메뉴 건너뛰기




Volumn 6, Issue 3, 1999, Pages 153-165

A hydrogen-bonding triad stabilizes the chemical transition state of a group I ribozyme

Author keywords

Interference suppression; Nucleotide analog interference mapping; Phosphoryl transfer; Reaction mechanism; Self splicing intron

Indexed keywords

ENZYME ACTIVE SITE; ENZYME STABILITY; RIBOZYME;

EID: 0033102218     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(99)89007-3     Document Type: Article
Times cited : (73)

References (64)
  • 1
    • 0030968710 scopus 로고    scopus 로고
    • Mechanistic aspects of enzymatic catalysis: Lessons from comparison of RNA and protein enzymes
    • Narlikar, G.J. & Herschlag, D. (1997). Mechanistic aspects of enzymatic catalysis: Lessons from comparison of RNA and protein enzymes. Annu. Rev. Biochem. 66, 19-59.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 19-59
    • Narlikar, G.J.1    Herschlag, D.2
  • 2
    • 0029837557 scopus 로고    scopus 로고
    • Two-metal ion catalysis in enzymatic acyl- and phosphoryl-transfer reactions
    • Strater, N., Lipscomb, W.N., Klabunde, T. & Krebs, B. (1996). Two-metal ion catalysis in enzymatic acyl- and phosphoryl-transfer reactions. Angew. Chem. Int. Ed. Engl. 35, 2024-2055.
    • (1996) Angew. Chem. Int. Ed. Engl. , vol.35 , pp. 2024-2055
    • Strater, N.1    Lipscomb, W.N.2    Klabunde, T.3    Krebs, B.4
  • 3
    • 0025367254 scopus 로고
    • Self-splicing of group I introns
    • Cech, T.R. (1990). Self-splicing of group I introns. Ann. Rev. Biochem. 59, 543-568.
    • (1990) Ann. Rev. Biochem. , vol.59 , pp. 543-568
    • Cech, T.R.1
  • 4
    • 0023364038 scopus 로고
    • The chemistry of self-splicing RNA and RNA enzymes
    • Cech, T.R. (1987). The chemistry of self-splicing RNA and RNA enzymes. Science 236, 1532-1539.
    • (1987) Science , vol.236 , pp. 1532-1539
    • Cech, T.R.1
  • 5
    • 0025877764 scopus 로고
    • Group I intron self-splicing with adenosine: Evidence for a single nucleoside-binding site
    • Been, M.D. & Perrotta, A.T. (1991). Group I intron self-splicing with adenosine: Evidence for a single nucleoside-binding site. Science 252, 434-438.
    • (1991) Science , vol.252 , pp. 434-438
    • Been, M.D.1    Perrotta, A.T.2
  • 6
    • 0024285808 scopus 로고
    • Sequence-specific endoribonuclease activity of the Tetrahymena ribozyme: Enhanced cleavage of certain oligonucleotide substrates that form mismatched ribozyme-substrate complexes
    • Zaug, A.J., Grosshans, C.A. & Cech, T.R. (1988). Sequence-specific endoribonuclease 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
  • 7
    • 0026649231 scopus 로고
    • Directed evolution of an RNA enzyme
    • Beaudry, A.A. & Joyce, G.F. (1992). Directed evolution of an RNA enzyme. Science 257, 635-641.
    • (1992) Science , vol.257 , pp. 635-641
    • Beaudry, A.A.1    Joyce, G.F.2
  • 8
    • 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, T.R. (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
  • 9
    • 0029882895 scopus 로고    scopus 로고
    • Mechanistic investigations of a ribozyme derived from the Tetrahymena group I intron. Insights into catalysis and the second step of self-splicing
    • Mei, R. & Herschlag, D. (1996). Mechanistic investigations of a ribozyme derived from the Tetrahymena group I intron. Insights into catalysis and the second step of self-splicing. Biochemistry 35, 5796-5809.
    • (1996) Biochemistry , vol.35 , pp. 5796-5809
    • Mei, R.1    Herschlag, D.2
  • 10
    • 0026678180 scopus 로고
    • Dynamics of ribozyme binding of substrate revealed by fluorescence-detected stopped-flow methods
    • Bevilacqua, P.C., Kierzek, R., Johnson, K.A. & Turner, D.H. (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
  • 11
    • 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 31, 1386-1399.
