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Volumn 6, Issue 6, 2000, Pages 795-813

An unconventional origin of metal-ion rescue and inhibition in the Tetrahymena group I ribozyme reaction

Author keywords

Chemical modification; Enzymatic catalysis; Metal ion; Ribozyme

Indexed keywords

CALCIUM ION; MAGNESIUM ION; MANGANESE; METAL ION; OLIGONUCLEOTIDE; PHOSPHOROTHIOIC ACID; RIBOZYME;

EID: 0034081812     PISSN: 13558382     EISSN: None     Source Type: Journal    
DOI: 10.1017/S1355838200000649     Document Type: Article
Times cited : (49)

References (77)
  • 1
    • 0028290073 scopus 로고
    • Small molecule analogs of phospholipid-metal ion binding sites: Potentiometric and spectroscopic studies of Mg(II) and Ca(II) complexes of cyclohexane-1,2,4,-triol trisphosphates
    • Amburgey JC, Huh N-M, Pedersen LG, Hiskey RG. 1994. Small molecule analogs of phospholipid-metal ion binding sites: Potentiometric and spectroscopic studies of Mg(II) and Ca(II) complexes of cyclohexane-1,2,4,-triol trisphosphates. Bioorg Chem 22:198-215.
    • (1994) Bioorg Chem , vol.22 , pp. 198-215
    • Amburgey, J.C.1    Huh, N.-M.2    Pedersen, L.G.3    Hiskey, R.G.4
  • 2
    • 0029903452 scopus 로고    scopus 로고
    • The ion-induced folding of the hammerhead ribozyme: Core sequence changes that perturb folding into the active conformation
    • Bassi GS, Murchie AIH, Lilley DMJ. 1996. The ion-induced folding of the hammerhead ribozyme: Core sequence changes that perturb folding into the active conformation. RNA 2:756-768.
    • (1996) RNA , vol.2 , pp. 756-768
    • Bassi, G.S.1    Murchie, A.I.H.2    Lilley, D.M.J.3
  • 3
    • 0032707136 scopus 로고    scopus 로고
    • Thiophilic metal ion rescue of phosphorothioate interference within the Tetrahymena ribozyme P4-P6 domain
    • Basu S, Strobel SA. 1999. Thiophilic metal ion rescue of phosphorothioate interference within the Tetrahymena ribozyme P4-P6 domain. RNA 5:1399-1407.
    • (1999) RNA , vol.5 , pp. 1399-1407
    • Basu, S.1    Strobel, S.A.2
  • 5
    • 0026678180 scopus 로고
    • Dynamics of ribozyme binding of substrate revealed by fluorescence-detected stopped-flow methods
    • Bevilacqua PC, Kierzek R, Johnson KA, Turner DH. 1992. Dynamics of ribozyme binding of substrate revealed by fluorescence-detected stopped-flow methods. Science 258:1355-1358.
    • (1992) Science , vol.258 , pp. 1355-1358
    • Bevilacqua, P.C.1    Kierzek, R.2    Johnson, K.A.3    Turner, D.H.4
  • 6
    • 0031836886 scopus 로고    scopus 로고
    • A critical-evaluation of metal-promoted Klenow 3′ → 5′ exonuclease activity: Calorimetric and kinetic analyses support a one-metal-ion mechanism
    • Black CB, Cowan JA. 1998. A critical-evaluation of metal-promoted Klenow 3′ → 5′ exonuclease activity: Calorimetric and kinetic analyses support a one-metal-ion mechanism. J Biol Inorg Chem 2:292-299.
    • (1998) J Biol Inorg Chem , vol.2 , pp. 292-299
    • Black, C.B.1    Cowan, J.A.2
  • 7
    • 0032571245 scopus 로고    scopus 로고
    • Structural principles for the inhibition of the 3′ → 5′ exonuclease activity of Escherichia coli DNA polymerase I by phosphorothioates
    • Brautigam CA, Steitz TA. 1998. Structural principles for the inhibition of the 3′ → 5′ exonuclease activity of Escherichia coli DNA polymerase I by phosphorothioates. J Mol Biol 277:363-377.
    • (1998) J Mol Biol , vol.277 , pp. 363-377
    • Brautigam, C.A.1    Steitz, T.A.2
  • 9
    • 0018287755 scopus 로고
    • A study of the mechanism of DNA polymerase I from E. coli with diastereomeric phosphorothioate analogs of deoxyadenosine triphosphate
    • Burgers PMJ, Eckstein F. 1979. A study of the mechanism of DNA polymerase I from E. coli with diastereomeric phosphorothioate analogs of deoxyadenosine triphosphate. J Biol Chem 254:6889-6893.
