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Volumn 15, Issue 8, 2009, Pages 1565-1577

Conformational change in the Bacillus subtilis RNase P holoenzyme-pre-tRNA complex enhances substrate affinity and limits cleavage rate

Author keywords

Mechanism; Ribonuclease P; Transient kinetics

Indexed keywords

CALCIUM; HOLOENZYME; MAGNESIUM; NUCLEOTIDE; RIBONUCLEASE P; TRANSFER RNA;

EID: 67651007225     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.1639409     Document Type: Article
Times cited : (41)

References (67)
  • 2
    • 0027930184 scopus 로고
    • Asp catalyzed by the RNA component of Bacillus subtilis ribonuclease P
    • Asp catalyzed by the RNA component of Bacillus subtilis ribonuclease P. Biochemistry 33: 10294-10304.
    • (1994) Biochemistry , vol.33 , pp. 10294-10304
    • Beebe, J.A.1    Fierke, C.A.2
  • 3
    • 0033773793 scopus 로고    scopus 로고
    • An improved synthesis of guanosine 5′- monothiophosphate
    • Behrman E. 2000. An improved synthesis of guanosine 5′- monothiophosphate. J Chem Res 9: 446-447.
    • (2000) J Chem Res , vol.9 , pp. 446-447
    • Behrman, E.1
  • 4
    • 0034635354 scopus 로고    scopus 로고
    • Mapping RNA-protein interactions in ribonuclease P from Escherichia coli using disulfide-linked EDTA-Fe
    • Biswas R, Ledman DW, Fox RO, Altman S, Gopalan V. 2000. Mapping RNA-protein interactions in ribonuclease P from Escherichia coli using disulfide-linked EDTA-Fe. J Mol Biol 296: 19-31.
    • (2000) J Mol Biol , vol.296 , pp. 19-31
    • Biswas, R.1    Ledman, D.W.2    Fox, R.O.3    Altman, S.4    Gopalan, V.5
  • 5
    • 27144527101 scopus 로고    scopus 로고
    • Protein activation of a ribozyme: The role of bacterial RNase P protein
    • Buck AH, Dalby AB, Poole AW, Kazantsev AV, Pace NR. 2005a. Protein activation of a ribozyme: The role of bacterial RNase P protein. EMBO J 24: 3360-3368.
    • (2005) EMBO J , vol.24 , pp. 3360-3368
    • Buck, A.H.1    Dalby, A.B.2    Poole, A.W.3    Kazantsev, A.V.4    Pace, N.R.5
  • 6
    • 33645008830 scopus 로고    scopus 로고
    • Structural perspective on the activation of RNase P RNA by protein
    • Buck AH, Kazantsev AV, Dalby AB, Pace NR. 2005b. Structural perspective on the activation of RNase P RNA by protein. Nat Struct Mol Biol 12: 958-964.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 958-964
    • Buck, A.H.1    Kazantsev, A.V.2    Dalby, A.B.3    Pace, N.R.4
  • 7
    • 0347763703 scopus 로고    scopus 로고
    • Understanding the transition states of phosphodiester bond cleavage: Insights from heavy atom isotope effects
    • Cassano AG, Anderson VE, Harris ME. 2004. Understanding the transition states of phosphodiester bond cleavage: insights from heavy atom isotope effects. Biopolymers 73: 110-129.
    • (2004) Biopolymers , vol.73 , pp. 110-129
    • Cassano, A.G.1    Anderson, V.E.2    Harris, M.E.3
  • 8
    • 0022555857 scopus 로고
    • Biological catalysis by RNA
    • Cech TR, Bass BL. 1986. Biological catalysis by RNA. Annu Rev Biochem 55: 599-629.
    • (1986) Annu Rev Biochem , vol.55 , pp. 599-629
    • Cech, T.R.1    Bass, B.L.2
  • 9
    • 0033613230 scopus 로고    scopus 로고
    • The track of the pre-tRNA 5′ leader in the ribonuclease P ribozyme-substrate complex
    • Christian EL, Harris ME. 1999. The track of the pre-tRNA 5′ leader in the ribonuclease P ribozyme-substrate complex. Biochemistry 38: 12629-12638.
