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Volumn 400, Issue 1, 2010, Pages 38-51

A divalent cation stabilizes the active conformation of the B. Subtilis RNase P·Pre-tRNA complex: A role for an inner-sphere metal ion in RNase P

Author keywords

Conformational change; Metals; RNase P; TrFRET; TRNA processing

Indexed keywords

CALCIUM; DIVALENT CATION; GLYCINE DEHYDROGENASE (DECARBOXYLATING); MAGNESIUM; METAL ION; RIBONUCLEASE P; TRANSFER RNA;

EID: 77953699478     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.04.050     Document Type: Article
Times cited : (26)

References (75)
  • 1
    • 0036940303 scopus 로고    scopus 로고
    • Metal ions in the structure and function of RNA
    • Pyle A.M. Metal ions in the structure and function of RNA. J. Biol. Inorg. Chem. 2002, 7:679-690.
    • (2002) J. Biol. Inorg. Chem. , vol.7 , pp. 679-690
    • Pyle, A.M.1
  • 2
    • 0032419499 scopus 로고    scopus 로고
    • On the role of magnesium ions in RNA stability
    • Misra V.K., Draper D.E. On the role of magnesium ions in RNA stability. Biopolymers 1998, 48:113-135.
    • (1998) Biopolymers , vol.48 , pp. 113-135
    • Misra, V.K.1    Draper, D.E.2
  • 4
    • 58249114463 scopus 로고    scopus 로고
    • Mapping metal-binding sites in the catalytic domain of bacterial RNase P RNA
    • Kazantsev A.V., Krivenko A.A., Pace N.R. Mapping metal-binding sites in the catalytic domain of bacterial RNase P RNA. RNA 2009, 15:266-276.
    • (2009) RNA , vol.15 , pp. 266-276
    • Kazantsev, A.V.1    Krivenko, A.A.2    Pace, N.R.3
  • 5
    • 9144253867 scopus 로고    scopus 로고
    • Nature of the chemical bond formed with the structural metal ion at the A9/G10.1 motif derived from hammerhead ribozymes
    • Tanaka Y., Kasai Y., Mochizuki S., Wakisaka A., Morita E.H., Kojima C., et al. Nature of the chemical bond formed with the structural metal ion at the A9/G10.1 motif derived from hammerhead ribozymes. J. Am. Chem. Soc. 2004, 126:744-752.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 744-752
    • Tanaka, Y.1    Kasai, Y.2    Mochizuki, S.3    Wakisaka, A.4    Morita, E.H.5    Kojima, C.6
  • 8
    • 70349279881 scopus 로고    scopus 로고
    • Identification of catalytic metal ion ligands in ribozymes
    • Frederiksen J.K., Piccirilli J.A. Identification of catalytic metal ion ligands in ribozymes. Methods 2009, 49:148-166.
    • (2009) Methods , vol.49 , pp. 148-166
    • Frederiksen, J.K.1    Piccirilli, J.A.2
  • 9
    • 37549069403 scopus 로고    scopus 로고
    • Importance of RNA-protein interactions in bacterial ribonuclease P structure and catalysis
    • Smith J.K., Hsieh J., Fierke C.A. Importance of RNA-protein interactions in bacterial ribonuclease P structure and catalysis. Biopolymers 2007, 87:329-338.
    • (2007) Biopolymers , vol.87 , pp. 329-338
    • Smith, J.K.1    Hsieh, J.2    Fierke, C.A.3
  • 10
    • 0017146579 scopus 로고
    • Ion effects on ligand-nucleic acid interactions
    • Record M.T., Lohman M.L., De Haseth P. Ion effects on ligand-nucleic acid interactions. J. Mol. Biol. 1976, 107:145-158.
