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Volumn 5, Issue 11, 1999, Pages 1419-1429

Structure of the phylogenetically most conserved domain of SRP RNA

Author keywords

4.5S RNA; Complete relaxation matrix analysis; NMR; RNA structure; RNA protein recognition; Signal recognition particle

Indexed keywords

RNA; SIGNAL RECOGNITION PARTICLE;

EID: 0032709518     PISSN: 13558382     EISSN: None     Source Type: Journal    
DOI: 10.1017/S1355838299991458     Document Type: Article
Times cited : (53)

References (42)
  • 1
    • 0028857598 scopus 로고
    • Association of biomolecular systems via pulsed field gradient NMR self-diffusion measurements
    • Altieri AS, Hinton DP, Byrd RA. 1995. Association of biomolecular systems via pulsed field gradient NMR self-diffusion measurements. J Am Chem Soc 117:7566-7567.
    • (1995) J Am Chem Soc , vol.117 , pp. 7566-7567
    • Altieri, A.S.1    Hinton, D.P.2    Byrd, R.A.3
  • 2
    • 0023443260 scopus 로고
    • Evidence for an extended 7SL RNAstructure in the signal recognition particle
    • Andrews DW, Walter P, Ottensmeyer FP. 1987. Evidence for an extended 7SL RNAstructure in the signal recognition particle. EMBO J 6:3471-3477.
    • (1987) EMBO J , vol.6 , pp. 3471-3477
    • Andrews, D.W.1    Walter, P.2    Ottensmeyer, F.P.3
  • 3
    • 0028803380 scopus 로고
    • Preparation of isotopically enriched RNAs for heteronuclear NMR
    • Batey RT, Battiste JL, Williamson JR. 1995. Preparation of isotopically enriched RNAs for heteronuclear NMR. Methods Enzymol 261:300-322.
    • (1995) Methods Enzymol , vol.261 , pp. 300-322
    • Batey, R.T.1    Battiste, J.L.2    Williamson, J.R.3
  • 4
    • 5144233105 scopus 로고
    • MLEV-17-based 2D homonuclear magnetization transfer spectroscopy
    • Bax A, Davies DG. 1985. MLEV-17-based 2D homonuclear magnetization transfer spectroscopy. J Magn Reson 65:355-360.
    • (1985) J Magn Reson , vol.65 , pp. 355-360
    • Bax, A.1    Davies, D.G.2
  • 5
    • 0027288333 scopus 로고
    • Functional substitution of the signal recognition particle 54-kDa subunit by its Escherichia coli homolog
    • Bernstein HD, Zopf D, Freymann DM, Walter P. 1993. Functional substitution of the signal recognition particle 54-kDa subunit by its Escherichia coli homolog. Proc Natl Acad Sci USA 90:5229-5233.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 5229-5233
    • Bernstein, H.D.1    Zopf, D.2    Freymann, D.M.3    Walter, P.4
  • 6
    • 0031547961 scopus 로고    scopus 로고
    • Solution structure of the conserved 16 S-like ribosomal RNA UGAA tetraloop
    • Butcher SE, Dieckmann T, Feigon J. 1997. Solution structure of the conserved 16 S-like ribosomal RNA UGAA tetraloop. J Mol Biol 260:348-358.
    • (1997) J Mol Biol , vol.260 , pp. 348-358
    • Butcher, S.E.1    Dieckmann, T.2    Feigon, J.3
  • 8
    • 0001216964 scopus 로고    scopus 로고
    • A second generation force field for the simulation of proteins, nucleic acids, and organic molecules
    • Cornell W, Cieplak P, Bayly CI, Gould IR, Kollman PA. 1996. A second generation force field for the simulation of proteins, nucleic acids, and organic molecules. J Am Chem Soc 118:2309-2309.
    • (1996) J Am Chem Soc , vol.118 , pp. 2309-2309
    • Cornell, W.1    Cieplak, P.2    Bayly, C.I.3    Gould, I.R.4    Kollman, P.A.5
  • 9
    • 0344506834 scopus 로고
    • San Francisco, California: University of California, San Francisco
    • Day M, Kneller DG. 1992. Striker. San Francisco, California: University of California, San Francisco.
    • (1992) Striker
    • Day, M.1    Kneller, D.G.2
  • 13
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Güntert P, Mumenthaler C, Wüthrich K. 1997. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J Mol Biol 273:283-298.
    • (1997) J Mol Biol , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 14
    • 0024352634 scopus 로고
    • Measurement of translational motion by pulse-gradient spin-echo NMR
    • Haner RL, Schleich T. 1989. Measurement of translational motion by pulse-gradient spin-echo NMR. Methods Enzymol 176:418-445.
    • (1989) Methods Enzymol , vol.176 , pp. 418-445