    • (1999) Biochemistry , vol.38 , pp. 12629-12638
    • Christian, E.L.1    Harris, M.E.2
  • 10
    • 0034002685 scopus 로고    scopus 로고
    • Helix P4 is a divalent metal ion binding site in the conserved core of the ribonuclease P ribozyme
    • Christian EL, Kaye NM, Harris ME. 2000. Helix P4 is a divalent metal ion binding site in the conserved core of the ribonuclease P ribozyme. RNA 6: 511-519.
    • (2000) RNA , vol.6 , pp. 511-519
    • Christian, E.L.1    Kaye, N.M.2    Harris, M.E.3
  • 11
    • 0036441045 scopus 로고    scopus 로고
    • Analysis of substrate recognition by the ribonucleoprotein endonuclease RNase P
    • Christian EL, Zahler NH, Kaye NM, Harris ME. 2002. Analysis of substrate recognition by the ribonucleoprotein endonuclease RNase P. Methods 28: 307-322.
    • (2002) Methods , vol.28 , pp. 307-322
    • Christian, E.L.1    Zahler, N.H.2    Kaye, N.M.3    Harris, M.E.4
  • 12
    • 0032581021 scopus 로고    scopus 로고
    • The protein component of Bacillus subtilis ribonuclease P increases catalytic efficiency by enhancing interactions with the 5′ leader sequence of pre-tRNAAsp
    • Crary SM, Niranjanakumari S, Fierke CA. 1998. The protein component of Bacillus subtilis ribonuclease P increases catalytic efficiency by enhancing interactions with the 5′ leader sequence of pre-tRNAAsp. Biochemistry 37: 9409-9416.
    • (1998) Biochemistry , vol.37 , pp. 9409-9416
    • Crary, S.M.1    Niranjanakumari, S.2    Fierke, C.A.3
  • 13
    • 0036071392 scopus 로고    scopus 로고
    • Specific phosphorothioate substitutions probe the active site of Bacillus subtilis ribonuclease P
    • Crary SM, Kurz JC, Fierke CA. 2002. Specific phosphorothioate substitutions probe the active site of Bacillus subtilis ribonuclease P. RNA 8: 933-947.
    • (2002) RNA , vol.8 , pp. 933-947
    • Crary, S.M.1    Kurz, J.C.2    Fierke, C.A.3
  • 14
    • 0037062949 scopus 로고    scopus 로고
    • The chemical repertoire of natural ribozymes
    • Doudna JA, Cech TR. 2002. The chemical repertoire of natural ribozymes. Nature 418: 222-228.
    • (2002) Nature , vol.418 , pp. 222-228
    • Doudna, J.A.1    Cech, T.R.2
  • 15
    • 33745166320 scopus 로고    scopus 로고
    • RNase P: Interface of the RNA and protein worlds
    • Evans D, Marquez SM, Pace NR. 2006. RNase P: Interface of the RNA and protein worlds. Trends Biochem Sci 31: 333-341.
    • (2006) Trends Biochem Sci , vol.31 , pp. 333-341
    • Evans, D.1    Marquez, S.M.2    Pace, N.R.3
  • 17
    • 33847775629 scopus 로고    scopus 로고
    • Uniformity amid diversity in RNase P
    • Gopalan V. 2007. Uniformity amid diversity in RNase P. Proc Natl Acad Sci 104: 2031-2032.
    • (2007) Proc Natl Acad Sci , vol.104 , pp. 2031-2032
    • Gopalan, V.1
  • 18
    • 0021013526 scopus 로고
    • The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme
    • Guerrier-Takada C, Gardiner K, Marsh T, Pace N, Altman S. 1983. The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme. Cell 35: 849-857.
    • (1983) Cell , vol.35 , pp. 849-857
    • Guerrier-Takada, C.1    Gardiner, K.2    Marsh, T.3    Pace, N.4    Altman, S.5
  • 20
    • 0028279011 scopus 로고
    • Further perspective on the catalytic core and secondary structure of ribonuclease P RNA
    • Haas ES, Brown JW, Pitulle C, Pace NR. 1994. Further perspective on the catalytic core and secondary structure of ribonuclease P RNA. Proc Natl Acad Sci 91: 2527-2531.
