메뉴 건너뛰기




Volumn 12, Issue 9, 2006, Pages 1661-1670

Hybrid E. coli - Mitochondrial ribonuclease P RNAs are catalytically active

Author keywords

Jakobids; Mitochondria; RNA secondary structure; RNase P; Tetraloop motifs

Indexed keywords

HYBRID PROTEIN; MESSENGER RNA; PROTEIN SUBUNIT; RIBONUCLEASE P; RIBONUCLEOPROTEIN; RNA; TRANSFER RNA;

EID: 33748163076     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.52106     Document Type: Article
Times cited : (23)

References (60)
  • 1
    • 0001636640 scopus 로고
    • Recent studies of RNase P
    • eds. D. Soll and U. RajBhandry, American Society for Microbiology Press, Washington DC
    • Altman, S., Kirsebom, L.A., and Talbot, S. 1995. Recent studies of RNase P. In tRNA structure, biosynthesis, and functions (eds. D. Soll and U. RajBhandry), pp. 67-78. American Society for Microbiology Press, Washington DC.
    • (1995) tRNA Structure, Biosynthesis, and Functions , pp. 67-78
    • Altman, S.1    Kirsebom, L.A.2    Talbot, S.3
  • 2
    • 0024316780 scopus 로고
    • Characterization in vitro of the defect in a temperature-sensitive mutant of the protein subunit of RNase P from Escherichia coli
    • Baer, M.F., Wesolowski, D., and Altman, S. 1989. Characterization in vitro of the defect in a temperature-sensitive mutant of the protein subunit of RNase P from Escherichia coli. J. Bacteriol. 171: 6862-6866.
    • (1989) J. Bacteriol. , vol.171 , pp. 6862-6866
    • Baer, M.F.1    Wesolowski, D.2    Altman, S.3
  • 3
    • 0029917137 scopus 로고    scopus 로고
    • RNase P from a photosynthetic organelle contains an RNA homologous to the cyanobacterial counterpart
    • Baum, M., Cordier, A., and Schon, A. 1996. RNase P from a photosynthetic organelle contains an RNA homologous to the cyanobacterial counterpart. J. Mol. Biol. 257: 43-52.
    • (1996) J. Mol. Biol. , vol.257 , pp. 43-52
    • Baum, M.1    Cordier, A.2    Schon, A.3
  • 4
    • 6044276865 scopus 로고    scopus 로고
    • Cross talk between the +73/294 interaction and the cleavage site in RNase P RNA mediated cleavage
    • Brannvall, M., Kikovska, E., and Kirsebom, L.A. 2004. Cross talk between the +73/294 interaction and the cleavage site in RNase P RNA mediated cleavage. Nucleic Acids Res. 32: 5418-5429.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 5418-5429
    • Brannvall, M.1    Kikovska, E.2    Kirsebom, L.A.3
  • 5
    • 0344298926 scopus 로고    scopus 로고
    • The ribonuclease P database
    • Brown, J.W. 1999. The ribonuclease P database. Nucleic Acids Res. 27: 314.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 314
    • Brown, J.W.1
  • 7
    • 0029935208 scopus 로고    scopus 로고
    • Comparative analysis of ribonuclease P RNA using gene sequences from natural microbial populations reveals tertiary structural elements
    • Brown, J.W., Nolan, J.M., Haas, E.S., Rubio, M.A., Major, F., and Pace, N.R. 1996. Comparative analysis of ribonuclease P RNA using gene sequences from natural microbial populations reveals tertiary structural elements. Proc. Natl. Acad. Sci. 93: 3001-3006.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 3001-3006
    • Brown, J.W.1    Nolan, J.M.2    Haas, E.S.3    Rubio, M.A.4    Major, F.5    Pace, N.R.6
  • 9
    • 0031156668 scopus 로고    scopus 로고
    • Identification of the universally conserved core of ribonuclease P RNA
    • Chen, J.L. and Pace, N.R. 1997. Identification of the universally conserved core of ribonuclease P RNA. RNA 3: 557-560.
    • (1997) RNA , vol.3 , pp. 557-560