    • (1976) J. Mol. Biol. , vol.107 , pp. 145-158
    • Record, M.T.1    Lohman, M.L.2    De Haseth, P.3
  • 11
    • 16244363320 scopus 로고    scopus 로고
    • Metal ions and RNA folding: a highly charged topic with a dynamic future
    • Woodson S.A. Metal ions and RNA folding: a highly charged topic with a dynamic future. Curr. Opin. Chem. Biol. 2005, 9:104-109.
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 104-109
    • Woodson, S.A.1
  • 12
    • 71549119274 scopus 로고    scopus 로고
    • RNase P RNA-mediated cleavage
    • Kirsebom L.A., Trobro S. RNase P RNA-mediated cleavage. IUBMB Life 2009, 61:189-200.
    • (2009) IUBMB Life , vol.61 , pp. 189-200
    • Kirsebom, L.A.1    Trobro, S.2
  • 13
    • 0038170017 scopus 로고    scopus 로고
    • Recent insights into the structure and function of the ribonucleoprotein enzyme ribonuclease P
    • Harris M.E., Christian E.L. Recent insights into the structure and function of the ribonucleoprotein enzyme ribonuclease P. Curr. Opin. Struct. Biol. 2003, 13:325-333.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 325-333
    • Harris, M.E.1    Christian, E.L.2
  • 17
    • 0032076249 scopus 로고    scopus 로고
    • Ribonuclease P protein structure: evolutionary origins in the translational apparatus
    • Stams T., Niranjanakumari S., Fierke C.A., Christianson D.W. Ribonuclease P protein structure: evolutionary origins in the translational apparatus. Science 1998, 280:752-755.
    • (1998) Science , vol.280 , pp. 752-755
    • Stams, T.1    Niranjanakumari, S.2    Fierke, C.A.3    Christianson, D.W.4
  • 18
    • 0034614360 scopus 로고    scopus 로고
    • The structure of ribonuclease P protein from Staphylococcus aureus reveals a unique binding site for single-stranded RNA
    • Spitzfaden C., Nicholson N., Jones J.J., Guth S., Lehr R., Prescott C.D., et al. The structure of ribonuclease P protein from Staphylococcus aureus reveals a unique binding site for single-stranded RNA. J. Mol. Biol. 2000, 295:105-115.
    • (2000) J. Mol. Biol. , vol.295 , pp. 105-115
    • Spitzfaden, C.1    Nicholson, N.2    Jones, J.J.3    Guth, S.4    Lehr, R.5    Prescott, C.D.6
  • 21
    • 33947716757 scopus 로고    scopus 로고
    • Probing the architecture of the B. subtilis RNase P holoenzyme active site by crosslinking and affinity cleavage
    • Niranjanakumari S., Day-Storms J.J., Ahmed M., Hsieh J., Zahler N.H., Venters R.A., Fierke C.A. Probing the architecture of the B. subtilis RNase P holoenzyme active site by crosslinking and affinity cleavage. RNA 2007, 13:512-535.
    • (2007) RNA , vol.13 , pp. 512-535
    • Niranjanakumari, S.1    Day-Storms, J.J.2    Ahmed, M.3    Hsieh, J.4    Zahler, N.H.5    Venters, R.A.6    Fierke, C.A.7
  • 22
    • 0032546728 scopus 로고    scopus 로고
    • Derivation of the three-dimensional architecture of bacterial ribonuclease P RNAs from comparative sequence analysis
    • Massire C., Jaeger L., Westhof E. Derivation of the three-dimensional architecture of bacterial ribonuclease P RNAs from comparative sequence analysis. J. Mol. Biol. 1998, 279:773-793.
    • (1998) J. Mol. Biol. , vol.279 , pp. 773-793
    • Massire, C.1    Jaeger, L.2    Westhof, E.3
  • 23
    • 67651007225 scopus 로고    scopus 로고
    • Conformational change in the Bacillus subtilis RNase P holoenzyme-pre-tRNA complex enhances substrate affinity and limits cleavage rate
    • Hsieh J., Fierke C.A. Conformational change in the Bacillus subtilis RNase P holoenzyme-pre-tRNA complex enhances substrate affinity and limits cleavage rate. RNA 2009, 15:1565-1577.