    • (1994) Proc Natl Acad Sci , vol.91 , pp. 2527-2531
    • Haas, E.S.1    Brown, J.W.2    Pitulle, C.3    Pace, N.R.4
  • 21
    • 1342302787 scopus 로고    scopus 로고
    • Dial tm for rescue: TmRNA engages ribosomes stalled on defective mRNAs
    • Haebel PW, Gutmann S, Ban N. 2004. Dial tm for rescue: tmRNA engages ribosomes stalled on defective mRNAs. Curr Opin Struct Biol 14: 58-65.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 58-65
    • Haebel, P.W.1    Gutmann, S.2    Ban, N.3
  • 22
    • 0036231352 scopus 로고    scopus 로고
    • Archaeal RNase P has multiple protein subunits homologous to eukaryotic nuclear RNase P proteins
    • Hall TA, Brown JW. 2002. Archaeal RNase P has multiple protein subunits homologous to eukaryotic nuclear RNase P proteins. RNA 8: 296-306.
    • (2002) RNA , vol.8 , pp. 296-306
    • Hall, T.A.1    Brown, J.W.2
  • 23
    • 0037008011 scopus 로고    scopus 로고
    • Multiple conformational changes in enzyme catalysis
    • Hammes GG. 2002. Multiple conformational changes in enzyme catalysis. Biochemistry 41: 8221-8228.
    • (2002) Biochemistry , vol.41 , pp. 8221-8228
    • Hammes, G.G.1
  • 25
    • 33744785989 scopus 로고    scopus 로고
    • How the group I intron works: A case study of RNA structure and function
    • 3rd ed, eds. RF Gesteland et al, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y
    • Hougland JL, Piccirilli JA, Forconi M, Lee J, Herschlag D. 2006. How the group I intron works: A case study of RNA structure and function. In: The RNA world, 3rd ed. (eds. RF Gesteland et al.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (2006) The RNA world
    • Hougland, J.L.1    Piccirilli, J.A.2    Forconi, M.3    Lee, J.4    Herschlag, D.5
  • 26
    • 0347763706 scopus 로고    scopus 로고
    • Roles of protein subunits in RNA-protein complexes: Lessons from ribonuclease P
    • Hsieh J, Andrews AJ, Fierke CA. 2004. Roles of protein subunits in RNA-protein complexes: lessons from ribonuclease P. Biopolymers 73: 79-89.
    • (2004) Biopolymers , vol.73 , pp. 79-89
    • Hsieh, J.1    Andrews, A.J.2    Fierke, C.A.3
  • 27
    • 0036210354 scopus 로고    scopus 로고
    • Human ribonuclease P: Subunits, function, and intranuclear localization
    • Jarrous N. 2002. Human ribonuclease P: Subunits, function, and intranuclear localization. RNA 8: 1-7.
    • (2002) RNA , vol.8 , pp. 1-7
    • Jarrous, N.1
  • 28
    • 34547102278 scopus 로고    scopus 로고
    • Human RNase P: A tRNA-processing enzyme and transcription factor
    • Jarrous N, Reiner R. 2007. Human RNase P: A tRNA-processing enzyme and transcription factor. Nucleic Acids Res 35: 3519-3524.
    • (2007) Nucleic Acids Res , vol.35 , pp. 3519-3524
    • Jarrous, N.1    Reiner, R.2
  • 29
    • 0642315208 scopus 로고
    • Transient-state kinetic analysis of enzyme reaction pathways
    • ed. DS Sigman, Academic, New York
    • Johnson KA. 1992. Transient-state kinetic analysis of enzyme reaction pathways. In: The enzymes (ed. DS Sigman), Vol. XX, pp. 1-61. Academic, New York.
    • (1992) The enzymes , vol.20 , pp. 1-61
    • Johnson, K.A.1
  • 31
    • 33847784925 scopus 로고    scopus 로고
    • Eukaryotic RNase P RNA mediates cleavage in the absence of protein
    • Kikovska E, Svard SG, Kirsebom LA. 2007. Eukaryotic RNase P RNA mediates cleavage in the absence of protein. Proc Natl Acad Sci 104: 2062-2067.
    • (2007) Proc Natl Acad Sci , vol.104 , pp. 2062-2067
    • Kikovska, E.1    Svard, S.G.2    Kirsebom, L.A.3
  • 32
    • 0028124122 scopus 로고
    • A tRNA-like structure is present in 10Sa RNA, a small stable RNA from Escherichia coli
    • Komine Y, Kitabatake M, Yokogawa T, Nishikawa K, Inokuchi H. 1994. A tRNA-like structure is present in 10Sa RNA, a small stable RNA from Escherichia coli. Proc Natl Acad Sci 91: 9223-9227.