    • (1992) Biochemistry , vol.31 , pp. 1386-1399
    • Herschlag, D.1
  • 12
    • 0021241894 scopus 로고
    • Specific interaction between the self-splicing RNA of Tetrahymena and its guanosine substrate: Implications for biological catalysis by RNA
    • Bass, B.L. & Cech, T.R. (1984). Specific interaction between the self-splicing RNA of Tetrahymena and its guanosine substrate: Implications for biological catalysis by RNA. Nature 308, 820-826.
    • (1984) Nature , vol.308 , pp. 820-826
    • Bass, B.L.1    Cech, T.R.2
  • 13
    • 0027281334 scopus 로고
    • Binding of guanosine and 3′ splice site analogues to a group I ribozyme: Interactions with functional groups of guanosine and with additional nucleotides
    • Moran, S., Kierzek, R. & Turner, D.H. (1993). Binding of guanosine and 3′ splice site analogues to a group I ribozyme: Interactions with functional groups of guanosine and with additional nucleotides. Biochemistry 32, 5247-5256.
    • (1993) Biochemistry , vol.32 , pp. 5247-5256
    • Moran, S.1    Kierzek, R.2    Turner, D.H.3
  • 14
    • 0030609842 scopus 로고    scopus 로고
    • 2+ and the 2′-OH of guanosine on steps required for substrate binding and reactivity with the Tetrahymena ribozyme reveal several local folding transitions
    • 2+ and the 2′-OH of guanosine on steps required for substrate binding and reactivity with the Tetrahymena ribozyme reveal several local folding transitions. Biochemistry 36, 11131-11139.
    • (1997) Biochemistry , vol.36 , pp. 11131-11139
    • Li, Y.1    Turner, D.H.2
  • 15
    • 0025305796 scopus 로고
    • DNA cleavage catalysed by the ribozyme from Tetrahymena
    • Herschlag, D. & Cech, T.R. (1990). DNA cleavage catalysed by the ribozyme from Tetrahymena. Nature 344, 405-409.
    • (1990) Nature , vol.344 , pp. 405-409
    • Herschlag, D.1    Cech, T.R.2
  • 16
    • 0027209722 scopus 로고
    • The importance of being ribose at the cleavage site in the Tetrahymena ribozyme reaction
    • Herschlag, D., Eckstein, F. & Cech, T.R. (1993). 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
  • 17
    • 0027181643 scopus 로고
    • Contributions 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, T.R. (1993). Contributions 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, 8299-8311.
    • (1993) Biochemistry , vol.32 , pp. 8299-8311
    • Herschlag, D.1    Eckstein, F.2    Cech, T.R.3
  • 18
    • 0028077048 scopus 로고
    • Dissection of the role of the conserved G-U pair in group I RNA self-splicing
    • Knitt, D.S., Narlikar, G.J. & 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
  • 19
    • 0028955347 scopus 로고
    • Minor groove recognition of the conserved G-U pair at the Tetrahymena ribozyme reaction site
    • Strobel, S.A. & Cech, T.R. (1995). Minor groove recognition of the conserved G-U pair at the Tetrahymena ribozyme reaction site. Science 267, 675-679.
    • (1995) Science , vol.267 , pp. 675-679
    • Strobel, S.A.1    Cech, T.R.2
  • 20
    • 0030068393 scopus 로고    scopus 로고
    • Exocyclic amine of the conserved G-U pair at the cleavage site of the Tetrahymena ribozyme contributes to 5′-splice site selection and transition state stabilization
    • Strobel, S.A. & Cech, T.R. (1996). Exocyclic amine of the conserved G-U pair at the cleavage site of the Tetrahymena ribozyme contributes to 5′-splice site selection and transition state stabilization. Biochemistry 35, 1201-1211.
    • (1996) Biochemistry , vol.35 , pp. 1201-1211
    • Strobel, S.A.1    Cech, T.R.2
  • 21
    • 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, G.J., 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
  • 22
    • 0027183545 scopus 로고
    • Ribozymes: A distinct class of metalloenzymes
    • Pyle, A.M. (1993). Ribozymes: A distinct class of metalloenzymes. Science 261, 709-714.