    • (1979) J Biol Chem , vol.254 , pp. 6889-6893
    • Burgers, P.M.J.1    Eckstein, F.2
  • 10
    • 0019321490 scopus 로고
    • Structure of the metal-nucleotide complex in the creatine kinase reaction
    • Burgers PMJ, Eckstein F. 1980. Structure of the metal-nucleotide complex in the creatine kinase reaction. J Biol Chem 255:8229-8233.
    • (1980) J Biol Chem , vol.255 , pp. 8229-8233
    • Burgers, P.M.J.1    Eckstein, F.2
  • 11
    • 0030587890 scopus 로고    scopus 로고
    • Metal-binding sites in the major groove of a large ribozyme domain
    • Cate JH, Doudna JA. 1996. Metal-binding sites in the major groove of a large ribozyme domain. Structure 4:1221-1229.
    • (1996) Structure , vol.4 , pp. 1221-1229
    • Cate, J.H.1    Doudna, J.A.2
  • 13
    • 0030929889 scopus 로고    scopus 로고
    • A magnesium ion core at the heart of a ribozyme domain
    • Cate JH, Hanna RL, Doudna JA. 1997. A magnesium ion core at the heart of a ribozyme domain. Nat Struct Biol 7:553-558.
    • (1997) Nat Struct Biol , vol.7 , pp. 553-558
    • Cate, J.H.1    Hanna, R.L.2    Doudna, J.A.3
  • 14
    • 0002754552 scopus 로고    scopus 로고
    • Group I ribozymes: Substrate recognition, catalytic strategies, and comparative mechanistic analysis
    • Cech TR, Herschlag D. 1996. Group I ribozymes: Substrate recognition, catalytic strategies, and comparative mechanistic analysis. Nucleic Acids Mol Biol 10:1-17.
    • (1996) Nucleic Acids Mol Biol , vol.10 , pp. 1-17
    • Cech, T.R.1    Herschlag, D.2
  • 15
    • 0025963132 scopus 로고
    • Visualizing the higher order folding of a catalytic RNA molecule
    • Celander DW, Cech TR. 1991. Visualizing the higher order folding of a catalytic RNA molecule. Science 251:401-407.
    • (1991) Science , vol.251 , pp. 401-407
    • Celander, D.W.1    Cech, T.R.2
  • 16
    • 0031027138 scopus 로고    scopus 로고
    • 2+ coordinated to the pro-Rp oxygen of the scissle bond
    • 2+ coordinated to the pro-Rp oxygen of the scissle bond. Biochemistry 36:2425-2438.
    • (1997) Biochemistry , vol.36 , pp. 2425-2438
    • Chen, Y.1    Li, X.2    Gegenheimer, P.3
  • 17
    • 0027247579 scopus 로고
    • Metal coordination sites that contribute to structure and catalysis in the group I intron from Tetrahymena
    • Christian EL, Yarus M. 1993. Metal coordination sites that contribute to structure and catalysis in the group I intron from Tetrahymena. Biochemistry 32:4475-4480.
    • (1993) Biochemistry , vol.32 , pp. 4475-4480
    • Christian, E.L.1    Yarus, M.2
  • 18
    • 0019888404 scopus 로고
    • Structures of the monovalent and divalent metal nucleotide complexes in the myosin ATPase
    • Connolly BA, Eckstein F. 1981. Structures of the monovalent and divalent metal nucleotide complexes in the myosin ATPase. J Biol Chem 256:9450-9456.
    • (1981) J Biol Chem , vol.256 , pp. 9450-9456
    • Connolly, B.A.1    Eckstein, F.2
  • 19
    • 0030856333 scopus 로고    scopus 로고
    • Metals, motifs, and recognition in the crystal structure of a 5S rRNA domain
    • Correll CC, Freeborn B, Moore PB, Steitz TA. 1997. Metals, motifs, and recognition in the crystal structure of a 5S rRNA domain. Cell 91:705-712.
