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Volumn 295, Issue , 1998, Pages 379-402

Following the folding of RNA with time-resolved synchrotron X-ray footprinting

Author keywords

[No Author keywords available]

Indexed keywords

RNA;

EID: 0032319210     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(98)95050-9     Document Type: Article
Times cited : (71)

References (51)
  • 3
    • 0003017978 scopus 로고
    • (R. F. Gesteland and J. F. Atkins, eds.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Reviewed by T. R. Cech, "The RNA World" (R. F. Gesteland and J. F. Atkins, eds.), p. 239. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, 1993.
    • (1993) The RNA World , pp. 239
    • Cech, T.R.1
  • 6
    • 0018199224 scopus 로고
    • D. Galas and A. Schmitz, Nucleic Acids Rev. 5, 3157 (1978); A. Schmitz and D. Galas, Nucleic Acids Res. 6, 111 (1979).
    • (1978) Nucleic Acids Rev. , vol.5 , pp. 3157
    • Galas, D.1    Schmitz, A.2
  • 7
  • 10
    • 0022437260 scopus 로고
    • M. Brenowitz, D. F. Senear, M. A. Shea, and G. K. Ackers, Methods Enzymol. 130, 132 (1986); M. Brenowitz, D. F. Senear, M. A. Shea, and G. K. Ackers, Proc. Nat. Acad. Sci. U.S.A. 83, 8462 (1986); K. S. Koblan, D. L. Bain, D. Beckett, M. A. Shea, and G. K. Ackers, Methods Enzymol. 210, 405 (1982); D. F. Senear and D. W. Bolen, Methods Enzymol. 210, 463 (1992).
    • (1986) Methods Enzymol. , vol.130 , pp. 132
    • Brenowitz, M.1    Senear, D.F.2    Shea, M.A.3    Ackers, G.K.4
  • 11
    • 0000660149 scopus 로고
    • M. Brenowitz, D. F. Senear, M. A. Shea, and G. K. Ackers, Methods Enzymol. 130, 132 (1986); M. Brenowitz, D. F. Senear, M. A. Shea, and G. K. Ackers, Proc. Nat. Acad. Sci. U.S.A. 83, 8462 (1986); K. S. Koblan, D. L. Bain, D. Beckett, M. A. Shea, and G. K. Ackers, Methods Enzymol. 210, 405 (1982); D. F. Senear and D. W. Bolen, Methods Enzymol. 210, 463 (1992).
    • (1986) Proc. Nat. Acad. Sci. U.S.A. , vol.83 , pp. 8462
    • Brenowitz, M.1    Senear, D.F.2    Shea, M.A.3    Ackers, G.K.4
  • 12
    • 0026769027 scopus 로고
    • M. Brenowitz, D. F. Senear, M. A. Shea, and G. K. Ackers, Methods Enzymol. 130, 132 (1986); M. Brenowitz, D. F. Senear, M. A. Shea, and G. K. Ackers, Proc. Nat. Acad. Sci. U.S.A. 83, 8462 (1986); K. S. Koblan, D. L. Bain, D. Beckett, M. A. Shea, and G. K. Ackers, Methods Enzymol. 210, 405 (1982); D. F. Senear and D. W. Bolen, Methods Enzymol. 210, 463 (1992).
    • (1982) Methods Enzymol. , vol.210 , pp. 405
    • Koblan, K.S.1    Bain, D.L.2    Beckett, D.3    Shea, M.A.4    Ackers, G.K.5
  • 13
    • 0026653485 scopus 로고
    • M. Brenowitz, D. F. Senear, M. A. Shea, and G. K. Ackers, Methods Enzymol. 130, 132 (1986); M. Brenowitz, D. F. Senear, M. A. Shea, and G. K. Ackers, Proc. Nat. Acad. Sci. U.S.A. 83, 8462 (1986); K. S. Koblan, D. L. Bain, D. Beckett, M. A. Shea, and G. K. Ackers, Methods Enzymol. 210, 405 (1982); D. F. Senear and D. W. Bolen, Methods Enzymol. 210, 463 (1992).
    • (1992) Methods Enzymol. , vol.210 , pp. 463
    • Senear, D.F.1    Bolen, D.W.2
  • 22
    • 0020510997 scopus 로고
    • G. K. Ackers, A. D. Johnson, and M. A. Shea, Proc. Natl. Acad. Sci. U.S.A. 79, 1129 (1982); G. K. Ackers, M. A. Shea, and F. R. Smith, J. Mol. Biol. 170, 223 (1983).
    • (1983) J. Mol. Biol. , vol.170 , pp. 223
    • Ackers, G.K.1    Shea, M.A.2    Smith, F.R.3
  • 26
    • 0026807036 scopus 로고
    • J. J. Hayes, L. Kam, and T. D. Tullius, Methods Enzymol. 186, 545 (1990); M. A. Price and T. D. Tullius, Methods Enzymol. 212, 194 (1992).
    • (1992) Methods Enzymol. , vol.212 , pp. 194
    • Price, M.A.1    Tullius, T.D.2
  • 28
    • 0025023607 scopus 로고
    • D. C. Calender and T. R. Cech, Biochemistry 29, 1355 (1990); D. C. Calender and T. R. Cech, Science 251, 401 (1991).
    • (1990) Biochemistry , vol.29 , pp. 1355
    • Calender, D.C.1    Cech, T.R.2
  • 29
    • 0025963132 scopus 로고