    • (1993) Science , vol.261 , pp. 709-714
    • Pyle, A.M.1
  • 23
    • 0024976556 scopus 로고
    • Metal ion requirements for sequence-specific endoribonuclease activity of the Tetrahymena ribozyme
    • Grosshans, C.A. & Cech, T.R. (1989). Metal ion requirements for sequence-specific endoribonuclease activity of the Tetrahymena ribozyme. Biochemistry 28, 6888-6894.
    • (1989) Biochemistry , vol.28 , pp. 6888-6894
    • Grosshans, C.A.1    Cech, T.R.2
  • 24
    • 0027398505 scopus 로고
    • Metal ion catalysis in the Tetrahymena ribozyme reaction
    • Piccirilli, J.A., Vyle, J.S., Caruthers, M.H. & Cech, T.R. (1993). Metal ion catalysis in the Tetrahymena ribozyme reaction. Nature 362, 85-88.
    • (1993) Nature , vol.362 , pp. 85-88
    • Piccirilli, J.A.1    Vyle, J.S.2    Caruthers, M.H.3    Cech, T.R.4
  • 25
    • 0030800470 scopus 로고    scopus 로고
    • A second catalytic metal ion in a group I ribozyme
    • Weinstein, L.B., Jones, B.c.n.m., Cosstick, R. & Cech, T.R. (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.N.M.2    Cosstick, R.3    Cech, T.R.4
  • 26
    • 0242271642 scopus 로고    scopus 로고
    • Metal ion interaction with cosubstrate in self-splicing of group I introns
    • Sjoegren, A.S., Pettersson, E., Sjoeberg, B.M. & Stroemberg, R. (1997). Metal ion interaction with cosubstrate in self-splicing of group I introns. Nucleic Acids Res. 25, 648-653.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 648-653
    • Sjoegren, A.S.1    Pettersson, E.2    Sjoeberg, B.M.3    Stroemberg, R.4
  • 27
    • 0026427239 scopus 로고
    • Ribozyme recognition of RNA by tertiary interactions with specific ribose 2′-OH groups
    • Pyle, A.M. & Cech, T.R. (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
  • 28
    • 0026347806 scopus 로고
    • Comparison of binding of mixed ribose-deoxyribose analogues of CUCU to a ribozyme and to GGAGAA by equilibrium dialysis: Evidence for ribozyme specific interactions with 2′ OH groups
    • Bevilacqua, P.C. & Turner, D.H. (1991). Comparison of binding of mixed ribose-deoxyribose analogues of CUCU to a ribozyme and to GGAGAA by equilibrium dialysis: Evidence for ribozyme specific interactions with 2′ OH groups. Biochemistry 30, 10632-10640.
    • (1991) Biochemistry , vol.30 , pp. 10632-10640
    • Bevilacqua, P.C.1    Turner, D.H.2
  • 29
    • 0027181643 scopus 로고
    • Contributions 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, T.R. (1993). Contributions 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, 8299-8311.
    • (1993) Biochemistry , vol.32 , pp. 8299-8311
    • Herschlag, D.1    Eckstein, F.2    Cech, T.R.3
  • 30
    • 0027767532 scopus 로고
    • Tertiary interactions with the internal guide sequence mediate docking of the P1 helix into the catalytic core of the Tetrahymena ribozyme
    • Strobel, S.A. & Cech, T.R. (1993). Tertiary interactions with the internal guide sequence mediate docking of the P1 helix into the catalytic core of the Tetrahymena ribozyme. Biochemistry 32, 13593-13604.
    • (1993) Biochemistry , vol.32 , pp. 13593-13604
    • Strobel, S.A.1    Cech, T.R.2
  • 32
    • 0026000848 scopus 로고
    • Crystal structure of an RNA double helix incorporating a track of non-Watson-Crick base pairs
    • Holbrook, S.R., Cheong, C., Tinoco, I. & Kim, S.-H. (1991). Crystal structure of an RNA double helix incorporating a track of non-Watson-Crick base pairs. Nature 353, 579-581.