    • (1997) Cell , vol.91 , pp. 705-712
    • Correll, C.C.1    Freeborn, B.2    Moore, P.B.3    Steitz, T.A.4
  • 20
    • 0030896611 scopus 로고    scopus 로고
    • Metal-mediated hydrolysis of biological phosphateesters: A critical analysis of the essential metal-ion stoichiometry for magnesium-dependent nuclease activation
    • Cowan JA. 1997. Metal-mediated hydrolysis of biological phosphateesters: A critical analysis of the essential metal-ion stoichiometry for magnesium-dependent nuclease activation. J Biol Inorg Chem 2:168-176.
    • (1997) J Biol Inorg Chem , vol.2 , pp. 168-176
    • Cowan, J.A.1
  • 21
    • 0000063535 scopus 로고    scopus 로고
    • Manganese enzymes with binuclear active sites
    • Dismukes GC. 1996. Manganese enzymes with binuclear active sites. Chem Rev 96:2909-2926.
    • (1996) Chem Rev , vol.96 , pp. 2909-2926
    • Dismukes, G.C.1
  • 22
    • 0029904022 scopus 로고    scopus 로고
    • Kinetic pathway for folding of the Tetrahymena ribozyme revealed by three ultraviolet-inducible cross-links
    • Downs WD, Cech TR. 1996. Kinetic pathway for folding of the Tetrahymena ribozyme revealed by three ultraviolet-inducible cross-links. RNA 2:718-732.
    • (1996) RNA , vol.2 , pp. 718-732
    • Downs, W.D.1    Cech, T.R.2
  • 23
    • 0029880537 scopus 로고    scopus 로고
    • Strategies for RNA folding
    • Draper DE. 1996. Strategies for RNA folding. Trends Biochem Sci 27:145-149.
    • (1996) Trends Biochem Sci , vol.27 , pp. 145-149
    • Draper, D.E.1
  • 24
    • 0032472205 scopus 로고    scopus 로고
    • Inhibition of the hammer-head ribozyme cleavage reaction by site-specific binding of Tb
    • Feig AL, Scott WG, Uhlenbeck, OC. 1998. Inhibition of the hammer-head ribozyme cleavage reaction by site-specific binding of Tb. Science 279:81-84.
    • (1998) Science , vol.279 , pp. 81-84
    • Feig, A.L.1    Scott, W.G.2    Uhlenbeck, O.C.3
  • 25
    • 0031406029 scopus 로고    scopus 로고
    • Folding of an mRNA pseudoknot required for stop codon readthrough: Effects of mono- and divalent ions on stability
    • Gluick TC, Wills NM, Gesteland RF, Draper DE. 1997. Folding of an mRNA pseudoknot required for stop codon readthrough: Effects of mono- and divalent ions on stability. Biochemistry 36:16173-16186.
    • (1997) Biochemistry , vol.36 , pp. 16173-16186
    • Gluick, T.C.1    Wills, N.M.2    Gesteland, R.F.3    Draper, D.E.4
  • 26
    • 0032500731 scopus 로고    scopus 로고
    • A preorganized active site in the crystal structure of the Tetrahymena ribozyme
    • Golden BL, Gooding AR, Podell ER, Cech TR. 1998. A preorganized active site in the crystal structure of the Tetrahymena ribozyme. Science 252:259-264.
    • (1998) Science , vol.252 , pp. 259-264
    • Golden, B.L.1    Gooding, A.R.2    Podell, E.R.3    Cech, T.R.4
  • 27
    • 0030886344 scopus 로고    scopus 로고
    • Does the restriction endonuclease EcoRV employ a two-metal-ion mechanism for DNA cleavage?
    • Groll DH, Jeltch A, Selent U, Pingoud A. 1997. Does the restriction endonuclease EcoRV employ a two-metal-ion mechanism for DNA cleavage? Biochemistry 36:11389-11401.
    • (1997) Biochemistry , vol.36 , pp. 11389-11401
    • Groll, D.H.1    Jeltch, A.2    Selent, U.3    Pingoud, A.4
  • 28
    • 0024976556 scopus 로고
    • Metal ion requirements for sequence-specific endonuclease activity of the Tetrahymena ribozyme
    • Grosshans CA, Cech TR. 1989. Metal ion requirements for sequence-specific endonuclease activity of the Tetrahymena ribozyme. Biochemistry 28:6888-6894.
    • (1989) Biochemistry , vol.28 , pp. 6888-6894
    • Grosshans, C.A.1    Cech, T.R.2
  • 29
    • 0026580844 scopus 로고
    • Evidence for processivity and two-step binding of the RNA substrate from studies of J1/2 mutants of the Tetrahymena ribozyme
    • Herschlag D. 1992. Evidence for processivity and two-step binding of the RNA substrate from studies of J1/2 mutants of the Tetrahymena ribozyme. Biochemistry 37:1386-1398.
