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Volumn 290, Issue 2, 1999, Pages 433-445

Role of metal ions in the hydrolysis reaction catalyzed by RNase P RNA from Bacillus subtilis

Author keywords

Cadmium rescue; Catalytic mechanism; Manganese rescue; Ribozymes; Rp and Sp phosphorothioate modifications

Indexed keywords

BACTERIAL RNA; CADMIUM; CALCIUM ION; MAGNESIUM ION; MANGANESE; METAL ION; OXYGEN; RIBONUCLEASE P; RNA PRECURSOR; TRANSFER RNA;

EID: 0033538479     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2890     Document Type: Article
Times cited : (86)

References (43)
  • 1
    • 0027930184 scopus 로고
    • Aspcatalyzed by the RNA component of Bacillus subtilis ribonuclease P
    • Aspcatalyzed by the RNA component of Bacillus subtilis ribonuclease P. Biochemistry. 33:1994;10294-10304.
    • (1994) Biochemistry , vol.33 , pp. 10294-10304
    • Beebe, J.A.1    Fierke, C.A.2
  • 3
    • 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 C. A., Steitz T. A. Structural principles for the inhibition of the 3′-5′ exonuclease activity of Escherichia coli DNA polymerase I by phosphorothioates. J. Mol. Biol. 277:1998;363-377.
    • (1998) J. Mol. Biol. , vol.277 , pp. 363-377
    • Brautigam, C.A.1    Steitz, T.A.2
  • 4
    • 0026606958 scopus 로고
    • Ribonuclease P RNA and protein subunits from bacteria
    • Brown J. W., Pace N. R. Ribonuclease P RNA and protein subunits from bacteria. Nucl. Acids Res. 20:1992;1451-1456.
    • (1992) Nucl. Acids Res. , vol.20 , pp. 1451-1456
    • Brown, J.W.1    Pace, N.R.2
  • 5
    • 0032473358 scopus 로고    scopus 로고
    • Comparative photocross-linking analysis of the tertiary structure of Escherichia coli and Bacillus subtilis RNase P RNAs
    • Chen J.-L., Nolan J. M., Harris M. E., Pace N. R. Comparative photocross-linking analysis of the tertiary structure of Escherichia coli and Bacillus subtilis RNase P RNAs. EMBO J. 17:1998;1515-1525.
    • (1998) EMBO J. , vol.17 , pp. 1515-1525
    • Chen, J.-L.1    Nolan, J.M.2    Harris, M.E.3    Pace, N.R.4
  • 6
    • 0031027138 scopus 로고    scopus 로고
    • 2+coordinated to the pro -Rp oxygen of the scissile bond
    • 2+coordinated to the pro -Rp oxygen of the scissile bond. Biochemistry. 36:1997;2425-2438.
    • (1997) Biochemistry , vol.36 , pp. 2425-2438
    • Chen, Y.1    Li, X.2    Gegenheimer, P.3
  • 8
    • 0027732494 scopus 로고
    • Evidence for the role of solvated metal hydroxide in the hammerhead cleavage mechanism
    • Dahm S. C., Derrick W. B., Uhlenbeck O. C. Evidence for the role of solvated metal hydroxide in the hammerhead cleavage mechanism. Biochemistry. 32:1993;13040-13045.
    • (1993) Biochemistry , vol.32 , pp. 13040-13045
    • Dahm, S.C.1    Derrick, W.B.2    Uhlenbeck, O.C.3
  • 10
    • 0022418143 scopus 로고
    • Bond order and charge localization in nucleoside phosphorothioates
    • Frey P. A., Sammons R. D. Bond order and charge localization in nucleoside phosphorothioates. Science. 228:1985;541-545.
    • (1985) Science , vol.228 , pp. 541-545
    • Frey, P.A.1    Sammons, R.D.2
  • 11
    • 0021870425 scopus 로고
    • Ion dependence of the Bacillus subtilis RNase P reaction
    • Gardiner K. J., Marsh T. L., Pace N. R. Ion dependence of the Bacillus subtilis RNase P reaction. J. Biol. Chem. 260:1985;5415-5419.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5415-5419