    • D. C. Calender and T. R. Cech, Biochemistry 29, 1355 (1990); D. C. Calender and T. R. Cech, Science 251, 401 (1991).
    • (1991) Science , vol.251 , pp. 401
    • Calender, D.C.1    Cech, T.R.2
  • 34
    • 84934485247 scopus 로고
    • (F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl, eds.), Wiley, New York
    • M. Brenowitz and D. F. Senear, in "Current Protocols in Molecular Biology" (F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl, eds.), Wiley, New York, 1989; M. Brenowitz, D, F. Senear, E. Jamison, and D. D. DalmaWeiszhausz, in "Footprinting Techniques for Studying Nucleic Acid-Protein Complexes" (A. Revzin, ed.), p. 1. Academic Press, New York, 1993.
    • (1989) Current Protocols in Molecular Biology
    • Brenowitz, M.1    Senear, D.F.2
  • 37
    • 13044279740 scopus 로고
    • (A. Primer and H. Winick, eds.), World Scientific, Singapore
    • H. Winick, in "Synchrotron Radiation Sources" (A. Primer and H. Winick, eds.), p. 1. World Scientific, Singapore, 1994.
    • (1994) Synchrotron Radiation Sources , pp. 1
    • Winick, H.1
  • 39
    • 85030369109 scopus 로고
    • (Offprint 1173) Scientific American, April and references cited therein
    • R. J. Britten and D. E. Kohne, "Repeated Segments of DNA" (Offprint 1173) Scientific American, April and references cited therein, 1970.
    • (1970) Repeated Segments of DNA
    • Britten, R.J.1    Kohne, D.E.2
  • 41
    • 0022961855 scopus 로고
    • J. Langowski, C. Urbanke, and E. Schuppe, Anal. Biochem. 142, 91 (1984); K. A. Johnson, Methods Enzymol 134, 677 (1986).
    • (1986) Methods Enzymol , vol.134 , pp. 677
    • Johnson, K.A.1
  • 42
    • 85030366335 scopus 로고    scopus 로고
    • note
    • Absorption of nucleic acids to the walls of the tubes has only been observed for sample reaction times greater than 2 min. The acquisition of time points on the order of minutes is not required for progress curves with millisecond time scales. However, because parts of the Tetrahymena ribozyme fold with time scales on the order of minutes, the acquisition of slow folding data with the rapid mixer is desirable in order to assure the consistency of the fast and slow folding progress curves. Unpublished data have established the consistency of manual and rapid mixing methods for reactions such as the slow folding of the core of the Tetrahymena ribozyme.
  • 43
    • 85030368430 scopus 로고    scopus 로고
    • note
    • Beam scattering can also be minimized by the insertion of an argon-filled or vacuum "flight tube" in the path of the beamline in situations where the presence of other equipment precludes placing the shutter and mixer close to the front port.
  • 46
    • 85030361301 scopus 로고    scopus 로고
    • note
    • The sample holder can be a temperature-regulated block in order to conduct experiments at temperatures other than ambient.
  • 47
    • 85030360523 scopus 로고    scopus 로고
    • The -OH cleavage reaction may need to be quenched depending on the time scale of the transition, see earlier. Control experiments for the RNA folding reaction conducted with and without a thiourea quench solution in syringe B were indistinguishable (unpublished data)
    • The -OH cleavage reaction may need to be quenched depending on the time scale of the transition, see earlier. Control experiments for the RNA folding reaction conducted with and without a thiourea quench solution in syringe B were indistinguishable (unpublished data).
  • 48
    • 85030362895 scopus 로고    scopus 로고
    • note
    • 9
  • 49
    • 85030361741 scopus 로고    scopus 로고
    • note
    • 9
  • 50
    • 85030360283 scopus 로고    scopus 로고
    • note
    • The ImageQuant software is integrated with the Microsoft spreadsheet. Other analysis programs can be substituted through the implementation of the appropriate export and conversion functions.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.