    • (1992) Biochemistry , vol.37 , pp. 1386-1398
    • Herschlag, D.1
  • 30
    • 0025085590 scopus 로고
    • Catalysis of RNA cleavage by the Tetrahymena thermophila ribozyme. 1. Kinetic description of the reaction of an RNA substrate complementary to the active site
    • Herschlag D, Cech TR. 1990. Catalysis of RNA cleavage by the Tetrahymena thermophila ribozyme. 1. Kinetic description of the reaction of an RNA substrate complementary to the active site. Biochemistry 29:10159-10171.
    • (1990) Biochemistry , vol.29 , pp. 10159-10171
    • Herschlag, D.1    Cech, T.R.2
  • 31
    • 0027181643 scopus 로고
    • Contribution of 2′-hydroxyl groups of the RNA substrate to binding and catalysis by the Tetrahymena ribozyme. An energetic picture of an active site composed of RNA
    • Herschlag D, Eckstein F, Cech TR. 1993a. Contribution of 2′-hydroxyl groups of the RNA substrate to binding and catalysis by the Tetrahymena ribozyme. An energetic picture of an active site composed of RNA. Biochemistry 32:8299-6311.
    • (1993) Biochemistry , vol.32 , pp. 8299-16311
    • Herschlag, D.1    Eckstein, F.2    Cech, T.R.3
  • 32
    • 0027209722 scopus 로고
    • The importance of being ribose at the cleavage site in the Tetrahymena ribozyme reaction
    • Herschlag D, Eckstein F, Cech TR. 1993b. The importance of being ribose at the cleavage site in the Tetrahymena ribozyme reaction. Biochemistry 32:8312-8321.
    • (1993) Biochemistry , vol.32 , pp. 8312-8321
    • Herschlag, D.1    Eckstein, F.2    Cech, T.R.3
  • 33
    • 0028216604 scopus 로고
    • Comparison of pH dependencies of the Tetrahymena ribozyme reactions with RNA2′-substituted and phosphorothioate substrates reveals a rate-limiting conformational step
    • Herschlag D, Khosla M. 1994. Comparison of pH dependencies of the Tetrahymena ribozyme reactions with RNA2′-substituted and phosphorothioate substrates reveals a rate-limiting conformational step. Biochemistry 33:5291-5297.
    • (1994) Biochemistry , vol.33 , pp. 5291-5297
    • Herschlag, D.1    Khosla, M.2
  • 34
    • 0025771210 scopus 로고
    • Ribozyme-catalyzed and nonenzymatic reactions of phosphate diesters: Rate effects upon substitution of sulfur for a nonbridging phosphoryl oxygen atom
    • Herschlag D, Piccirilli JA, Cech TR. 1991. Ribozyme-catalyzed and nonenzymatic reactions of phosphate diesters: Rate effects upon substitution of sulfur for a nonbridging phosphoryl oxygen atom. Biochemistry 30:4844-4854.
    • (1991) Biochemistry , vol.30 , pp. 4844-4854
    • Herschlag, D.1    Piccirilli, J.A.2    Cech, T.R.3
  • 35
    • 0032506110 scopus 로고    scopus 로고
    • Metal ion-mediated substrate-assisted catalysis in type II restriction endonucleases
    • Horton NC, Newberry KJ, Perona JJ. 1998. Metal ion-mediated substrate-assisted catalysis in type II restriction endonucleases. Proc Natl Acad Sci USA 95:13489-13494.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 13489-13494
    • Horton, N.C.1    Newberry, K.J.2    Perona, J.J.3
  • 36
    • 0018148406 scopus 로고
    • Divalent cation-dependent stereospecificity of adenosine 5′-O-(2-thiotriphosphate) in the hexokinase and pyruvate kinase reactions
    • Jaffe EK, Cohn M. 1978. Divalent cation-dependent stereospecificity of adenosine 5′-O-(2-thiotriphosphate) in the hexokinase and pyruvate kinase reactions. J Biol Chem 253:4823-4825.
    • (1978) J Biol Chem , vol.253 , pp. 4823-4825
    • Jaffe, E.K.1    Cohn, M.2
  • 37
    • 0032733278 scopus 로고    scopus 로고
    • Quantitative evaluation of metal íon binding to Pvull restriction endonuclease
    • Jose TJ, Conlan LH, Dupureur CM. 1999. Quantitative evaluation of metal íon binding to Pvull restriction endonuclease. J Biol Inorg Chem 4:814-823.