    • (1994) Proc Natl Acad Sci , vol.91 , pp. 9223-9227
    • Komine, Y.1    Kitabatake, M.2    Yokogawa, T.3    Nishikawa, K.4    Inokuchi, H.5
  • 33
    • 67650797605 scopus 로고    scopus 로고
    • Kinetic mechanism of bacterial RNase P
    • eds. S Altman and F Liu, Springer, New York
    • Koutmou KS, Hsieh J, Fierke CA. 2009. Kinetic mechanism of bacterial RNase P. In: Ribonuclease P (eds. S Altman and F Liu). Springer, New York.
    • (2009) Ribonuclease P
    • Koutmou, K.S.1    Hsieh, J.2    Fierke, C.A.3
  • 34
    • 0033779905 scopus 로고    scopus 로고
    • Ribonuclease P: A ribonucleoprotein enzyme
    • Kurz JC, Fierke CA. 2000. Ribonuclease P: A ribonucleoprotein enzyme. Curr Opin Chem Biol 4: 553-558.
    • (2000) Curr Opin Chem Biol , vol.4 , pp. 553-558
    • Kurz, J.C.1    Fierke, C.A.2
  • 35
    • 0037199416 scopus 로고    scopus 로고
    • The affinity of magnesium binding sites in the Bacillus subtilis RNase P x pre-tRNA complex is enhanced by the protein subunit
    • Kurz JC, Fierke CA. 2002. The affinity of magnesium binding sites in the Bacillus subtilis RNase P x pre-tRNA complex is enhanced by the protein subunit. Biochemistry 41: 9545-9558.
    • (2002) Biochemistry , vol.41 , pp. 9545-9558
    • Kurz, J.C.1    Fierke, C.A.2
  • 37
    • 0345255620 scopus 로고    scopus 로고
    • A specific endoribonuclease, RNase P, affects gene expression of polycistronic operon mRNAs
    • Li Y, Altman S. 2003. A specific endoribonuclease, RNase P, affects gene expression of polycistronic operon mRNAs. Proc Natl Acad Sci 100: 13213-13218.
    • (2003) Proc Natl Acad Sci , vol.100 , pp. 13213-13218
    • Li, Y.1    Altman, S.2
  • 38
    • 0242515818 scopus 로고    scopus 로고
    • The effect of a single, temperature-sensitive mutation on global gene expression in Escherichia coli
    • Li Y, Cole K, Altman S. 2003. The effect of a single, temperature-sensitive mutation on global gene expression in Escherichia coli. RNA 9: 518-532.
    • (2003) RNA , vol.9 , pp. 518-532
    • Li, Y.1    Cole, K.2    Altman, S.3
  • 39
    • 0026793123 scopus 로고
    • Nonspecific ligand-DNA equilibrium binding parameters determined by fluorescence methods
    • Lohman TM, Mascotti DP. 1992. Nonspecific ligand-DNA equilibrium binding parameters determined by fluorescence methods. Methods Enzymol 212: 424-458.
    • (1992) Methods Enzymol , vol.212 , pp. 424-458
    • Lohman, T.M.1    Mascotti, D.P.2
  • 40
    • 0032516438 scopus 로고    scopus 로고
    • Recognition of the 5′ leader and the acceptor stem of a pre-tRNA substrate by the ribozyme from Bacillus subtilis RNase P
    • Loria A, Pan T. 1998. Recognition of the 5′ leader and the acceptor stem of a pre-tRNA substrate by the ribozyme from Bacillus subtilis RNase P. Biochemistry 37: 10126-10133.
    • (1998) Biochemistry , vol.37 , pp. 10126-10133
    • Loria, A.1    Pan, T.2
  • 41
    • 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. 1999. The cleavage step of ribonuclease P catalysis is determined by ribozyme-substrate interactions both distal and proximal to the cleavage site. Biochemistry 38: 8612-8620.
    • (1999) Biochemistry , vol.38 , pp. 8612-8620
    • Loria, A.1    Pan, T.2
  • 42
    • 0032480795 scopus 로고    scopus 로고
    • Recognition of a pre-tRNA substrate by the Bacillus subtilis RNase P holoenzyme
    • Loria A, Niranjanakumari S, Fierke CA, Pan T. 1998. Recognition of a pre-tRNA substrate by the Bacillus subtilis RNase P holoenzyme. Biochemistry 37: 15466-15473.
