.257 , pp. 76-80
    • Puglisi, J.D.1    Tan, R.2    Calnan, B.J.3    Frankel, A.D.4    Williamson, J.R.5
  • 16
    • 0027288664 scopus 로고
    • Clustered arginine residues of bacteriophage λ N protein are essential to antitermination of transcription, but their locale cannot compensate for boxB loop defects
    • Franklin, N. C. Clustered arginine residues of bacteriophage λ N protein are essential to antitermination of transcription, but their locale cannot compensate for boxB loop defects. J. Mol. Biol. 231, 343-360 (1993).
    • (1993) J. Mol. Biol. , vol.231 , pp. 343-360
    • Franklin, N.C.1
  • 17
    • 0030713372 scopus 로고    scopus 로고
    • RNA recognition by a bent α-helix regulates transcriptional antitermination in phage λ
    • Su, L. et al. RNA recognition by a bent α-helix regulates transcriptional antitermination in phage λ. Biochemistry 36, 12722-12732 (1997).
    • (1997) Biochemistry , vol.36 , pp. 12722-12732
    • Su, L.1
  • 18
    • 0030931149 scopus 로고    scopus 로고
    • An RNA enhancer in a phage transcriptional antitermination complex functions as a structural switch
    • Su, L. et al. An RNA enhancer in a phage transcriptional antitermination complex functions as a structural switch. Genes Dev. 11, 2214-2226 (1997).
    • (1997) Genes Dev. , vol.11 , pp. 2214-2226
    • Su, L.1
  • 19
    • 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
    • Zwahlen, 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
    • Zwahlen, C.1
  • 20
    • 0028858599 scopus 로고
    • Solution structure of a bovine immunodeficiency virus Tat-TAR peptide-RNA complex
    • Puglisi, J. D., Chen, L., Blanchard, S. & Frankel, A. D. Solution structure of a bovine immunodeficiency virus Tat-TAR peptide-RNA complex. Science 270, 1200-1203 (1995).
    • (1995) Science , vol.270 , pp. 1200-1203
    • Puglisi, J.D.1    Chen, L.2    Blanchard, S.3    Frankel, A.D.4
  • 21
    • 0029613238 scopus 로고
    • Molecular recognition in the bovine immunodeficiency virus Tat peptide-TAR RNA complex
    • Ye, X., Kumar, R. A. & Patel, D. J. Molecular recognition in the bovine immunodeficiency virus Tat peptide-TAR RNA complex. Chem. Biol. 2, 827-840 (1995).
    • (1995) Chem. Biol. , vol.2 , pp. 827-840
    • Ye, X.1    Kumar, R.A.2    Patel, D.J.3
  • 22
    • 0029784592 scopus 로고    scopus 로고
    • α helix-RNA major groove recognition in an HIV-1 rev peptide-RRE RNA complex
    • Battiste, J. L. et al. α helix-RNA major groove recognition in an HIV-1 rev peptide-RRE RNA complex. Science 273, 1547-1551 (1996).
    • (1996) Science , vol.273 , pp. 1547-1551
    • Battiste, J.L.1
  • 23
    • 0030475417 scopus 로고    scopus 로고
    • Deep penetration of an α-helix into a widened RNA major groove in the HIV-1 rev peptide-RNA aptamer complex
    • Ye, X., Gorin, A., Ellington, A. D. & Patel, D. J. Deep penetration of an α-helix into a widened RNA major groove in the HIV-1 rev peptide-RNA aptamer complex. Nature Struct. Biol. 3, 1026-1033 (1996).
    • (1996) Nature Struct. Biol. , vol.3 , pp. 1026-1033
    • Ye, X.1    Gorin, A.2    Ellington, A.D.3    Patel, D.J.4
  • 24
    • 0025744320 scopus 로고
    • Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase
    • Rould, M. A., Perona, J. J. & Steitz, T. A. Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase. Nature 352, 213-218 (1991).
    • (1991) Nature , vol.352 , pp. 213-218
    • Rould, M.A.1    Perona, J.J.2    Steitz, T.A.3
  • 25
    • 0028004607 scopus 로고
    • Crystal structure at 1.92 Å 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. & Nagai, K. Crystal structure at 1.92 Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin. Nature 372, 432-438 (1994).
    • (1994) Nature , vol.372 , pp. 432-438
    • Oubridge, C.1    Ito, N.2    Evans, P.R.3    Teo, C.H.4    Nagai, K.5
  • 26
    • 0031951789 scopus 로고    scopus 로고
    • Crystal structure of an RNA aptamer-protein complex at 2.8 Å resolution
    • Convery, M.A. et al. Crystal structure of an RNA aptamer-protein complex at 2.8 Å resolution. Nature Struct Biol. 5, 133-139 (1998).