    • Chen, J.L.1    Pace, N.R.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, E.L., Kaye, N.M., and Harris, M.E. 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
    • 0025183518 scopus 로고
    • Similar cage-shaped structures for the RNA components of all ribonuclease P and ribonuclease MRP enzymes
    • Forster, A.C. and Altman, S. 1990. Similar cage-shaped structures for the RNA components of all ribonuclease P and ribonuclease MRP enzymes. Cell 62: 407-409.
    • (1990) Cell , vol.62 , pp. 407-409
    • Forster, A.C.1    Altman, S.2
  • 12
    • 0031711821 scopus 로고    scopus 로고
    • Ribonuclease P: Unity and diversity in a tRNA processing ribozyme
    • Frank, D.N. and Pace, N.R. 1998. Ribonuclease P: Unity and diversity in a tRNA processing ribozyme. Annu. Rev. Biochem. 67: 153-180.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 153-180
    • Frank, D.N.1    Pace, N.R.2
  • 13
    • 0019128225 scopus 로고
    • RNase P of Bacillus subtilis has a RNA component
    • Gardiner, K. and Pace, N.R. 1980. RNase P of Bacillus subtilis has a RNA component. J. Biol. Chem. 255: 7507-7509.
    • (1980) J. Biol. Chem. , vol.255 , pp. 7507-7509
    • Gardiner, K.1    Pace, N.R.2
  • 14
    • 0021870425 scopus 로고
    • Ion dependence of the Bacillus subtilis RNase P reaction
    • Gardiner, K.J., Marsh, T.L., and Pace, N.R. 1985. Ion dependence of the Bacillus subtilis RNase P reaction. J. Biol. Chem. 260: 5415-5419.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5415-5419
    • Gardiner, K.J.1    Marsh, T.L.2    Pace, N.R.3
  • 15
    • 0026527506 scopus 로고
    • Reconstitution of enzymatic activity from fragments of M1 RNA
    • Guerrier-Takada, C. and Altman, S. 1992. Reconstitution of enzymatic activity from fragments of M1 RNA. Proc. Natl. Acad. Sci. 89:1266-1270.
    • (1992) Proc. Natl. Acad. Sci. , vol.89 , pp. 1266-1270
    • Guerrier-Takada, C.1    Altman, S.2
  • 16
    • 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., and 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
  • 17
    • 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., and Altman, S. 1986. Metal ion requirements and other aspects of the reaction catalyzed by M1 RNA, the RNA subunit of ribonuclease P from Escherichia coli. Biochemistry 25: 1509-1515.
    • (1986) Biochemistry , vol.25 , pp. 1509-1515
    • Guerrier-Takada, C.1    Haydock, K.2    Allen, L.3    Altman, S.4
  • 18
    • 0028856792 scopus 로고
    • Artificial regulation of gene expression in Escherichia coli by RNase P
    • Guerrier-Takada, C., Li, Y., and Altman, S. 1995. Artificial regulation of gene expression in Escherichia coli by RNase P. Proc. Natl. Acad. Sci. 92: 11115-11119.
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 11115-11119
    • Guerrier-Takada, C.1    Li, Y.2    Altman, S.3
  • 19
    • 0032530462 scopus 로고    scopus 로고
    • Evolutionary variation in bacterial RNase P RNAs
    • Haas, E.S. and Brown, J.W. 1998. Evolutionary variation in bacterial RNase P RNAs. Nucleic Acids Res. 26: 4093-4099.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4093-4099
    • Haas, E.S.1    Brown, J.W.2
  • 20
    • 0032518591 scopus 로고    scopus 로고
    • Purification and characterization of the nuclear ribonuclease P of Aspergillus nidulans
    • Han, S.J., Lee, B.J., and Kang, H.S. 1998. Purification and characterization of the nuclear ribonuclease P of Aspergillus nidulans. Eur. J. Biochem. 251: 244-251.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 244-251
    • Han, S.J.1    Lee, B.J.2    Kang, H.S.3
  • 21
    • 0141450351 scopus 로고    scopus 로고
    • The enigma of ribonuclease P evolution