    • Haner, R.L.1    Schleich, T.2
  • 15
    • 0027444622 scopus 로고
    • An NMR study of the HIV-1 TAR element hairpin
    • Jaeger JA, Tinoco I Jr. 1993. An NMR study of the HIV-1 TAR element hairpin. Biochemistry 32:12522-12530.
    • (1993) Biochemistry , vol.32 , pp. 12522-12530
    • Jaeger, J.A.1    Tinoco J. I2
  • 17
    • 0032563163 scopus 로고    scopus 로고
    • Crystal structure of the signal sequence binding subunit of the signal recognition particle
    • Keenan RJ, Freymann DM, Stroud R, Walter P. 1998. Crystal structure of the signal sequence binding subunit of the signal recognition particle. Cell 94:181-191.
    • (1998) Cell , vol.94 , pp. 181-191
    • Keenan, R.J.1    Freymann, D.M.2    Stroud, R.3    Walter, P.4
  • 18
    • 15844397001 scopus 로고    scopus 로고
    • Identification of a region of Bacillus subtilis ffh, a homolog of mammalian SRP54 protein that is essential for binding to small cytoplasmic RNA
    • Kurita K, Honda K, Suzuma S, Takamatsu H, Nakamura K, Yamane K. 1996. Identification of a region of Bacillus subtilis ffh, a homolog of mammalian SRP54 protein that is essential for binding to small cytoplasmic RNA. J Biol Chem 271:13140-13146.
    • (1996) J Biol Chem , vol.271 , pp. 13140-13146
    • Kurita, K.1    Honda, K.2    Suzuma, S.3    Takamatsu, H.4    Nakamura, K.5    Yamane, K.6
  • 19
    • 0031241810 scopus 로고    scopus 로고
    • Measurement of diffusion constants for nucleic acids by NMR
    • Lapham J, Rife JP, Moore PB, Crothers DM. 1997. Measurement of diffusion constants for nucleic acids by NMR. J Biomol NMR 10:255-262.
    • (1997) J Biomol NMR , vol.10 , pp. 255-262
    • Lapham, J.1    Rife, J.P.2    Moore, P.B.3    Crothers, D.M.4
  • 20
    • 0031866668 scopus 로고    scopus 로고
    • The Signal Recognition Particle Database (SRPDB)
    • Larsen N, Samuelsson T, Zwieb C. 1998. The Signal Recognition Particle Database (SRPDB). Nucleic Acids Res 26:177-178.
    • (1998) Nucleic Acids Res , vol.26 , pp. 177-178
    • Larsen, N.1    Samuelsson, T.2    Zwieb, C.3
  • 21
    • 33646817966 scopus 로고
    • Paris: Laboratory for Theoretical Biochemistry, Centre Nationale pour la Récherche Scientifique
    • Lavery R, Sklenar H. 1990. CURVES 3.0. Paris: Laboratory for Theoretical Biochemistry, Centre Nationale pour la Récherche Scientifique.
    • (1990) CURVES 3.0
    • Lavery, R.1    Sklenar, H.2
  • 24
    • 0029805727 scopus 로고    scopus 로고
    • Structure of 4.5S RNA in the signal recognition particle of Escherichia coli as studied by enzymatic and chemical probing
    • Lentzen G, Moine H, Ehresmann B, Wintermeyer W. 1996. Structure of 4.5S RNA in the signal recognition particle of Escherichia coli as studied by enzymatic and chemical probing. RNA 2:244-253.
    • (1996) RNA , vol.2 , pp. 244-253
    • Lentzen, G.1    Moine, H.2    Ehresmann, B.3    Wintermeyer, W.4
  • 25
    • 0344937692 scopus 로고
    • San Francisco, California: University of California, San Francisco
    • Liu H, Borgias B, Kumar A, James TL. 1990, 1994. MARDIGRAS. San Francisco, California: University of California, San Francisco.
    • (1990) MARDIGRAS
    • Liu, H.1    Borgias, B.2    Kumar, A.3    James, T.L.4
  • 26
    • 0029450044 scopus 로고
    • Interproton distance bounds from two-dimensional NOE intensities - Effect of experimental noise and peak integration errors
    • Liu H, Spielmann HP, Ulyanov NB, Wemmer DE, James TL. 1995. Interproton distance bounds from two-dimensional NOE intensities - effect of experimental noise and peak integration errors. J Biomol NMR 6:390-402.
    • (1995) J Biomol NMR , vol.6 , pp. 390-402
    • Liu, H.1    Spielmann, H.P.2    Ulyanov, N.B.3    Wemmer, D.E.4    James, T.L.5
  • 27
    • 0030117290 scopus 로고    scopus 로고
    • Correcting NOESY cross-peak intensities for partial relaxation effects enabling accurate distance information
    • Liu H, Tonelli M, James TL. 1996. Correcting NOESY cross-peak intensities for partial relaxation effects enabling accurate distance information. J Magn Reson 111:85-89.
    • (1996) J Magn Reson , vol.111 , pp. 85-89
    • Liu, H.1    Tonelli, M.2    James, T.L.3