    • (1999) J Biol Inorg Chem , vol.4 , pp. 814-823
    • Jose, T.J.1    Conlan, L.H.2    Dupureur, C.M.3
  • 38
    • 2142859139 scopus 로고    scopus 로고
    • Calcium ion coordination: A comparison with that of beryllium, magnesium, and zinc
    • Katz AK, Glusker JP, Beebe SA, Bock CW. 1996. Calcium ion coordination: A comparison with that of beryllium, magnesium, and zinc. J Am Chem Soc 118:5752-5763.
    • (1996) J Am Chem Soc , vol.118 , pp. 5752-5763
    • Katz, A.K.1    Glusker, J.P.2    Beebe, S.A.3    Bock, C.W.4
  • 39
    • 0032545251 scopus 로고    scopus 로고
    • Activation/attenuation model for RNase H
    • Keck JL, Goedken ER, Marqusee S. 1998. Activation/attenuation model for RNase H. J Biol Chem 273:34128-34133.
    • (1998) J Biol Chem , vol.273 , pp. 34128-34133
    • Keck, J.L.1    Goedken, E.R.2    Marqusee, S.3
  • 40
    • 0028077048 scopus 로고
    • Dissection of the role of the conserved G•U pair in group I RNA self-splicing
    • Knitt DS, Narlikar GJ, Herschlag D. 1994. Dissection of the role of the conserved G•U pair in group I RNA self-splicing. Biochemistry 33:13864-13879.
    • (1994) Biochemistry , vol.33 , pp. 13864-13879
    • Knitt, D.S.1    Narlikar, G.J.2    Herschlag, D.3
  • 41
    • 0024359787 scopus 로고
    • Defining the inside and outside of a catalytic RNA molecule
    • Latham JA, Cech TR. 1989. Defining the inside and outside of a catalytic RNA molecule. Science 245:276-282.
    • (1989) Science , vol.245 , pp. 276-282
    • Latham, J.A.1    Cech, T.R.2
  • 42
    • 0027525989 scopus 로고
    • Evolution in in vitro of an RNA enzyme with altered metal dependence
    • Lehman N, Joyce GF. 1993. Evolution in in vitro of an RNA enzyme with altered metal dependence. Nature 361:182-185.
    • (1993) Nature , vol.361 , pp. 182-185
    • Lehman, N.1    Joyce, G.F.2
  • 43
    • 0029184233 scopus 로고
    • Determinants that govern high-affinity calcium binding
    • Means AR, ed. New York: Raven Press
    • Linse S, Forsen S. 1995. Determinants that govern high-affinity calcium binding. In: Means AR, ed. Advances in second messenger andphosphoprotein research. New York: Raven Press, pp 89-151.
    • (1995) Advances in Second Messenger Andphosphoprotein Research , pp. 89-151
    • Linse, S.1    Forsen, S.2
  • 44
    • 0031882388 scopus 로고    scopus 로고
    • A two-metal ion mechanism operates in the hammerhead ribozyme-mediated cleavage of an RNA substrate
    • Lott WB, Pontius BW, von Hippel PH. 1998. A two-metal ion mechanism operates in the hammerhead ribozyme-mediated cleavage of an RNA substrate. Proc Natl Acad Sci USA 95:542-547.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 542-547
    • Lott, W.B.1    Pontius, B.W.2    Von Hippel, P.H.3
  • 46
    • 0028904988 scopus 로고
    • A positive entropy change for guanosine binding and for the chemical step in the Tetrahymena ribozyme reaction
    • McConnell TS, Cech TR. 1995. A positive entropy change for guanosine binding and for the chemical step in the Tetrahymena ribozyme reaction. Biochemistry 34:4056-4067.
    • (1995) Biochemistry , vol.34 , pp. 4056-4067
    • McConnell, T.S.1    Cech, T.R.2
  • 47
    • 0027170454 scopus 로고
    • Guanosine binding to the Tetrahymena ribozyme: Thermodynamic coupling with oligonucleotide binding
    • McConnell TS, Cech TR, Herschlag DH. 1993. Guanosine binding to the Tetrahymena ribozyme: Thermodynamic coupling with oligonucleotide binding. Proc Natl Acad Sci USA 90:8362-8366.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8362-8366
    • McConnell, T.S.1    Cech, T.R.2    Herschlag, D.H.3
  • 48
    • 0030750183 scopus 로고    scopus 로고
    • Effects of divalent metal ions on individual steps of the Tetrahymena ribozyme reaction
    • McConnell TS, Herschlag D, Cech TR. 1997. Effects of divalent metal ions on individual steps of the Tetrahymena ribozyme reaction. Biochemistry 36:8293-8303.