    • (2009) RNA , vol.15 , pp. 1565-1577
    • Hsieh, J.1    Fierke, C.A.2
  • 25
    • 0033779905 scopus 로고    scopus 로고
    • Ribonuclease P: a ribonucleoprotein enzyme
    • Kurz J.C., Fierke C.A. Ribonuclease P: a ribonucleoprotein enzyme. Curr. Opin. Chem. Biol. 2000, 4:553-558.
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 553-558
    • Kurz, J.C.1    Fierke, C.A.2
  • 26
    • 0037199416 scopus 로고    scopus 로고
    • The affinity of magnesium binding sites in the Bacillus subtilis RNase P-pre-tRNA complex is enhanced by the protein subunit
    • Kurz J.C., Fierke C.A. The affinity of magnesium binding sites in the Bacillus subtilis RNase P-pre-tRNA complex is enhanced by the protein subunit. Biochemistry 2002, 41:9545-9558.
    • (2002) Biochemistry , vol.41 , pp. 9545-9558
    • Kurz, J.C.1    Fierke, C.A.2
  • 27
    • 4043057879 scopus 로고    scopus 로고
    • Analysis of solvent nucleophile isotope effects: evidence for concerted mechanisms and nucleophilic activation by metal coordination in nonenzymatic and ribozyme-catalyzed phosphodiester hydrolysis
    • Cassano A.G., Anderson V.E., Harris M.E. Analysis of solvent nucleophile isotope effects: evidence for concerted mechanisms and nucleophilic activation by metal coordination in nonenzymatic and ribozyme-catalyzed phosphodiester hydrolysis. Biochemistry 2004, 43:10547-10559.
    • (2004) Biochemistry , vol.43 , pp. 10547-10559
    • Cassano, A.G.1    Anderson, V.E.2    Harris, M.E.3
  • 28
    • 0032590020 scopus 로고    scopus 로고
    • 2+-dependent folding of a large ribozyme without kinetic traps
    • 2+-dependent folding of a large ribozyme without kinetic traps. Nat. Struct. Biol. 1999, 6:1091-1095.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 1091-1095
    • Fang, X.W.1    Pan, T.2    Sosnick, T.R.3
  • 29
    • 0037173087 scopus 로고    scopus 로고
    • The rate-limiting step in the folding of a large ribozyme without kinetic traps
    • Fang X.W., Thiyagarajan P., Sosnick T.R., Pan T. The rate-limiting step in the folding of a large ribozyme without kinetic traps. Proc. Natl Acad. Sci. USA 2002, 99:8518-8523.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 8518-8523
    • Fang, X.W.1    Thiyagarajan, P.2    Sosnick, T.R.3    Pan, T.4
  • 30
    • 0036071392 scopus 로고    scopus 로고
    • Specific phosphorothioate substitutions probe the active site of Bacillus subtilis ribonuclease P
    • Crary S.M., Kurz J.C., Fierke C.A. Specific phosphorothioate substitutions probe the active site of Bacillus subtilis ribonuclease P. RNA 2002, 8:933-947.
    • (2002) RNA , vol.8 , pp. 933-947
    • Crary, S.M.1    Kurz, J.C.2    Fierke, C.A.3
  • 31
    • 0036445585 scopus 로고    scopus 로고
    • Conservation of helical structure contributes to functional metal ion interactions in the catalytic domain of ribonuclease P RNA
    • Kaye N.M., Zahler N.H., Christian E.L., Harris M.E. Conservation of helical structure contributes to functional metal ion interactions in the catalytic domain of ribonuclease P RNA. J. Mol. Biol. 2002, 324:429-442.
