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Volumn 292, Issue 1, 1999, Pages 53-63

Manganese ions induce miscleavage in the escherichia coli RNase P RNA-catalyzed reaction

Author keywords

Catalytic RNA; Divalent metal ions; Ribozyme; RNase P

Indexed keywords

MANGANESE; METAL ION; RIBONUCLEASE; RIBONUCLEASE P; RIBOZYME;

EID: 0242366429     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3048     Document Type: Article
Times cited : (37)

References (39)
  • 1
    • 0003120548 scopus 로고    scopus 로고
    • Ribonuclease P
    • R. F. Gesteland, T. Cech, & J. F. Atkins. Cold Spring Harbor: Cold Spring Harbor Laboratory Press
    • Altman S., Kirsebom L. A. Ribonuclease P. Gesteland R. F., Cech T., Atkins J. F. The RNA World. 1999;351-380 Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
    • (1999) The RNA World , pp. 351-380
    • Altman, S.1    Kirsebom, L.A.2
  • 2
    • 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
    • 0032491460 scopus 로고    scopus 로고
    • RNase P RNA structure and cleavage reflect the primary structure of tRNA genes
    • Brännvall M., Mattsson J. G., Svärd S. G., Kirsebom L. A. RNase P RNA structure and cleavage reflect the primary structure of tRNA genes. J. Mol. Biol. 283:1998;771-783.
    • (1998) J. Mol. Biol. , vol.283 , pp. 771-783
    • Brännvall, M.1    Mattsson, J.G.2    Svärd, S.G.3    Kirsebom, L.A.4
  • 4
    • 0003251937 scopus 로고    scopus 로고
    • Appendix 1 Structures of base-pairs involving at least two hydrogen bonds
    • R. F. Gesteland, T. Cech, & J. F. Atkins. Cold Spring Harbor: Cold Spring Harbor Laboratory Press
    • Burkard M. E., Turner D. H., Tinoco I. Jr. Appendix 1 Structures of base-pairs involving at least two hydrogen bonds. Gesteland R. F., Cech T., Atkins J. F. The RNA World. 1999;675-680 Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
    • (1999) The RNA World , pp. 675-680
    • Burkard, M.E.1    Turner, D.H.2    Tinoco I., Jr.3
  • 5
    • 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
  • 9
    • 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
  • 10
    • 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
  • 11
    • 0022530665 scopus 로고
    • Metal ion requirements and other aspects of the reaction catalyzed by M1 RNA, the RNA subunit of ribonuclease P from Escherichia 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 from Escherichia 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
  • 12
    • 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
  • 14
    • 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
    • 0017361887 scopus 로고
    • A crystallographic study of metal-binding to yeast phenylalanine transfer RNA
    • Jack A., Ladner J. E., Rhodes D., Brown R. S., Klug A. A crystallographic study of metal-binding to yeast phenylalanine transfer RNA. J. Mol. Biol. 111:1977;315-328.
    • (1977) J. Mol. Biol. , vol.111 , pp. 315-328
    • Jack, A.1    Ladner, J.E.2    Rhodes, D.3    Brown, R.S.4    Klug, A.5
  • 18
    • 0025992237 scopus 로고
    • Site-specific cleavage by metal ion cofactors and inhibitors of M1 RNA, the catalytic subunit of RNase P from Escherichia coli
    • Kazakov S., Altman S. Site-specific cleavage by metal ion cofactors and inhibitors of M1 RNA, the catalytic subunit of RNase P from Escherichia coli. Proc. Natl Acad. Sci. USA. 88:1991;9193-9197.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 9193-9197
    • Kazakov, S.1    Altman, S.2
  • 19
    • 0029131905 scopus 로고
    • RNase P-a "scarlet Pimpernel"
    • Kirsebom L. A. RNase P-a "Scarlet Pimpernel" Mol. Microbiol. 17:1995;411-420.
    • (1995) Mol. Microbiol. , vol.17 , pp. 411-420
    • Kirsebom, L.A.1
  • 20
    • 0026555146 scopus 로고
    • The kinetics and specificity of cleavage by RNase P is mainly dependent on the structure of the amino acid acceptor stem
    • Kirsebom L. A., Svärd S. G. The kinetics and specificity of cleavage by RNase P is mainly dependent on the structure of the amino acid acceptor stem. Nucl. Acids Res. 20:1992;425-432.
    • (1992) Nucl. Acids Res. , vol.20 , pp. 425-432
    • Kirsebom, L.A.1    Svärd, S.G.2
  • 21
    • 0027228358 scopus 로고
    • Identification of a region within M1 RNA of Escherichia coli RNase P important for the location of the cleavage site on a wild-type tRNA precursor
    • Kirsebom L. A., Svärd S. G. Identification of a region within M1 RNA of Escherichia coli RNase P important for the location of the cleavage site on a wild-type tRNA precursor. J. Mol. Biol. 231:1993;594-604.
    • (1993) J. Mol. Biol. , vol.231 , pp. 594-604
    • Kirsebom, L.A.1    Svärd, S.G.2
  • 22
    • 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
  • 23