    • (1991) Nature , vol.353 , pp. 579-581
    • Holbrook, S.R.1    Cheong, C.2    Tinoco, I.3    Kim, S.-H.4
  • 33
    • 0031984645 scopus 로고    scopus 로고
    • Complementary sets of noncanonical base pairs mediate RNA helix packing in the group I intron active site
    • Strobel, S.A., Ortoleva-Donnelly, L., Ryder, S.P., Cate, J.H. & 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
  • 34
    • 0027295270 scopus 로고
    • Modification interference approach to detect ribose moieties important for the optimal activity of a ribozyme
    • Gaur, R.K. & Krupp, G. (1993). Modification interference approach to detect ribose moieties important for the optimal activity of a ribozyme. Nucleic Acids Res. 21, 21-26.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 21-26
    • Gaur, R.K.1    Krupp, G.2
  • 35
    • 0030965811 scopus 로고    scopus 로고
    • Defining the chemical groups essential for Tetrahymena group I intron function by nucleotide analog interference mapping
    • Strobel, S.A. & Shetty, K. (1997). Defining the chemical groups essential for Tetrahymena group I intron function by nucleotide analog interference mapping. Proc. Natl Acad. Sci. USA 94, 2903-2908.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 2903-2908
    • Strobel, S.A.1    Shetty, K.2
  • 36
    • 0024283277 scopus 로고
    • DNA and RNA sequence determination based on phosphorothioate chemistry
    • Gish, G. & Eckstein, F. (1988). DNA and RNA sequence determination based on phosphorothioate chemistry. Science 240, 1520-1522.
    • (1988) Science , vol.240 , pp. 1520-1522
    • Gish, G.1    Eckstein, F.2
  • 37
    • 0025885722 scopus 로고
    • Mutations in a nonconserved sequence of the Tetrahymena ribozyme increase activity and specificity
    • Young, B., Herschlag, D. & Cech, T.R. (1991). Mutations in a nonconserved sequence of the Tetrahymena ribozyme increase activity and specificity. Cell 67, 1007-1019.
    • (1991) Cell , vol.67 , pp. 1007-1019
    • Young, B.1    Herschlag, D.2    Cech, T.R.3
  • 38
    • 0026680843 scopus 로고
    • Site-specific modification of pre-mRNA: The 2′-hydroxyl groups at the splice sites
    • Moore, M.J. & Sharp, P.A. (1992). Site-specific modification of pre-mRNA: The 2′-hydroxyl groups at the splice sites. Science 256, 992-997.
    • (1992) Science , vol.256 , pp. 992-997
    • Moore, M.J.1    Sharp, P.A.2
  • 40
    • 0028367586 scopus 로고
    • Translocation of an RNA duplex on a ribozyme
    • Strobel, S.A. & Cech, T.R. (1994). Translocation of an RNA duplex on a ribozyme. Nat Struct. Biol. 1, 13-17.
    • (1994) Nat Struct. Biol. , vol.1 , pp. 13-17
    • Strobel, S.A.1    Cech, T.R.2
  • 42
    • 0025155692 scopus 로고
    • Direct measurement of oligonucleotide substrate binding to wild-type and mutant ribozymes from Tetrahymena
    • Pyle, A.M., McSwiggen, J.A. & Cech, T.R. (1990). Direct measurement of oligonucleotide substrate binding to wild-type and mutant ribozymes from Tetrahymena. Proc. Natl Acad. Sci. USA 87, 8187-8191.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 8187-8191
    • Pyle, A.M.1    McSwiggen, J.A.2    Cech, T.R.3
  • 43
    • 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, J.A. & Cech, T.R. (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
  • 44
    • 0027170454 scopus 로고
    • Guanosine binding to the Tetrahymena ribozyme: Thermodynamic coupling with oligonucleotide binding
    • McConnell, T.S., Cech, T.R. & Herschlag, D. (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.3
  • 45
    • 0028146967 scopus 로고
    • A comparative database of group I intron structures
    • Damberger, S.H. & Gutell, R.R. (1994). A comparative database of group I intron structures. Nucleic Acids Res. 22, 3508-3510.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 3508-3510
    • Damberger, S.H.1    Gutell, R.R.2
  • 46
    • 0029820625 scopus 로고    scopus 로고
    • Crystal structure of a group I ribozyme domain: Principles of RNA packing
    • Cate, J.H., et al., & Doudna, J.A. (1996). Crystal structure of a group I ribozyme domain: Principles of RNA packing. Science 273, 1678-1685.
