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Volumn 271, Issue 5247, 1996, Pages 345-348

Assembly of a ribonucleoprotein catalyst by tertiary structure capture

Author keywords

[No Author keywords available]

Indexed keywords

CBP2 PROTEIN, S CEREVISIAE; CYTOCHROME B; FUNGAL PROTEIN; FUNGAL RNA; MAGNESIUM; RIBONUCLEOPROTEIN; RIBOZYME; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 0030593036     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.271.5247.345     Document Type: Article
Times cited : (104)

References (43)
  • 1
    • 0003604405 scopus 로고
    • Cold Spnng Harbor Laboratory Press, Cold Spring Harbor, NY
    • R. F. Gesteland and J. F. Atkins, Eds. The RNA World (Cold Spnng Harbor Laboratory Press, Cold Spring Harbor, NY 1993).
    • (1993) The RNA World
    • Gesteland, R.F.1    Atkins, J.F.2
  • 2
    • 0021099817 scopus 로고
    • CBP2, cytochrome b pre-mRNA processing factor 2; P. McGraw and A. Tzagoloff, J. Biol. Chem 258, 9459 (1983); A. Gampel, M. Nishikimi, A Tzagoloff, Mol. Cell Biol. 9, 5424 (1989).
    • (1983) J. Biol. Chem , vol.258 , pp. 9459
    • McGraw, P.1    Tzagoloff, A.2
  • 3
    • 0024345431 scopus 로고
    • CBP2, cytochrome b pre-mRNA processing factor 2; P. McGraw and A. Tzagoloff, J. Biol. Chem 258, 9459 (1983); A. Gampel, M. Nishikimi, A Tzagoloff, Mol. Cell Biol. 9, 5424 (1989).
    • (1989) Mol. Cell Biol. , vol.9 , pp. 5424
    • Gampel, A.1    Nishikimi, M.2    Tzagoloff, A.3
  • 5
    • 0029050588 scopus 로고
    • _, Biochemistry 34, 7728 (1995)
    • (1995) Biochemistry , vol.34 , pp. 7728
  • 6
    • 0023375058 scopus 로고
    • A. Gampel and A. Tzagoloff, Mol. Cell. Biol. 7, 2545 (1987), S Partono and A. S. Lewin, ibid 8, 2562 (1988); A. Gampel and T R. Cech, Genes Dev. 5, 1870 (1991).
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2545
    • Gampel, A.1    Tzagoloff, A.2
  • 7
    • 0024024594 scopus 로고
    • A. Gampel and A. Tzagoloff, Mol. Cell. Biol. 7, 2545 (1987), S Partono and A. S. Lewin, ibid 8, 2562 (1988); A. Gampel and T R. Cech, Genes Dev. 5, 1870 (1991).
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2562
    • Partono, S.1    Lewin, A.S.2
  • 8
    • 0026045993 scopus 로고
    • A. Gampel and A. Tzagoloff, Mol. Cell. Biol. 7, 2545 (1987), S Partono and A. S. Lewin, ibid 8, 2562 (1988); A. Gampel and T R. Cech, Genes Dev. 5, 1870 (1991).
    • (1991) Genes Dev. , vol.5 , pp. 1870
    • Gampel, A.1    Cech, T.R.2
  • 9
    • 4243072631 scopus 로고    scopus 로고
    • note
    • 32P RNA and quantified with a Phosphorlmager (Molecular Dynamics).
  • 10
    • 4243202409 scopus 로고    scopus 로고
    • note
    • -kt), where B is the size of the burst, if any, and A + B gives the endpoint.
  • 11
    • 0011845373 scopus 로고
    • A Pingoud et al., FEBS Lett 30, 1 (1973); J Carey and O. C Uhlenbeck, Biochemistry 2, 2610 (1983); X. Gu and D. V. Santi, ibid. 31, 10295 (1992); K S. Long and D M. Crothers, ibid. 34, 8885 (1995)
    • (1973) FEBS Lett , vol.30 , pp. 1
    • Pingoud, A.1
  • 12
    • 0021111035 scopus 로고
    • A Pingoud et al., FEBS Lett 30, 1 (1973); J Carey and O. C Uhlenbeck, Biochemistry 2, 2610 (1983); X. Gu and D. V. Santi, ibid. 31, 10295 (1992); K S. Long and D M. Crothers, ibid. 34, 8885 (1995)
    • (1983) Biochemistry , vol.2 , pp. 2610
    • Carey, J.1    Uhlenbeck, O.C.2
  • 13
    • 0026474956 scopus 로고