  • 29
    • 0028121697 scopus 로고
    • Correlation of adenine H2/H8 resonances in uniformly 13C-labeled RNAs by 2D HCCH-TOCSY: A new tool for 1H assignment
    • Marino JP, Prestegard JH, Crothers DM. 1994. Correlation of adenine H2/H8 resonances in uniformly 13C-labeled RNAs by 2D HCCH-TOCSY: A new tool for 1H assignment. J Am Chem Soc 116:2205-2206.
    • (1994) J Am Chem Soc , vol.116 , pp. 2205-2206
    • Marino, J.P.1    Prestegard, J.H.2    Crothers, D.M.3
  • 30
    • 45249127991 scopus 로고
    • Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins
    • Marion D, Ikura M, Tschudin R, Bax A. 1989. Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins. J Magn Reson 85:393-399.
    • (1989) J Magn Reson , vol.85 , pp. 393-399
    • Marion, D.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 31
    • 0024819449 scopus 로고
    • Synthesis of small RNAs using T7 RNA polymerase
    • Milligan JF, Uhlenbeck OC. 1989. Synthesis of small RNAs using T7 RNA polymerase. Methods Enzymol 180:51-62.
    • (1989) Methods Enzymol , vol.180 , pp. 51-62
    • Milligan, J.F.1    Uhlenbeck, O.C.2
  • 32
    • 0027199672 scopus 로고
    • An efficient procedure for assignment of the proton, carbon, and nitrogen resonances in C-13/N-15 labeled nucleic acids
    • Nikonowicz EP, Pardi A. 1993. An efficient procedure for assignment of the proton, carbon, and nitrogen resonances in C-13/N-15 labeled nucleic acids. J Mol Biol 232:1141-1156.
    • (1993) J Mol Biol , vol.232 , pp. 1141-1156
    • Nikonowicz, E.P.1    Pardi, A.2
  • 34
    • 0030832397 scopus 로고    scopus 로고
    • Co-translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor
    • Powers T, Walter P. 1997. Co-translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor. EMBO J 16:4880-4886.
    • (1997) EMBO J , vol.16 , pp. 4880-4886
    • Powers, T.1    Walter, P.2
  • 35
    • 44049118414 scopus 로고
    • A constant-time 2D overBodenhausen experiment for inverse correlation of isotopically enriched species
    • Santoro J, King GC. 1992. A constant-time 2D overBodenhausen experiment for inverse correlation of isotopically enriched species. J Magn Reson 97:202-207.
    • (1992) J Magn Reson , vol.97 , pp. 202-207
    • Santoro, J.1    King, G.C.2
  • 37
    • 0344506829 scopus 로고
    • How to get accurate solution structures of double-helical fragments using NMR and restrained molecular dynamics
    • Schmitz U, James TL. 1995. How to get accurate solution structures of double-helical fragments using NMR and restrained molecular dynamics. Methods Enzymol 261:1-43.
    • (1995) Methods Enzymol , vol.261 , pp. 1-43
    • Schmitz, U.1    James, T.L.2
  • 39
    • 12044251259 scopus 로고
    • Solvent suppression with symmetrically-shifted pulses
    • Smallcombe SH. 1993. Solvent suppression with symmetrically-shifted pulses. J Am Chem Soc 115:4776-4785.
    • (1993) J Am Chem Soc , vol.115 , pp. 4776-4785
    • Smallcombe, S.H.1
  • 40
    • 0031472242 scopus 로고    scopus 로고
    • The E. Coli signal recognition particle is required for the insertion of a subset of inner membrane proteins
    • Ulbrandt ND, Newitt JA, Bernstein HD. 1997. The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins. Cell 88:187-196.
    • (1997) Cell , vol.88 , pp. 187-196
    • Ulbrandt, N.D.1    Newitt, J.A.2    Bernstein, H.D.3
  • 41
    • 0028170807 scopus 로고
    • Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane
    • Walter P, Johnson AE. 1994. Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu Rev Cell Biol 10:87-119.
    • (1994) Annu Rev Cell Biol , vol.10 , pp. 87-119
    • Walter, P.1    Johnson, A.E.2
  • 42
    • 0031310942 scopus 로고    scopus 로고
    • Domain interactions in E. Coli SRP: Stabilization of M domain by RNA is required for effective signal sequence modulation of NG domain
    • Zheng N, Gierasch LM. 1997. Domain interactions in E. coli SRP: Stabilization of M domain by RNA is required for effective signal sequence modulation of NG domain. Mol Cell 1:79-87.
    • (1997) Mol Cell , vol.1 , pp. 79-87
    • Zheng, N.1    Gierasch, L.M.2


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