    • (1997) Biochemistry , vol.36 , pp. 8293-8303
    • McConnell, T.S.1    Herschlag, D.2    Cech, T.R.3
  • 49
    • 0025678737 scopus 로고
    • Modeling of the three-dimensional architecture of group I catalytic introns based on comparative sequence analysis
    • Michel F, Westhof E. 1990. Modeling of the three-dimensional architecture of group I catalytic introns based on comparative sequence analysis. J Mol Biol 276:585-610.
    • (1990) J Mol Biol , vol.276 , pp. 585-610
    • Michel, F.1    Westhof, E.2
  • 50
    • 0033607247 scopus 로고    scopus 로고
    • Characterization of a local folding event of the Tetrahymena group I ribozyme: Effects of oligonucleotide substrate length, pH, and temperature on the two substrate binding steps
    • Narlikar GJ, Bartley LE, Khosla M, Herschlag D. 1999. Characterization of a local folding event of the Tetrahymena group I ribozyme: Effects of oligonucleotide substrate length, pH, and temperature on the two substrate binding steps. Biochemistry 38:14192-14204.
    • (1999) Biochemistry , vol.38 , pp. 14192-14204
    • Narlikar, G.J.1    Bartley, L.E.2    Khosla, M.3    Herschlag, D.4
  • 52
    • 0029746472 scopus 로고    scopus 로고
    • Isolation of a local tertiary folding transition in the context of a globally folded RNA
    • Narlikar GJ, Herschlag D. 1996. Isolation of a local tertiary folding transition in the context of a globally folded RNA. Nat Struct Biol 3:701-710.
    • (1996) Nat Struct Biol , vol.3 , pp. 701-710
    • Narlikar, G.J.1    Herschlag, D.2
  • 53
    • 0031036847 scopus 로고    scopus 로고
    • Quantitating tertiary binding energies of 2′-OH groups on the P1 duplex of the Tetrahymena ribozyme: Intrinsic binding energy in an RNA enzyme
    • Narlikar GJ, Khosla M, Usman N, Herschlag D. 1997. Quantitating tertiary binding energies of 2′-OH groups on the P1 duplex of the Tetrahymena ribozyme: Intrinsic binding energy in an RNA enzyme. Biochemistry 36:2465-2477.
    • (1997) Biochemistry , vol.36 , pp. 2465-2477
    • Narlikar, G.J.1    Khosla, M.2    Usman, N.3    Herschlag, D.4
  • 54
    • 0028945859 scopus 로고
    • Higher order folding and domain analysis of the ribozyme from Bacillus subtilis ribonuclease P
    • Pan T. 1995. Higher order folding and domain analysis of the ribozyme from Bacillus subtilis ribonuclease P. Biochemistry 34:902-909.
    • (1995) Biochemistry , vol.34 , pp. 902-909
    • Pan, T.1
  • 55
    • 0003156250 scopus 로고
    • Divalent metal ions in RNA folding and catalysis
    • Gesteland RF, Atkins JF, eds. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press
    • Pan T, Long DM, Uhlenbeck OC. 1993. Divalent metal ions in RNA folding and catalysis. In: Gesteland RF, Atkins JF, eds. The RNA world. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press, pp 271-302.
    • (1993) The RNA World , pp. 271-302
    • Pan, T.1    Long, D.M.2    Uhlenbeck, O.C.3
  • 56
    • 0030876444 scopus 로고    scopus 로고
    • Involvement of a specific metal ion in the transition of the hammerhead ribozyme to its catalytic conformation
    • Peracchi A, Beigelman L, Scott EC, Uhlenbeck OC, Herschlag DH. 1997. Involvement of a specific metal ion in the transition of the hammerhead ribozyme to its catalytic conformation. J Biol Chem 272:26822-26826.