    • (2002) J. Mol. Biol. , vol.324 , pp. 429-442
    • Kaye, N.M.1    Zahler, N.H.2    Christian, E.L.3    Harris, M.E.4
  • 32
    • 0034002685 scopus 로고    scopus 로고
    • Helix P4 is a divalent metal ion binding site in the conserved core of the ribonuclease P ribozyme
    • Christian E.L., Kaye N.M., Harris M.E. Helix P4 is a divalent metal ion binding site in the conserved core of the ribonuclease P ribozyme. RNA 2000, 6:511-519.
    • (2000) RNA , vol.6 , pp. 511-519
    • Christian, E.L.1    Kaye, N.M.2    Harris, M.E.3
  • 33
    • 0035339722 scopus 로고    scopus 로고
    • Modular construction for function of a ribonucleoprotein enzyme: the catalytic domain of Bacillus subtilis RNase P complexed with B. subtilis RNase P protein
    • Loria A., Pan T. Modular construction for function of a ribonucleoprotein enzyme: the catalytic domain of Bacillus subtilis RNase P complexed with B. subtilis RNase P protein. Nucleic Acids Res. 2001, 29:1892-1897.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1892-1897
    • Loria, A.1    Pan, T.2
  • 34
    • 0029913930 scopus 로고    scopus 로고
    • In vitro selection of RNase P RNA reveals optimized catalytic activity in a highly conserved structural domain
    • Frank D.N., Ellington A.E., Pace N.R. In vitro selection of RNase P RNA reveals optimized catalytic activity in a highly conserved structural domain. RNA 1996, 2:1179-1188.
    • (1996) RNA , vol.2 , pp. 1179-1188
    • Frank, D.N.1    Ellington, A.E.2    Pace, N.R.3
  • 35
    • 0031475158 scopus 로고    scopus 로고
    • In vitro selection for altered divalent metal specificity in the RNase P RNA
    • Frank D.N., Pace N.R. In vitro selection for altered divalent metal specificity in the RNase P RNA. Proc. Natl Acad. Sci. USA 1997, 94:14355-14360.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 14355-14360
    • Frank, D.N.1    Pace, N.R.2
  • 36
    • 33846443976 scopus 로고    scopus 로고
    • 2+ binding properties of RNase P P4 from combined analysis of NMR residual dipolar couplings and motionally decoupled spin relaxation
    • 2+ binding properties of RNase P P4 from combined analysis of NMR residual dipolar couplings and motionally decoupled spin relaxation. RNA 2007, 13:251-266.
    • (2007) RNA , vol.13 , pp. 251-266
    • Getz, M.M.1    Andrews, A.J.2    Fierke, C.A.3    Al-Hashimi, H.M.4
  • 39
    • 0026792946 scopus 로고
    • Influence of metal ions on the ribonuclease P reaction. Distinguishing substrate binding from catalysis
    • Smith D., Burgin A.B., Haas E.S., Pace N.R. Influence of metal ions on the ribonuclease P reaction. Distinguishing substrate binding from catalysis. J. Biol. Chem. 1992, 267:2429-2436.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2429-2436
    • Smith, D.1    Burgin, A.B.2    Haas, E.S.3    Pace, N.R.4
  • 40
    • 58249097693 scopus 로고    scopus 로고
    • Pre-tRNA turnover catalyzed by the yeast nuclear RNase P holoenzyme is limited by product release
    • Hsieh J., Walker S.C., Fierke C.A., Engelke D.R. Pre-tRNA turnover catalyzed by the yeast nuclear RNase P holoenzyme is limited by product release. RNA 2009, 15:224-234.
    • (2009) RNA , vol.15 , pp. 224-234
    • Hsieh, J.1    Walker, S.C.2    Fierke, C.A.3    Engelke, D.R.4
  • 42
    • 4644305092 scopus 로고    scopus 로고
    • Ionic interactions between PRNA and P protein in Bacillus subtilis RNase P characterized using a magnetocapture-based assay
    • Day-Storms J.J., Niranjanakumari S., Fierke C.A. Ionic interactions between PRNA and P protein in Bacillus subtilis RNase P characterized using a magnetocapture-based assay. RNA 2004, 10:1595-1608.