    • (1998) Nature Struct Biol. , vol.5 , pp. 133-139
    • Convery, M.A.1
  • 27
    • 0029920331 scopus 로고    scopus 로고
    • Specificity of ribonucleoprotein interaction determined by RNA folding during complex formation
    • Allain, F. H. et al. Specificity of ribonucleoprotein interaction determined by RNA folding during complex formation. Nature 380, 646-650 (1996).
    • (1996) Nature , vol.380 , pp. 646-650
    • Allain, F.H.1
  • 28
    • 2242469712 scopus 로고    scopus 로고
    • Structure of the HIV-1 nucleocapsid protein bound to the SL3 stem-loop recognition element of the genomic ψ-RNA packaging signal
    • De Guzman, R. N. et al. Structure of the HIV-1 nucleocapsid protein bound to the SL3 stem-loop recognition element of the genomic ψ-RNA packaging signal. Science, 279, 384-388 (1998).
    • (1998) Science , vol.279 , pp. 384-388
    • De Guzman, R.N.1
  • 29
    • 0029670478 scopus 로고    scopus 로고
    • Identification of D-peptide ligands through mirror-image phage display
    • Schumather, T. N. et al. Identification of D-peptide ligands through mirror-image phage display. Science 271, 1854-1857 (1996).
    • (1996) Science , vol.271 , pp. 1854-1857
    • Schumather, T.N.1
  • 30
    • 0023651444 scopus 로고
    • Oligoribonucleotide synthesis using T7 RNA polymerase and synthetic DNA templates
    • Milligan, J. F., Groebe, D. R., Witherell, G. W. & Uhlenbeck, O. C. Oligoribonucleotide synthesis using T7 RNA polymerase and synthetic DNA templates. Nucleic Acids Res. 15, 8783-8798 (1987).
    • (1987) Nucleic Acids Res. , vol.15 , pp. 8783-8798
    • Milligan, J.F.1    Groebe, D.R.2    Witherell, G.W.3    Uhlenbeck, O.C.4
  • 31
    • 0026611261 scopus 로고
    • 15N labeled RNAs for heteronuctear multi-dimensional NMR studies
    • 15N labeled RNAs for heteronuctear multi-dimensional NMR studies. Nucleic Acids Res. 20, 4507-4513 (1992).
    • (1992) Nucleic Acids Res. , vol.20 , pp. 4507-4513
    • Nikonowicz, E.P.1
  • 32
    • 0026744912 scopus 로고
    • Preparation of isotopically labeled ribonucleotides for multidimensional NMR spectroscopy of RNA
    • Batey, R. T., Inada, M., Kujawinski, E., Puglisi, J. D. & Williamson, J. R. Preparation of isotopically labeled ribonucleotides for multidimensional NMR spectroscopy of RNA. Nucleic Acids Res. 20, 4515-4523 (1992).
    • (1992) Nucleic Acids Res. , vol.20 , pp. 4515-4523
    • Batey, R.T.1    Inada, M.2    Kujawinski, E.3    Puglisi, J.D.4    Williamson, J.R.5
  • 33
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G., Zu, G., Pfeiffer, J. & Bax, A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293 (1995).
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.3    Zu, G.4    Pfeiffer, J.5    Bax, A.6
  • 34
    • 0028885514 scopus 로고
    • Multidimensional heteronuclear NMR experiments for structure determination of isotopically labeled RNA
    • Pardi, A. Multidimensional heteronuclear NMR experiments for structure determination of isotopically labeled RNA. Meths Enz. 261, 350-380 (1995).
    • (1995) Meths Enz. , vol.261 , pp. 350-380
    • Pardi, A.1
  • 36
    • 0002608849 scopus 로고
    • Applications of three- And four-dimensional heteronuclear NMR spectroscopy to protein structure determination
    • Clore, G. M. & Gronenborn, A. M. Applications of three- and four-dimensional heteronuclear NMR spectroscopy to protein structure determination. Prog. NMR Spect. 23, 43-92 (1991).
    • (1991) Prog. NMR Spect. , vol.23 , pp. 43-92
    • Clore, G.M.1    Gronenborn, A.M.2
  • 37
    • 0029437296 scopus 로고
    • Pulsed field gradient multi-dimensional NMR methods for the study of protein structure and dynamics in solution
    • Kay, L. E. Pulsed field gradient multi-dimensional NMR methods for the study of protein structure and dynamics in solution. Prog. NMR Spect. 63, 277-299 (1995).
    • (1995) Prog. NMR Spect. , vol.63 , pp. 277-299
    • Kay, L.E.1
  • 38
    • 0030338440 scopus 로고    scopus 로고
    • NMR pulse schemes for the sequential assignment of arginine side-chain H∈ protons
    • Rao, N. S. et al. NMR pulse schemes for the sequential assignment of arginine side-chain H∈ protons. J. Magn Reson. 113, 272-276 (1996).
    • (1996) J. Magn Reson. , vol.113 , pp. 272-276
    • Rao, N.S.1
  • 40
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. A. & Honig, B. H. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296 (1991).
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.H.3


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