    • (1998) Biochemistry , vol.37 , pp. 15466-15473
    • Loria, A.1    Niranjanakumari, S.2    Fierke, C.A.3    Pan, T.4
  • 43
    • 0024819449 scopus 로고
    • Synthesis of small RNAs using T7 RNA polymerase
    • Milligan JF, Uhlenbeck OC. 1989. Synthesis of small RNAs using T7 RNA polymerase. Methods Enzymol 180: 51-62.
    • (1989) Methods Enzymol , vol.180 , pp. 51-62
    • Milligan, J.F.1    Uhlenbeck, O.C.2
  • 44
    • 0032126549 scopus 로고    scopus 로고
    • Expression, purification and characterization of the recombinant ribonuclease P protein component from Bacillus subtilis
    • Niranjanakumari S, Kurz JC, Fierke CA. 1998a. Expression, purification and characterization of the recombinant ribonuclease P protein component from Bacillus subtilis. Nucleic Acids Res 26: 3090-3096.
    • (1998) Nucleic Acids Res , vol.26 , pp. 3090-3096
    • Niranjanakumari, S.1    Kurz, J.C.2    Fierke, C.A.3
  • 45
    • 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 SM, Christianson DW, Fierke CA. 1998b. Protein component of the ribozyme ribonuclease P alters substrate recognition by directly contacting precursor tRNA. Proc Natl Acad Sci 95: 15212-15217.
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 15212-15217
    • Niranjanakumari, S.1    Stams, T.2    Crary, S.M.3    Christianson, D.W.4    Fierke, C.A.5
  • 46
    • 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 JJ, Ahmed M, Hsieh J, Zahler NH, Venters RA, Fierke CA. 2007. Probing the architecture of the B. subtilis RNase P Holoenzyme active site by crosslinking and affinity cleavage. RNA 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
  • 47
    • 0028962136 scopus 로고
    • Evolutionary perspective on the structure and function of ribonuclease P, a ribozyme
    • Pace NR, Brown JW. 1995. Evolutionary perspective on the structure and function of ribonuclease P, a ribozyme. J Bacteriol 177: 1919-1928.
    • (1995) J Bacteriol , vol.177 , pp. 1919-1928
    • Pace, N.R.1    Brown, J.W.2
  • 49
    • 0025826411 scopus 로고
    • Kinetics of the processing of the precursor to 4.5 S RNA, a naturally occurring substrate for RNase P from Escherichia coli
    • Peck-Miller KA, Altman S. 1991. Kinetics of the processing of the precursor to 4.5 S RNA, a naturally occurring substrate for RNase P from Escherichia coli. J Mol Biol 221: 1-5.
    • (1991) J Mol Biol , vol.221 , pp. 1-5
    • Peck-Miller, K.A.1    Altman, S.2
  • 51
    • 0023865082 scopus 로고
    • Role of the protein moiety of ribonuclease P, a ribonucleoprotein enzyme
    • Reich C, Olsen GJ, Pace B, Pace NR. 1988. Role of the protein moiety of ribonuclease P, a ribonucleoprotein enzyme. Science 239: 178-181.
    • (1988) Science , vol.239 , pp. 178-181
    • Reich, C.1    Olsen, G.J.2    Pace, B.3    Pace, N.R.4
  • 53
    • 44149107344 scopus 로고    scopus 로고
    • RNase P cleaves the adenine riboswitch and stabilizes pbuE mRNA in Bacillus subtilis
    • Seif E, Altman S. 2008. RNase P cleaves the adenine riboswitch and stabilizes pbuE mRNA in Bacillus subtilis. RNA 14: 1237-1243.
    • (2008) RNA , vol.14 , pp. 1237-1243
    • Seif, E.1    Altman, S.2
  • 54
    • 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
  • 55
    • 0026792946 scopus 로고
    • Influence of metal ions on the ribonuclease P reaction. Distinguishing substrate binding from catalysis
    • Smith D, Burgin AB, Haas ES, Pace NR. 1992. Influence of metal ions on the ribonuclease P reaction. Distinguishing substrate binding from catalysis. J Biol Chem 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
  • 56
    • 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 ME. 2007. Evidence that binding of C5 protein to P RNA enhances ribozyme catalysis by influencing active site metal ion affinity. RNA 13: 1505-1515.