    • (2004) RNA , vol.10 , pp. 1595-1608
    • Day-Storms, J.J.1    Niranjanakumari, S.2    Fierke, C.A.3
  • 43
    • 0033538479 scopus 로고    scopus 로고
    • Role of metal ions in the hydrolysis reaction catalyzed by RNase P RNA from Bacillus subtilis
    • Warnecke J.M., Held R., Busch S., Hartmann R.K. Role of metal ions in the hydrolysis reaction catalyzed by RNase P RNA from Bacillus subtilis. J. Mol. Biol. 1999, 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
  • 45
    • 0030806152 scopus 로고    scopus 로고
    • A conformational switch in Escherichia coli 16S ribosomal RNA during decoding of messenger RNA
    • Lodmell J.S., Dahlberg A.E. A conformational switch in Escherichia coli 16S ribosomal RNA during decoding of messenger RNA. Science 1997, 277:1262-1267.
    • (1997) Science , vol.277 , pp. 1262-1267
    • Lodmell, J.S.1    Dahlberg, A.E.2
  • 46
    • 0032488946 scopus 로고    scopus 로고
    • Molecular movement inside the translational engine
    • Wilson K.S., Noller H.F. Molecular movement inside the translational engine. Cell 1998, 92:337-349.
    • (1998) Cell , vol.92 , pp. 337-349
    • Wilson, K.S.1    Noller, H.F.2
  • 47
    • 0036074219 scopus 로고    scopus 로고
    • Dissection of a metal-ion-mediated conformational change in Tetrahymena ribozyme catalysis
    • Shan S.O., Herschlag D. Dissection of a metal-ion-mediated conformational change in Tetrahymena ribozyme catalysis. RNA 2002, 8:861-872.
    • (2002) RNA , vol.8 , pp. 861-872
    • Shan, S.O.1    Herschlag, D.2
  • 48
    • 0031552355 scopus 로고    scopus 로고
    • Multiple tertiary interactions involving domain II of group II self-splicing introns
    • Costa M., Deme E., Jacquier A., Michel F. Multiple tertiary interactions involving domain II of group II self-splicing introns. J. Mol. Biol. 1997, 267:520-536.
    • (1997) J. Mol. Biol. , vol.267 , pp. 520-536
    • Costa, M.1    Deme, E.2    Jacquier, A.3    Michel, F.4
  • 50
    • 0034687167 scopus 로고    scopus 로고
    • Cobalt hexammine inhibition of the hammerhead ribozyme
    • Horton T.E., DeRose V.J. Cobalt hexammine inhibition of the hammerhead ribozyme. Biochemistry 2000, 39:11408-11416.
    • (2000) Biochemistry , vol.39 , pp. 11408-11416
    • Horton, T.E.1    DeRose, V.J.2
  • 52
    • 0032417685 scopus 로고    scopus 로고
    • Protein component of the ribozyme ribonuclease P alters substrate recognition by directly contacting precursor tRNA
    • Niranjanakumari S., Stams T., Crary S.M., Christianson D.W., Fierke C.A. Protein component of the ribozyme ribonuclease P alters substrate recognition by directly contacting precursor tRNA. Proc. Natl Acad. Sci. USA 1998, 95:15212-15217.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 15212-15217
    • Niranjanakumari, S.1    Stams, T.2    Crary, S.M.3    Christianson, D.W.4    Fierke, C.A.5
  • 53
    • 74649084795 scopus 로고    scopus 로고
    • Protein-precursor tRNA contact leads to sequence-specific recognition of 5' leaders by bacterial ribonuclease P
    • Koutmou K.S., Zahler N.H., Kurz J.C., Campbell F.E., Harris M.E., Fierke C.A. Protein-precursor tRNA contact leads to sequence-specific recognition of 5' leaders by bacterial ribonuclease P. J. Mol. Biol. 2010, 396:195-208.