    • A Pingoud et al., FEBS Lett 30, 1 (1973); J Carey and O. C Uhlenbeck, Biochemistry 2, 2610 (1983); X. Gu and D. V. Santi, ibid. 31, 10295 (1992); K S. Long and D M. Crothers, ibid. 34, 8885 (1995)
    • (1992) Biochemistry , vol.31 , pp. 10295
    • Gu, X.1    Santi, D.V.2
  • 14
    • 0029014899 scopus 로고
    • A Pingoud et al., FEBS Lett 30, 1 (1973); J Carey and O. C Uhlenbeck, Biochemistry 2, 2610 (1983); X. Gu and D. V. Santi, ibid. 31, 10295 (1992); K S. Long and D M. Crothers, ibid. 34, 8885 (1995)
    • (1995) Biochemistry , vol.34 , pp. 8885
    • Long, K.S.1    Crothers, D.M.2
  • 15
    • 4243061364 scopus 로고    scopus 로고
    • note
    • Splicing assays were performed as described (4) To measure the CBP2 association rate, CBP2 and pG were added simultaneously to trace concentrations of renatured RNA. For experiments designed to measure the rate of conversion of the folded nbozyme, CBP2 was incubated with RNA for 1 hour to ensure complete binding prior to initiating splicing by addition of pG (final concentration 2 mM)
  • 16
    • 4243089070 scopus 로고    scopus 로고
    • note
    • If the CBP2 concentration is low enough, some step involving the protein will become rate-limiting. However, this concentration must be much smaller than 0.2 nM, the lowest concentration at which we determined the association rate At such concentrations the fraction of RNA found in a complex with CBP2 would be small.
  • 19
    • 33947476119 scopus 로고
    • R. A. Alberty and G G. Hammes, J. Phys. Chem 62, 154 (1957), A Fersht, Enzyme Structure and Mechanism (Freeman, New York, ed. 2, 1985), pp. 150-152, P. H. von Hippel and O. G Berg, J. Biol. Chem. 264, 675 (1989)
    • (1957) J. Phys. Chem , vol.62 , pp. 154
    • Alberty, R.A.1    Hammes, G.G.2
  • 20
    • 0003481596 scopus 로고
    • Freeman, New York, ed. 2
    • R. A. Alberty and G G. Hammes, J. Phys. Chem 62, 154 (1957), A Fersht, Enzyme Structure and Mechanism (Freeman, New York, ed. 2, 1985), pp. 150-152, P. H. von Hippel and O. G Berg, J. Biol. Chem. 264, 675 (1989)
    • (1985) Enzyme Structure and Mechanism , pp. 150-152
    • Fersht, A.1
  • 21
    • 0024531901 scopus 로고
    • R. A. Alberty and G G. Hammes, J. Phys. Chem 62, 154 (1957), A Fersht, Enzyme Structure and Mechanism (Freeman, New York, ed. 2, 1985), pp. 150-152, P. H. von Hippel and O. G Berg, J. Biol. Chem. 264, 675 (1989)
    • (1989) J. Biol. Chem. , vol.264 , pp. 675
    • Von Hippel, P.H.1    Berg, O.G.2
  • 22
    • 4243054607 scopus 로고    scopus 로고
    • note
    • Dissociation rates were determined by incubating renatured RNA and CBP2 for 1 hour to ensure complete binding and subsequently trapping any protein that dissociated by addition of heparin to a final concentration of 20 to 500 μg/ml Fraction RNA bound was analyzed by filter binding (4). Dissociation rates were independent of heparin concentration. End-points were obtained from reactions in which the heparin was added before CBP2
  • 23
    • 4243193346 scopus 로고    scopus 로고
    • note
    • -1) = 30 pM.
  • 26
    • 0015497428 scopus 로고
    • P E. Cole and D. M. Crothers, Biochemistry 11, 4368 (1972); D. M. Crothers, P. E. Cole, C. W. Hilbers, R. G. Schulman, J. Mol Biol. 87, 63 (1974).
    • (1972) Biochemistry , vol.11 , pp. 4368
    • Cole, P.E.1    Crothers, D.M.2
  • 28
  • 29
    • 0026580844 scopus 로고