    • (1996) Science , vol.273 , pp. 1678-1685
    • Cate, J.H.1    Doudna, J.A.2
  • 48
    • 0023047647 scopus 로고
    • Ribozyme inhibitors: Deoxyguanosine and dideoxyguanosine are competitive inhibitors of self-splicing of the Tetrahymena ribosomal ribonucleic acid precursor
    • Bass, B.L. & Cech, T.R. (1986). Ribozyme inhibitors: Deoxyguanosine and dideoxyguanosine are competitive inhibitors of self-splicing of the Tetrahymena ribosomal ribonucleic acid precursor. Biochemistry 25, 4473-4477.
    • (1986) Biochemistry , vol.25 , pp. 4473-4477
    • Bass, B.L.1    Cech, T.R.2
  • 49
    • 0015924871 scopus 로고
    • Enzymatic catalysis and transition-state theory
    • Lienhard, G.E. (1973). Enzymatic catalysis and transition-state theory. Science 180, 149-180.
    • (1973) Science , vol.180 , pp. 149-180
    • Lienhard, G.E.1
  • 50
    • 0016624901 scopus 로고
    • Binding energy, specificity, and enzymic catalysis: The Circe effect
    • Jencks, W.P. (1975). Binding energy, specificity, and enzymic catalysis: The Circe effect. Adv. Enzymol. 43, 219-410.
    • (1975) Adv. Enzymol. , vol.43 , pp. 219-410
    • Jencks, W.P.1
  • 52
    • 0032516432 scopus 로고    scopus 로고
    • Direct demonstration of the catalytic role of binding interaction in an enzymatic reaction
    • Narlikar, G.J. & Herschlag, D. (1998). Direct demonstration of the catalytic role of binding interaction in an enzymatic reaction. Biochemistry 37, 9902-9911.
    • (1998) Biochemistry , vol.37 , pp. 9902-9911
    • Narlikar, G.J.1    Herschlag, D.2
  • 53
    • 0027184481 scopus 로고
    • A general two-metal-ion mechanism for catalytic RNA
    • Steitz, T.A. & Steitz, J.A. (1993). A general two-metal-ion mechanism for catalytic RNA. Proc. Natl Acad. Sci. USA 90, 6498-6502.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6498-6502
    • Steitz, T.A.1    Steitz, J.A.2
  • 54
    • 0026019625 scopus 로고
    • Structural basis for the 3′-5′ exonuclease activity of Escherichia coli DNA polymerase I: A two metal ion mechanism
    • Beese, L.S. & Steitz, T.A. (1991). Structural basis for the 3′-5′ exonuclease activity of Escherichia coli DNA polymerase I: A two metal ion mechanism. EMBO J. 10, 25-33.
    • (1991) EMBO J. , vol.10 , pp. 25-33
    • Beese, L.S.1    Steitz, T.A.2
  • 55
    • 0026085471 scopus 로고
    • The 3′-5′ exonuclease of DNA polymerase I of Escherichia coli: Contribution of each amino acid at the active site to the reaction
    • Derbyshire, V., Grindley, N.D.F. & Joyce, C.M. (1991). The 3′-5′ exonuclease of DNA polymerase I of Escherichia coli: Contribution of each amino acid at the active site to the reaction. EMBO J. 10, 17-24.
    • (1991) EMBO J. , vol.10 , pp. 17-24
    • Derbyshire, V.1    Grindley, N.D.F.2    Joyce, C.M.3
  • 56
    • 0027458881 scopus 로고
    • Crystallographic studies of the catalytic mechanism of the neutral form of fructose-1,6-bisphosphatase
    • Zhang, Y., Liang, J.-Y., Huang, S., Ke, H. & Lipscomb, W.N. (1993). Crystallographic studies of the catalytic mechanism of the neutral form of fructose-1,6-bisphosphatase. Biochemistry 32, 1844-1857.