    • (2010) J. Mol. Biol. , vol.396 , pp. 195-208
    • Koutmou, K.S.1    Zahler, N.H.2    Kurz, J.C.3    Campbell, F.E.4    Harris, M.E.5    Fierke, C.A.6
  • 54
    • 0029286551 scopus 로고
    • Identification of phosphates involved in catalysis by the ribozyme RNase P RNA
    • Harris M.E., Pace N.R. Identification of phosphates involved in catalysis by the ribozyme RNase P RNA. RNA 1995, 1:210-218.
    • (1995) RNA , vol.1 , pp. 210-218
    • Harris, M.E.1    Pace, N.R.2
  • 55
    • 34548371821 scopus 로고    scopus 로고
    • Evidence that binding of C5 protein to P RNA enhances ribozyme catalysis by influencing active site metal ion affinity
    • Sun L., Harris M.E. Evidence that binding of C5 protein to P RNA enhances ribozyme catalysis by influencing active site metal ion affinity. RNA 2007, 13:1505-1515.
    • (2007) RNA , vol.13 , pp. 1505-1515
    • Sun, L.1    Harris, M.E.2
  • 56
    • 33746538312 scopus 로고    scopus 로고
    • The P4 metal binding site in RNase P RNA affects active site metal affinity through substrate positioning
    • Christian E.L., Smith K.M., Perera N., Harris M.E. The P4 metal binding site in RNase P RNA affects active site metal affinity through substrate positioning. RNA 2006, 12:1463-1467.
    • (2006) RNA , vol.12 , pp. 1463-1467
    • Christian, E.L.1    Smith, K.M.2    Perera, N.3    Harris, M.E.4
  • 57
    • 0027184481 scopus 로고
    • A general two-metal-ion mechanism for catalytic RNA
    • Steitz T.A., Steitz J.A. A general two-metal-ion mechanism for catalytic RNA. Proc. Natl Acad. Sci. USA 1993, 90:6498-6502.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6498-6502
    • Steitz, T.A.1    Steitz, J.A.2
  • 59
    • 0034602925 scopus 로고    scopus 로고
    • Evidence for helical unwinding of an RNA substrate by the RNA enzyme RNase P: use of an interstrand disulfide crosslink in substrate
    • Pomeranz Krummel D.A., Kent O., MacMillan A.M., Altman S. Evidence for helical unwinding of an RNA substrate by the RNA enzyme RNase P: use of an interstrand disulfide crosslink in substrate. J. Mol. Biol. 2000, 295:1113-1118.
    • (2000) J. Mol. Biol. , vol.295 , pp. 1113-1118
    • Pomeranz Krummel, D.A.1    Kent, O.2    MacMillan, A.M.3    Altman, S.4
  • 60
    • 0033529287 scopus 로고    scopus 로고
    • The cleavage step of ribonuclease P catalysis is determined by ribozyme-substrate interactions both distal and proximal to the cleavage site
    • Loria A., Pan T. The cleavage step of ribonuclease P catalysis is determined by ribozyme-substrate interactions both distal and proximal to the cleavage site. Biochemistry 1999, 38:8612-8620.
    • (1999) Biochemistry , vol.38 , pp. 8612-8620
    • Loria, A.1    Pan, T.2
  • 61
    • 34548501510 scopus 로고    scopus 로고
    • Evidence for induced fit in bacterial RNase P RNA-mediated cleavage
    • Brannvall M., Kikovska E., Wu S., Kirsebom L.A. Evidence for induced fit in bacterial RNase P RNA-mediated cleavage. J. Mol. Biol. 2007, 372:1149-1164.