    • (1997) J Biol Chem , vol.272 , pp. 26822-26826
    • Peracchi, A.1    Beigelman, L.2    Scott, E.C.3    Uhlenbeck, O.C.4    Herschlag, D.H.5
  • 57
  • 58
    • 0026427239 scopus 로고
    • Ribozyme recognition of RNA by tertiary interactions with specific ribose 2′-OH groups
    • Pyle AM, Cech TR. 1991. Ribozyme recognition of RNA by tertiary interactions with specific ribose 2′-OH groups. Nature 350:628-631.
    • (1991) Nature , vol.350 , pp. 628-631
    • Pyle, A.M.1    Cech, T.R.2
  • 59
    • 0008875663 scopus 로고
    • Structural analysis of spermine and magnesium ion binding to yeast phenylalanine transfer RNA
    • Quigley GJ, Teeter MM, Rich A. 1978. Structural analysis of spermine and magnesium ion binding to yeast phenylalanine transfer RNA. Proc Natl Acad Sci USA 75:64-68.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 64-68
    • Quigley, G.J.1    Teeter, M.M.2    Rich, A.3
  • 60
    • 0024405753 scopus 로고
    • Stereochemical course of catalysis by the Tetrahymena ribozyme
    • Rajagopal J, Doudna JA, Szostak JW. 1989. Stereochemical course of catalysis by the Tetrahymena ribozyme. Science 244:692-694.
    • (1989) Science , vol.244 , pp. 692-694
    • Rajagopal, J.1    Doudna, J.A.2    Szostak, J.W.3
  • 61
    • 0016301992 scopus 로고
    • Determination of the rate of hexokinase-glucose dissociation by the isotope-trapping method
    • Rose IA, O'Connell EL, Litwin S, Bar Tana J. 1974. Determination of the rate of hexokinase-glucose dissociation by the isotope-trapping method. J Biol Chem 249:5163-5168.
    • (1974) J Biol Chem , vol.249 , pp. 5163-5168
    • Rose, I.A.1    O'Connell, E.L.2    Litwin, S.3    Bar Tana, J.4
  • 62
    • 0033555778 scopus 로고    scopus 로고
    • A re-investigation of the thio effect at the hammerhead cleavage site
    • Scott EC, Uhlenbeck OC. 1999. A re-investigation of the thio effect at the hammerhead cleavage site. Nucleic Acids Res 27:479-484.
    • (1999) Nucleic Acids Res , vol.27 , pp. 479-484
    • Scott, E.C.1    Uhlenbeck, O.C.2
  • 63
    • 0033600571 scopus 로고    scopus 로고
    • Probing the role of metal ions in RNA catalysis: Kinetic and thermodynamic characterization of a metal ion interaction with the 2′-moiety of the guanosine nucleophile in the Tetrahymena ribozyme reaction
    • Shan S, Herschlag D. 1999. Probing the role of metal ions in RNA catalysis: Kinetic and thermodynamic characterization of a metal ion interaction with the 2′-moiety of the guanosine nucleophile in the Tetrahymena ribozyme reaction. Biochemistry 33:10958-10975.
    • (1999) Biochemistry , vol.33 , pp. 10958-10975
    • Shan, S.1    Herschlag, D.2
  • 64
    • 0033607225 scopus 로고    scopus 로고
    • Three distinct metal ions at the active site of the Tetrahymena group I ribozyme
    • Shan S, Yoshida A, Sun S, Piccirilli J, Herschlag D. 1999. Three distinct metal ions at the active site of the Tetrahymena group I ribozyme. Proc Natl Acad Sci USA 96:12299-12304.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 12299-12304
    • Shan, S.1    Yoshida, A.2    Sun, S.3    Piccirilli, J.4    Herschlag, D.5
  • 66
    • 0027256149 scopus 로고
    • Multiple magnesium ions in the ribonuclease P reaction mechanism
    • Smith D, Pace NR. 1993. Multiple magnesium ions in the ribonuclease P reaction mechanism. Biochemistry 32:5273-5281.
    • (1993) Biochemistry , vol.32 , pp. 5273-5281
    • Smith, D.1    Pace, N.R.2
  • 67
    • 0030833215 scopus 로고    scopus 로고
    • Metal ion catalysis during splicing of pre-messenger RNA
    • Sontheimer EJ, Sun S, Piccirilli J. 1997. Metal ion catalysis during splicing of pre-messenger RNA. Nature 388:801-805.