    • Gardiner, K.J.1    Marsh, T.L.2    Pace, N.R.3
  • 12
    • 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. The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme. Cell. 35:1983;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
  • 13
    • 0022530665 scopus 로고
    • Metal ion requirements and other aspects of the reaction catalyzed by M1 RNA, the RNA subunit of ribonuclease P fromEscherichia coli
    • Guerrier-Takada C., Haydock K., Allen L., Altman S. Metal ion requirements and other aspects of the reaction catalyzed by M1 RNA, the RNA subunit of ribonuclease P fromEscherichia coli. Biochemistry. 25:1986;1509-1515.
    • (1986) Biochemistry , vol.25 , pp. 1509-1515
    • Guerrier-Takada, C.1    Haydock, K.2    Allen, L.3    Altman, S.4
  • 14
    • 0029803926 scopus 로고    scopus 로고
    • Structure and evolution of ribonuclease P RNA in Gram-positive bacteria
    • Haas E. S., Banta A. B., Harris J. K., Pace N. R., Brown J. W. Structure and evolution of ribonuclease P RNA in Gram-positive bacteria. Nucl. Acids Res. 24:1996;4775-4782.
    • (1996) Nucl. Acids Res. , vol.24 , pp. 4775-4782
    • Haas, E.S.1    Banta, A.B.2    Harris, J.K.3    Pace, N.R.4    Brown, J.W.5
  • 16
    • 0028934068 scopus 로고
    • Kinetics and thermodynamics of the RNase P RNA cleavage reaction: Analysis of tRNA 3′-end variants
    • Hardt W.-D., Schlegl J., Erdmann V. A., Hartmann R. K. Kinetics and thermodynamics of the RNase P RNA cleavage reaction: analysis of tRNA 3′-end variants. J. Mol. Biol. 247:1995;161-172.
    • (1995) J. Mol. Biol. , vol.247 , pp. 161-172
    • Hardt, W.-D.1    Schlegl, J.2    Erdmann, V.A.3    Hartmann, R.K.4
  • 17
    • 0029905957 scopus 로고    scopus 로고
    • Rp-deoxy-phosphorothioate modification interference experiments identify 2′-OH groups in RNase P RNA that are crucial to tRNA binding
    • Hardt W.-D., Erdmann V. A., Hartmann R. K. Rp-deoxy-phosphorothioate modification interference experiments identify 2′-OH groups in RNase P RNA that are crucial to tRNA binding. RNA. 2:1996;1189-1198.
    • (1996) RNA , vol.2 , pp. 1189-1198
    • Hardt, W.-D.1    Erdmann, V.A.2    Hartmann, R.K.3
  • 18
    • 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. Ribozyme-catalyzed and nonenzymatic reactions of phosphate diesters: rate effects upon substitution of sulfur for a nonbridging phosphoryl oxygen atom. Biochemistry. 30:1991;4844-4854.
    • (1991) Biochemistry , vol.30 , pp. 4844-4854
    • Herschlag, D.1    Piccirilli, J.A.2    Cech, T.R.3
  • 19
    • 0027973546 scopus 로고
    • Base pairing between Escherichia coli RNase P RNA and its substrate
    • Kirsebom L. A., Svärd S. G. Base pairing between Escherichia coli RNase P RNA and its substrate. EMBO J. 13:1994;4870-4876.
    • (1994) EMBO J. , vol.13 , pp. 4870-4876
    • Kirsebom, L.A.1    Svärd, S.G.2
  • 21
    • 0028146083 scopus 로고
    • Phylogenetic comparative chemical footprint analysis of the interaction between ribonuclease P RNA and tRNA
    • LaGrandeur T. E., Hüttenhofer A., Noller H. F., Pace N. R. Phylogenetic comparative chemical footprint analysis of the interaction between ribonuclease P RNA and tRNA. EMBO J. 13:1994;3945-3952.
    • (1994) EMBO J. , vol.13 , pp. 3945-3952
    • Lagrandeur, T.E.1    Hüttenhofer, A.2    Noller, H.F.3    Pace, N.R.4
  • 22
    • 0029949699 scopus 로고    scopus 로고