    • P. C Bevilacqua, R Kierzek, K A. Johnson, D. H Turner, Science 258, 1355 (1992); D. Herschlag, Biochemistry 31, 1386 (1992); Y. Li, P. C. Bevilacqua, D Mathews, D H Turner, ibid. 34, 14394 (1995)
    • (1992) Biochemistry , vol.31 , pp. 1386
    • Herschlag, D.1
  • 30
    • 0028824549 scopus 로고
    • P. C Bevilacqua, R Kierzek, K A. Johnson, D. H Turner, Science 258, 1355 (1992); D. Herschlag, Biochemistry 31, 1386 (1992); Y. Li, P. C. Bevilacqua, D Mathews, D H Turner, ibid. 34, 14394 (1995)
    • (1995) Biochemistry , vol.34 , pp. 14394
    • Li, Y.1    Bevilacqua, P.C.2    Mathews, D.3    Turner, D.H.4
  • 32
    • 0028936110 scopus 로고
    • CYT18, mitochrondnal tyrosyl tRNA synthetase which facilitates splicing of group I introns in Neurospora crassa; R. J. Saldanha, S. S. Patel, R Surendran, J C Lee, A. M Lambowitz [ibid. 34, 1275 (1995)] observed rapid formation of an initial CYT18 pre-nbosomal RNA complex characterized by a second-order rate constant, in contrast to our observations with bl5 RNA. These data emphasize that there exist alternate pathways for simple RNP assembly.
    • (1995) Biochemistry , vol.34 , pp. 1275
    • Saldanha, R.J.1    Patel, S.S.2    Surendran, R.3    Lee, J.C.4    Lambowitz, A.M.5
  • 33
    • 0029286628 scopus 로고
    • T. Powers and H. F. Noller, RNA 1, 194 (1995); V. Mandiyan, S. J. Tumminia, J. S. Wall, J. F. Hainfield, M. Boublik, J. Mol. Biol. 210, 323 (1989).
    • (1995) RNA , vol.1 , pp. 194
    • Powers, T.1    Noller, H.F.2
  • 36
    • 0016153699 scopus 로고
    • M. Nomura, S. Mizushima, M. Ozaki, P. Traub, C V. Lowry, Cold Spring Harbor Symp. Quant. Biol. 34, 49 (1969); W. A Held, B. Ballou, S. Mizushima, M. Nomura, J. Biol. Chem. 249, 3103 (1974); T. Powers, G. Daubresse, H. F. Noller, J Mol. Biol. 232, 362 (1993)
    • (1974) J. Biol. Chem. , vol.249 , pp. 3103
    • Held, W.A.1    Ballou, B.2    Mizushima, S.3    Nomura, M.4
  • 37
    • 0027171312 scopus 로고
    • M. Nomura, S. Mizushima, M. Ozaki, P. Traub, C V. Lowry, Cold Spring Harbor Symp. Quant. Biol. 34, 49 (1969); W. A Held, B. Ballou, S. Mizushima, M. Nomura, J. Biol. Chem. 249, 3103 (1974); T. Powers, G. Daubresse, H. F. Noller, J Mol. Biol. 232, 362 (1993)
    • (1993) J Mol. Biol. , vol.232 , pp. 362
    • Powers, T.1    Daubresse, G.2    Noller, H.F.3
  • 38
    • 0015793219 scopus 로고
    • W A. Held and M Nomura, Biochemistry 12, 3273 (1973). Assembly of the large subunit of the ribosome involves two rate-limiting unimolecular transitions [G. Sieber and K H. Nierhaus, ibid 17, 3505 (1978)].
    • (1973) Biochemistry , vol.12 , pp. 3273
    • Held, W.A.1    Nomura, M.2
  • 39
    • 0017897638 scopus 로고
    • W A. Held and M Nomura, Biochemistry 12, 3273 (1973). Assembly of the large subunit of the ribosome involves two rate-limiting unimolecular transitions [G. Sieber and K H. Nierhaus, ibid 17, 3505 (1978)].
    • (1978) Biochemistry , vol.17 , pp. 3505
    • Sieber, G.1    Nierhaus, K.H.2
  • 40
    • 0025678737 scopus 로고
    • F Michel and E Westhof, J Mol. Biol. 216, 585 (1990); L. Jaeger, E. Westhof, F. Michel, ibid 221, 1153 (1991).
    • (1990) J Mol. Biol. , vol.216 , pp. 585
    • Michel, F.1    Westhof, E.2
  • 43
    • 4243056894 scopus 로고    scopus 로고
    • note
    • We thank P. Bevilacqua for discussion. Supported by a fellowship from the Jane Coffin Childs Memorial Fund for Medical Research (K.M.W.) and by the Howard Hughes Medical Institute (T.R.C.).


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