    • (2007) J. Mol. Biol. , vol.372 , pp. 1149-1164
    • Brannvall, M.1    Kikovska, E.2    Wu, S.3    Kirsebom, L.A.4
  • 63
    • 33748361597 scopus 로고    scopus 로고
    • Evidence that substrate-specific effects of C5 protein lead to uniformity in binding and catalysis by RNase P
    • Sun L., Campbell F.E., Zahler N.H., Harris M.E. Evidence that substrate-specific effects of C5 protein lead to uniformity in binding and catalysis by RNase P. EMBO J. 2006, 25:3998-4007.
    • (2006) EMBO J. , vol.25 , pp. 3998-4007
    • Sun, L.1    Campbell, F.E.2    Zahler, N.H.3    Harris, M.E.4
  • 64
    • 0033773793 scopus 로고    scopus 로고
    • An improved synthesis of guanosine 5'-monothiophosphate
    • Behrman E. An improved synthesis of guanosine 5'-monothiophosphate. J. Chem. Res. 2000, S:446-447.
    • (2000) J. Chem. Res. , vol.S , pp. 446-447
    • Behrman, E.1
  • 65
    • 0032838373 scopus 로고    scopus 로고
    • Structural effects of cobalt-amine compounds on DNA condensation
    • Deng H., Bloomfield V.A. Structural effects of cobalt-amine compounds on DNA condensation. Biophys. J. 1999, 77:1556-1561.
    • (1999) Biophys. J. , vol.77 , pp. 1556-1561
    • Deng, H.1    Bloomfield, V.A.2
  • 66
    • 0024819449 scopus 로고
    • Synthesis of small RNAs using T7 RNA polymerase
    • Milligan J.F., Uhlenbeck O.C. Synthesis of small RNAs using T7 RNA polymerase. Methods Enzymol. 1989, 180:51-62.
    • (1989) Methods Enzymol. , vol.180 , pp. 51-62
    • Milligan, J.F.1    Uhlenbeck, O.C.2
  • 69
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch H. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 1967, 6:1948-1954.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 70
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill S.C., von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 1989, 182:319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    von Hippel, P.H.2
  • 71
    • 0026808625 scopus 로고
    • Thermodynamics of ligand-nucleic acid interactions
    • Lohman T.M., Mascotti D.P. Thermodynamics of ligand-nucleic acid interactions. Methods Enzymol. 1992, 212:400-424.
    • (1992) Methods Enzymol. , vol.212 , pp. 400-424
    • Lohman, T.M.1    Mascotti, D.P.2
  • 72
    • 0034808071 scopus 로고    scopus 로고
    • Structural dynamics of catalytic RNA highlighted by fluorescence resonance energy transfer
    • Walter N.G. Structural dynamics of catalytic RNA highlighted by fluorescence resonance energy transfer. Methods 2001, 25:19-30.
    • (2001) Methods , vol.25 , pp. 19-30
    • Walter, N.G.1
  • 73
    • 0041972623 scopus 로고    scopus 로고
    • 2+ ions slightly reorient stems I and II of the hammerhead ribozyme to increase the probability of formation of the catalytic core
    • 2+ ions slightly reorient stems I and II of the hammerhead ribozyme to increase the probability of formation of the catalytic core. Biochemistry 2003, 42:9924-9936.
    • (2003) Biochemistry , vol.42 , pp. 9924-9936
    • Rueda, D.1    Wick, K.2    McDowell, S.E.3    Walter, N.G.4
  • 74
    • 0032979707 scopus 로고    scopus 로고
    • Stability of hairpin ribozyme tertiary structure is governed by the interdomain junction
    • Walter N.G., Burke J.M., Millar D.P. Stability of hairpin ribozyme tertiary structure is governed by the interdomain junction. Nat. Struct. Biol. 1999, 6:544-549.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 544-549
    • Walter, N.G.1    Burke, J.M.2    Millar, D.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.