    • Domain structure of the ribozyme from eubacterial ribonuclease P
    • Loria A., Pan T. Domain structure of the ribozyme from eubacterial ribonuclease P. RNA. 2:1996;551-563.
    • (1996) RNA , vol.2 , pp. 551-563
    • Loria, A.1    Pan, T.2
  • 23
    • 0031009290 scopus 로고    scopus 로고
    • Recognition of the T stem-loop of a pre-tRNA substrate by the ribozyme from Bacillus subtilis ribonuclease P
    • Loria A., Pan T. Recognition of the T stem-loop of a pre-tRNA substrate by the ribozyme from Bacillus subtilis ribonuclease P. Biochemistry. 36:1997;6317-6325.
    • (1997) Biochemistry , vol.36 , pp. 6317-6325
    • Loria, A.1    Pan, T.2
  • 24
    • 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. Recognition of the 5′ leader and the acceptor stem of a pre-tRNA substrate by the ribozyme from Bacillus subtilis RNase P. Biochemistry. 37:1998;10126-10133.
    • (1998) Biochemistry , vol.37 , pp. 10126-10133
    • Loria, A.1    Pan, T.2
  • 26
    • 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. 279:1998;773-793.
    • (1998) J. Mol. Biol. , vol.279 , pp. 773-793
    • Massire, C.1    Jaeger, L.2    Westhof, E.3
  • 27
    • 0030750183 scopus 로고    scopus 로고
    • Effects of divalent metal ions on individual steps of the Tetrahymena ribozyme reaction
    • McConnell T. S., Herschlag D., Cech T. R. Effects of divalent metal ions on individual steps of the Tetrahymena ribozyme reaction. Biochemistry. 36:1997;8293-8303.
    • (1997) Biochemistry , vol.36 , pp. 8293-8303
    • McConnell, T.S.1    Herschlag, D.2    Cech, T.R.3
  • 28
    • 0028945859 scopus 로고
    • Higher order folding and domain analysis of the ribozyme from Bacillus subtilis ribonuclease P
    • Pan T. Higher order folding and domain analysis of the ribozyme from Bacillus subtilis ribonuclease P. Biochemistry. 34:1995;902-909.
    • (1995) Biochemistry , vol.34 , pp. 902-909
    • Pan, T.1
  • 29
    • 0028088780 scopus 로고
    • Selection of circularly permuted ribozymes from Bacillus subtilis RNase P by substrate binding
    • Pan T., Zhong K. Selection of circularly permuted ribozymes from Bacillus subtilis RNase P by substrate binding. Biochemistry. 33:1994;14207-14212.
    • (1994) Biochemistry , vol.33 , pp. 14207-14212
    • Pan, T.1    Zhong, K.2
  • 30
    • 0029556990 scopus 로고
    • Probing of tertiary interactions in RNA: 2′-hydroxyl-base contacts between the RNase P RNA and pre-tRNA
    • Pan T., Loria A., Zhong K. Probing of tertiary interactions in RNA: 2′-hydroxyl-base contacts between the RNase P RNA and pre-tRNA. Proc. Natl Acad. Sci. USA. 92:1995;12510-12514.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 12510-12514
    • Pan, T.1    Loria, A.2    Zhong, K.3
  • 31
    • 0023865082 scopus 로고
    • Role of the protein moiety of ribonuclease P, a ribonucleoprotein enzyme
    • Reich C., Olsen G. J., Pace B., Pace N. R. Role of the protein moiety of ribonuclease P, a ribonucleoprotein enzyme. Science. 239:1988;178-181.
    • (1988) Science , vol.239 , pp. 178-181
    • Reich, C.1    Olsen, G.J.2    Pace, B.3    Pace, N.R.4
  • 32
    • 0026613980 scopus 로고
    • Cleavage efficiencies of model substrates for ribonuclease P from Escherichia coli and Thermus thermophilus
    • Schlegl J., Fürste J. P., Bald R., Erdmann V. A., Hartmann R. K. Cleavage efficiencies of model substrates for ribonuclease P from Escherichia coli and Thermus thermophilus. Nucl. Acids Res. 20:1992;5963-5970.