    • (1993) Biochemistry , vol.32 , pp. 1844-1857
    • Zhang, Y.1    Liang, J.-Y.2    Huang, S.3    Ke, H.4    Lipscomb, W.N.5
  • 57
    • 0017123092 scopus 로고
    • Inhibition of bovine hepatic fructose-1,6-diphosphatase by substrate analogs
    • Marcus, C.J. (1976). Inhibition of bovine hepatic fructose-1,6-diphosphatase by substrate analogs. J. Biol. Chem. 251, 2963.
    • (1976) J. Biol. Chem. , vol.251 , pp. 2963
    • Marcus, C.J.1
  • 58
    • 0027173944 scopus 로고
    • Isolation of a human liver fructose-1,6-bisphosphatase cDNA and expression of the protein in Escherichia coli. Role of Asp-118 and Asp-121 in catalysis
    • El-Maghrabi, M.R., Gidh-Jain, M., Austin, L.R. & Pilkis, S.J. (1993). Isolation of a human liver fructose-1,6-bisphosphatase cDNA and expression of the protein in Escherichia coli. Role of Asp-118 and Asp-121 in catalysis. J. Biol. Chem. 268, 9466-9472.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9466-9472
    • El-Maghrabi, M.R.1    Gidh-Jain, M.2    Austin, L.R.3    Pilkis, S.J.4
  • 59
    • 0031967099 scopus 로고    scopus 로고
    • The chemical basis of adenosine conservation throughout the Tetrahymena ribozyme
    • Ortoleva-Donnelly, L., Szewczak, A.A., Gutell, R.R. & Strobel, S.A. (1998). The chemical basis of adenosine conservation throughout the Tetrahymena ribozyme. RNA 4, 498-519.
    • (1998) RNA , vol.4 , pp. 498-519
    • Ortoleva-Donnelly, L.1    Szewczak, A.A.2    Gutell, R.R.3    Strobel, S.A.4
  • 60
    • 0032545045 scopus 로고    scopus 로고
    • Novel RNA synthesis method using 5'-O-silyl-2'-O-orthoester protecting groups
    • Scaringe, S.A., Wincott, F.E. & Caruthers, M.H. (1998). Novel RNA synthesis method using 5'-O-silyl-2'-O-orthoester protecting groups. J. Am. Chem. Soc. 120, 11820-11821.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 11820-11821
    • Scaringe, S.A.1    Wincott, F.E.2    Caruthers, M.H.3
  • 61
    • 0029091457 scopus 로고
    • A mutant T7 RNA polymerase as a DNA polymerase
    • Sousa, R. & Padilla, R. (1995). A mutant T7 RNA polymerase as a DNA polymerase. EMBO J. 14, 4609-4621.
    • (1995) EMBO J. , vol.14 , pp. 4609-4621
    • Sousa, R.1    Padilla, R.2
  • 62
    • 0027250384 scopus 로고
    • 3′-end labeling of RNA with recombinant yeast poly(A) polymerase
    • Lingner, J. & Keller, W. (1993). 3′-end labeling of RNA with recombinant yeast poly(A) polymerase. Nucleic Acids Res. 21, 2917-2920.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 2917-2920
    • Lingner, J.1    Keller, W.2
  • 63
    • 0024313959 scopus 로고
    • Miniribozymes, small derivatives of the sunY intron, are catalytically active
    • Doudna, J.A. & Szostak, J.W. (1989). Miniribozymes, small derivatives of the sunY intron, are catalytically active. Mol. Cell. Biol. 9, 5480-5483.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 5480-5483
    • Doudna, J.A.1    Szostak, J.W.2
  • 64
    • 0027997590 scopus 로고
    • Replacement of the conserved G-U with a G-C pair at the cleavage site of the Tetrahymena ribozyme decreases binding, reactivity, and fidelity
    • Pyle, A.M., Moran, S., Strobel, S.A., Chapman, T., Turner, D.H. & Cech, T.R. (1994). Replacement of the conserved G-U with a G-C pair at the cleavage site of the Tetrahymena ribozyme decreases binding, reactivity, and fidelity. Biochemistry 33, 13856-13863.
    • (1994) Biochemistry , vol.33 , pp. 13856-13863
    • Pyle, A.M.1    Moran, S.2    Strobel, S.A.3    Chapman, T.4    Turner, D.H.5    Cech, T.R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.