    • (2007) RNA , vol.13 , pp. 1505-1515
    • Sun, L.1    Harris, M.E.2
  • 57
    • 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 FE, Zahler NH, Harris ME. 2006. Evidence that substrate-specific effects of C5 protein lead to uniformity in binding and catalysis by RNase P. EMBO J 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
  • 58
    • 0027174003 scopus 로고
    • Product release is a rate-limiting step during cleavage by the catalytic RNA subunit of Escherichia coli RNase P
    • Tallsjo A, Kirsebom LA. 1993. Product release is a rate-limiting step during cleavage by the catalytic RNA subunit of Escherichia coli RNase P. Nucleic Acids Res 21: 51-57.
    • (1993) Nucleic Acids Res , vol.21 , pp. 51-57
    • Tallsjo, A.1    Kirsebom, L.A.2
  • 60
    • 0037462929 scopus 로고    scopus 로고
    • Molecular modeling of the three-dimensional structure of the bacterial RNase P holoenzyme
    • Tsai HY, Masquida B, Biswas R, Westhof E, Gopalan V. 2003. Molecular modeling of the three-dimensional structure of the bacterial RNase P holoenzyme. J Mol Biol 325: 661-675.
    • (2003) J Mol Biol , vol.325 , pp. 661-675
    • Tsai, H.Y.1    Masquida, B.2    Biswas, R.3    Westhof, E.4    Gopalan, V.5
  • 61
    • 33645747326 scopus 로고    scopus 로고
    • Ribonuclease P: The evolution of an ancient RNA enzyme
    • Walker SC, Engelke DR. 2006. Ribonuclease P: The evolution of an ancient RNA enzyme. Crit Rev Biochem Mol Biol 41: 77-102.
    • (2006) Crit Rev Biochem Mol Biol , vol.41 , pp. 77-102
    • Walker, S.C.1    Engelke, D.R.2
  • 62
    • 0032522574 scopus 로고    scopus 로고
    • Tertiary structure formation in the hairpin ribozyme monitored by fluorescence resonance energy transfer
    • Walter NG, Hampel KJ, Brown KM, Burke JM. 1998. Tertiary structure formation in the hairpin ribozyme monitored by fluorescence resonance energy transfer. EMBO J 17: 2378-2391.
    • (1998) EMBO J , vol.17 , pp. 2378-2391
    • Walter, N.G.1    Hampel, K.J.2    Brown, K.M.3    Burke, J.M.4
  • 63
    • 0027389805 scopus 로고
    • Gap-scan deletion analysis of Bacillus subtilis RNase P RNA
    • Waugh DS, Pace NR. 1993. Gap-scan deletion analysis of Bacillus subtilis RNase P RNA. FASEB J 7: 188-195.
    • (1993) FASEB J , vol.7 , pp. 188-195
    • Waugh, D.S.1    Pace, N.R.2
  • 65
    • 0038475910 scopus 로고    scopus 로고
    • Recognition of the 5′ leader of pre-tRNA substrates by the active site of ribonuclease P
    • Zahler NH, Christian EL, Harris ME. 2003. Recognition of the 5′ leader of pre-tRNA substrates by the active site of ribonuclease P. RNA 9: 734-745.
    • (2003) RNA , vol.9 , pp. 734-745
    • Zahler, N.H.1    Christian, E.L.2    Harris, M.E.3
  • 66
    • 11844256433 scopus 로고    scopus 로고
    • The pre-tRNA nucleotide base and 2′-hydroxyl at N(-1) contribute to fidelity in tRNA processing by RNase P
    • Zahler NH, Sun L, Christian EL, Harris ME. 2005. The pre-tRNA nucleotide base and 2′-hydroxyl at N(-1) contribute to fidelity in tRNA processing by RNase P. J Mol Biol 345: 969-985.
    • (2005) J Mol Biol , vol.345 , pp. 969-985
    • Zahler, N.H.1    Sun, L.2    Christian, E.L.3    Harris, M.E.4
  • 67
    • 0035916939 scopus 로고    scopus 로고
    • Correlation between processing efficiency for ribonuclease P minimal substrates and conformation of the nucleotide -1 at the cleavage position
    • Zuleeg T, Hansen A, Pfeiffer T, Schubel H, Kreutzer R, Hartmann RK, Limmer S. 2001. Correlation between processing efficiency for ribonuclease P minimal substrates and conformation of the nucleotide -1 at the cleavage position. Biochemistry 40: 3363-3369.
    • (2001) Biochemistry , vol.40 , pp. 3363-3369
    • Zuleeg, T.1    Hansen, A.2    Pfeiffer, T.3    Schubel, H.4    Kreutzer, R.5    Hartmann, R.K.6    Limmer, S.7


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