    • (1992) Nucl. Acids Res. , vol.20 , pp. 5963-5970
    • Schlegl, J.1    Fürste, J.P.2    Bald, R.3    Erdmann, V.A.4    Hartmann, R.K.5
  • 33
    • 0003518480 scopus 로고
    • New York: John Wiley & Sons, Inc. p. 100-107
    • Segel I. H. Enzyme Kinetics. 1993a;John Wiley & Sons, Inc. New York. p. 100-107.
    • (1993) Enzyme Kinetics
    • Segel, I.H.1
  • 34
    • 0003518480 scopus 로고
    • New York: John Wiley & Sons, Inc. p. 465-473
    • Segel I. H. Enzyme Kinetics. 1993b;John Wiley & Sons, Inc. New York. p. 465-473.
    • (1993) Enzyme Kinetics
    • Segel, I.H.1
  • 35
    • 0027256149 scopus 로고
    • Multiple magnesium ions in the ribonuclease P reaction mechanism
    • Smith D., Pace N. R. Multiple magnesium ions in the ribonuclease P reaction mechanism. Biochemistry. 32:1993;5273-5281.
    • (1993) Biochemistry , vol.32 , pp. 5273-5281
    • Smith, D.1    Pace, N.R.2
  • 36
    • 0026792946 scopus 로고
    • Influence of Metal Ions on the Ribonuclease P Reaction
    • Smith D., Burgin A. B., Haas E. S., Pace N. R. Influence of Metal Ions on the Ribonuclease P Reaction. J. Biol. Chem. 267:1992;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
  • 37
    • 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. 280:1998;752-755.
    • (1998) Science , vol.280 , pp. 752-755
    • Stams, T.1    Niranjanakumari, S.2    Fierke, C.A.3    Christianson, D.W.4
  • 38
    • 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. 90:1993;6498-6502.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6498-6502
    • Steitz, T.A.1    Steitz, J.A.2
  • 39
    • 77957219383 scopus 로고
    • Product release is a rate-limiting step during cleavage by the catalytic RNA subunit of Escherichia coli RNase P
    • Tallsjö A., Kirsebom L. A. Product release is a rate-limiting step during cleavage by the catalytic RNA subunit of Escherichia coli RNase P. Nucl. Acids Res. 21:1993;51-57.
    • (1993) Nucl. Acids Res. , vol.21 , pp. 51-57
    • Tallsjö, A.1    Kirsebom, L.A.2
  • 40
    • 0023141241 scopus 로고
    • Structural analysis of the 3′-distal portion of the two rDNA operons from Thermus thermophilus HB8
    • Vogel D. W., Hartmann R. K., Kröger B., Ulbrich N., Erdmann V. A. Structural analysis of the 3′-distal portion of the two rDNA operons from Thermus thermophilus HB8. Biochem. Internat. 14:1987;167-175.
    • (1987) Biochem. Internat. , vol.14 , pp. 167-175
    • Vogel, D.W.1    Hartmann, R.K.2    Kröger, B.3    Ulbrich, N.4    Erdmann, V.A.5
  • 42
    • 0030792415 scopus 로고    scopus 로고
    • Role of metal ions in the cleavage mechanism by the E. coli RNase P holoenzyme
    • Warnecke J. M., Green C. J., Hartmann R. K. Role of metal ions in the cleavage mechanism by the E. coli RNase P holoenzyme. Nucleosides Nucleotides. 16:1997;721-725.
    • (1997) Nucleosides Nucleotides , vol.16 , pp. 721-725
    • Warnecke, J.M.1    Green, C.J.2    Hartmann, R.K.3
  • 43
    • 0029958503 scopus 로고    scopus 로고
    • Slow folding kinetics of RNase P RNA
    • Zarrinkar P. P., Wang J., Williamson J. R. Slow folding kinetics of RNase P RNA. RNA. 2:1996;564-573.
    • (1996) RNA , vol.2 , pp. 564-573
    • Zarrinkar, P.P.1    Wang, J.2    Williamson, J.R.3


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