    • 0027967452 scopus 로고
    • Cleavage site selection by M1 RNA, the catalytic subunit of Escherichia coli RNase P, is influenced by pH
    • Kufel J., Kirsebom L. A. Cleavage site selection by M1 RNA, the catalytic subunit of Escherichia coli RNase P, is influenced by pH. J. Mol. Biol. 244:1994;511-521.
    • (1994) J. Mol. Biol. , vol.244 , pp. 511-521
    • Kufel, J.1    Kirsebom, L.A.2
  • 24
    • 0029898934 scopus 로고    scopus 로고
    • Different cleavage sites are aligned differently in the active site of M1 RNA, the catalytic subunit of Escherichia coli RNase P
    • Kufel J., Kirsebom L. A. Different cleavage sites are aligned differently in the active site of M1 RNA, the catalytic subunit of Escherichia coli RNase P. Proc. Natl Acad. Sci. USA. 93:1996a;6085-6090.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 6085-6090
    • Kufel, J.1    Kirsebom, L.A.2
  • 25
    • 0030589091 scopus 로고    scopus 로고
    • Residues in Escherichia coli RNase P RNA important for cleavage site selection and divalent metal ion binding
    • Kufel J., Kirsebom L. A. Residues in Escherichia coli RNase P RNA important for cleavage site selection and divalent metal ion binding. J. Mol. Biol. 263:1996b;685-698.
    • (1996) J. Mol. Biol. , vol.263 , pp. 685-698
    • Kufel, J.1    Kirsebom, L.A.2
  • 26
    • 0031849761 scopus 로고    scopus 로고
    • The P15-loop of Escherichia coli RNase P RNA is an autonomous divalent metal ion binding domain
    • Kufel J., Kirsebom L. A. The P15-loop of Escherichia coli RNase P RNA is an autonomous divalent metal ion binding domain. RNA. 4:1998;777-788.
    • (1998) RNA , vol.4 , pp. 777-788
    • Kufel, J.1    Kirsebom, L.A.2
  • 28
  • 30
    • 0026684994 scopus 로고
    • Important 2′-hydroxyl groups in model substrates for M1 RNA, the catalytic RNA subunit of RNase P from Escherichia coli
    • Perreault J.-P., Altman S. Important 2′-hydroxyl groups in model substrates for M1 RNA, the catalytic RNA subunit of RNase P from Escherichia coli. J. Mol. Biol. 226:1992;399-409.
    • (1992) J. Mol. Biol. , vol.226 , pp. 399-409
    • Perreault, J.-P.1    Altman, S.2
  • 31
    • 0027223564 scopus 로고
    • Pathway of activation by magnesium ions of substrates for the catalytic subunit of RNase P RNA from Escherichia coli
    • Perreault J.-P., Altman S. Pathway of activation by magnesium ions of substrates for the catalytic subunit of RNase P RNA from Escherichia coli. J. Mol. Biol. 230:1993;750-756.
    • (1993) J. Mol. Biol. , vol.230 , pp. 750-756
    • Perreault, J.-P.1    Altman, S.2
  • 32
    • 84984087935 scopus 로고
    • Electrophoresis of DNA. II. Specific interactions of univalent and divalent cations with DNA
    • Ross P. D., Scruggs R. L. Electrophoresis of DNA. II. Specific interactions of univalent and divalent cations with DNA. Biopolymers. 2:1964;79-89.
    • (1964) Biopolymers , vol.2 , pp. 79-89
    • Ross, P.D.1    Scruggs, R.L.2
  • 33
    • 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
  • 34
    • 0029903905 scopus 로고    scopus 로고
    • Phylogenetic comparative mutational analysis of the base-pairing between RNase P RNA and its substrate
    • Svärd S. G., Kagardt U., Kirsebom L. A. Phylogenetic comparative mutational analysis of the base-pairing between RNase P RNA and its substrate. RNA. 2:1996;463-472.
    • (1996) RNA , vol.2 , pp. 463-472
    • Svärd, S.G.1    Kagardt, U.2    Kirsebom, L.A.3
  • 35
    • 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
  • 36
    • 0029827586 scopus 로고    scopus 로고
    • Interaction between Escherichia coli RNase P RNA and the discriminator base results in slow product release
    • Tallsjö A., Kufel J., Kirsebom L. A. Interaction between Escherichia coli RNase P RNA and the discriminator base results in slow product release. RNA. 2:1996;299-307.
    • (1996) RNA , vol.2 , pp. 299-307
    • Tallsjö, A.1    Kufel, J.2    Kirsebom, L.A.3
  • 38
    • 0023696278 scopus 로고
    • Protein-RNA interactions in the RNase P holoenzyme from Escherichia coli
    • Vioque A., Arnez J., Altman S. Protein-RNA interactions in the RNase P holoenzyme from Escherichia coli. J. Mol. Biol. 202:1988;835-848.
    • (1988) J. Mol. Biol. , vol.202 , pp. 835-848
    • Vioque, A.1    Arnez, J.2    Altman, S.3
  • 39
    • 0027729890 scopus 로고
    • Lead-catalyzed cleavage of ribonuclease P RNA as a probe for integrity of tertiary structure
    • Zito K., Hüttenhofer A., Pace N. R. Lead-catalyzed cleavage of ribonuclease P RNA as a probe for integrity of tertiary structure. Nucl. Acids Res. 21:1993;5916-5920.
    • (1993) Nucl. Acids Res. , vol.21 , pp. 5916-5920
    • Zito, K.1    Hüttenhofer, A.2    Pace, N.R.3


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