    • (1997) Nature , vol.388 , pp. 801-805
    • Sontheimer, E.J.1    Sun, S.2    Piccirilli, J.3
  • 68
    • 0031984645 scopus 로고    scopus 로고
    • Complementary sets of noncanonical base pairs mediate RNA helix packing in the group I intron active site
    • Strobel SA, Ortoleva-Donnelly L, Ryder SP, Cate JH, Moncoeur E. 1998. Complementary sets of noncanonical base pairs mediate RNA helix packing in the group I intron active site. Nat Struct Biol 5:60-66.
    • (1998) Nat Struct Biol , vol.5 , pp. 60-66
    • Strobel, S.A.1    Ortoleva-Donnelly, L.2    Ryder, S.P.3    Cate, J.H.4    Moncoeur, E.5
  • 70
    • 0032491204 scopus 로고    scopus 로고
    • Structure and activity of the hairpin ribozyme in its natural junction conformation: Effect of metal ions
    • Walter F, Murchie AIH, Thomson JB, Lilley DMJ. 1998. Structure and activity of the hairpin ribozyme in its natural junction conformation: Effect of metal ions. Biochemistry 37:14195-14203.
    • (1998) Biochemistry , vol.37 , pp. 14195-14203
    • Walter, F.1    Murchie, A.I.H.2    Thomson, J.B.3    Lilley, D.M.J.4
  • 72
    • 0033538479 scopus 로고    scopus 로고
    • Role of metal ions in the hydrolysis reaction catalyzed by RNase P RNA from Bacillus subtilis
    • Warnecke JM, Held R, Busch S, Hartmann RK. 1999. Role of metal ions in the hydrolysis reaction catalyzed by RNase P RNA from Bacillus subtilis. J Mol Biol 290:433-445.
    • (1999) J Mol Biol , vol.290 , pp. 433-445
    • Warnecke, J.M.1    Held, R.2    Busch, S.3    Hartmann, R.K.4
  • 73
    • 0030800470 scopus 로고    scopus 로고
    • A second catalytic metal ion in a group I ribozyme
    • Weinstein LB, Jones BC, Cosstick R, Cech TR. 1997. A second catalytic metal ion in a group I ribozyme. Nature 388:805-808.
    • (1997) Nature , vol.388 , pp. 805-808
    • Weinstein, L.B.1    Jones, B.C.2    Cosstick, R.3    Cech, T.R.4
  • 74
    • 0001431264 scopus 로고    scopus 로고
    • Binuclear metallohydrolases
    • Wilcox DE. 1996. Binuclear metallohydrolases. Chem Rev 96:2435-2458.
    • (1996) Chem Rev , vol.96 , pp. 2435-2458
    • Wilcox, D.E.1
  • 75
    • 0034142032 scopus 로고    scopus 로고
    • The role of the cleavage site 2′-OH in the Tetrahymena ribozyme reaction: Evidence for catalysis by hydrogen bond donation to the 3′-leaving group oxygen
    • Yoshida A, Shan S, Herschlag D, Piccirilli JA. 2000. The role of the cleavage site 2′-OH in the Tetrahymena ribozyme reaction: Evidence for catalysis by hydrogen bond donation to the 3′-leaving group oxygen. Chem Biol 7:85-96.
    • (2000) Chem Biol , vol.7 , pp. 85-96
    • Yoshida, A.1    Shan, S.2    Herschlag, D.3    Piccirilli, J.A.4
  • 76
    • 0032893740 scopus 로고    scopus 로고
    • A new metal ion interaction in the Tetrahymena ribozyme reaction revealed by double sulfur substitution
    • Yoshida A, Sun S, Piccirilli JA. 1999. A new metal ion interaction in the Tetrahymena ribozyme reaction revealed by double sulfur substitution. Nat Struct Biol 6:318-321.
    • (1999) Nat Struct Biol , vol.6 , pp. 318-321
    • Yoshida, A.1    Sun, S.2    Piccirilli, J.A.3
  • 77
    • 0024285808 scopus 로고
    • Sequence-specific endo-ribonuclease activity of the Tetrahymena ribozyme: Enhanced cleavage of certain oligonucleotide substrates that form mismatched ribozyme-substrate complexes
    • Zaug AJ, Grosshans CA, Cech TR. 1988. Sequence-specific endo-ribonuclease activity of the Tetrahymena ribozyme: Enhanced cleavage of certain oligonucleotide substrates that form mismatched ribozyme-substrate complexes. Biochemistry 27:8924-8931.
    • (1988) Biochemistry , vol.27 , pp. 8924-8931
    • Zaug, A.J.1    Grosshans, C.A.2    Cech, T.R.3


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