    • Hartmann, E. and Hartmann, R.K. 2003. The enigma of ribonuclease P evolution. Trends Genet. 19: 561-569.
    • (2003) Trends Genet. , vol.19 , pp. 561-569
    • Hartmann, E.1    Hartmann, R.K.2
  • 22
    • 0026423027 scopus 로고
    • Structural features that give rise to the unusual stability of RNA hairpins containing GNRA loops
    • Heus, H.A. and Pardi, A. 1991. Structural features that give rise to the unusual stability of RNA hairpins containing GNRA loops. Science 253: 191-194.
    • (1991) Science , vol.253 , pp. 191-194
    • Heus, H.A.1    Pardi, A.2
  • 23
    • 0022623266 scopus 로고
    • RNase P activity in the mitochondria of Saccharomyces cerevisiae depends on both mitochondrion and nucleus-encoded components
    • Hollingsworth, M.J. and Martin, N.C. 1986. RNase P activity in the mitochondria of Saccharomyces cerevisiae depends on both mitochondrion and nucleus-encoded components. Mol. Cell. Biol. 6: 1058-1064.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 1058-1064
    • Hollingsworth, M.J.1    Martin, N.C.2
  • 24
    • 1642569682 scopus 로고    scopus 로고
    • Loss of the mRNA-like region in mitochondrial tmRNAs of jakobids
    • Jacob, Y., Seif, E., Paquet, P.O., and Lang, B.F. 2004. Loss of the mRNA-like region in mitochondrial tmRNAs of jakobids. RNA 10: 605-614.
    • (2004) RNA , vol.10 , pp. 605-614
    • Jacob, Y.1    Seif, E.2    Paquet, P.O.3    Lang, B.F.4
  • 25
    • 0028294458 scopus 로고
    • Involvement of a GNRA tetraloop in long-range RNA tertiary interactions
    • Jaeger, L., Michel, F., and Westhof, E. 1994. Involvement of a GNRA tetraloop in long-range RNA tertiary interactions. J. Mol. Biol. 236: 1271-1276.
    • (1994) J. Mol. Biol. , vol.236 , pp. 1271-1276
    • Jaeger, L.1    Michel, F.2    Westhof, E.3
  • 26
    • 0026691092 scopus 로고
    • Characterization of ribonuclease P isolated from rat liver cytosol
    • Jayanthi, G.P. and Van Tuyle, G.C. 1992. Characterization of ribonuclease P isolated from rat liver cytosol. Arch. Biochem. Biophys. 296: 264-270.
    • (1992) Arch. Biochem. Biophys. , vol.296 , pp. 264-270
    • Jayanthi, G.P.1    Van Tuyle, G.C.2
  • 27
    • 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., and Harris, M.E. 2002. Conservation of helical structure contributes to functional metal ion interactions in the catalytic domain of ribonuclease P RNA. J. Mol. Biol. 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
  • 28
    • 0027973546 scopus 로고
    • Base pairing between Escherichia coli RNase P RNA and its substrate
    • Kirsebom, L.A. and Svard, S.G. 1994. Base pairing between Escherichia coli RNase P RNA and its substrate. EMBO J. 13: 4870-4876.
    • (1994) EMBO J. , vol.13 , pp. 4870-4876
    • Kirsebom, L.A.1    Svard, S.G.2
  • 29
    • 0019416148 scopus 로고
    • Partial purification of RNase P from Schizosaccharomyces pombe
    • Kline, L., Nishikawa, S., and Soll, D. 1981. Partial purification of RNase P from Schizosaccharomyces pombe. J. Biol. Chem. 256: 5058-5063.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5058-5063
    • Kline, L.1    Nishikawa, S.2    Soll, D.3
  • 30
    • 0031849761 scopus 로고    scopus 로고
    • The P15-loop of Escherichia coli RNase P RNA is an autonomous divalent metal ion binding domain
    • Kufel, J. and Kirsebom, L.A. 1998. The P15-loop of Escherichia coli RNase P RNA is an autonomous divalent metal ion binding domain. RNA 4: 777-788.
    • (1998) RNA , vol.4 , pp. 777-788
    • Kufel, J.1    Kirsebom, L.A.2
  • 32
    • 0033367329 scopus 로고    scopus 로고
    • Mitochondrial genome evolution and the origin of eukaryotes
    • Lang, B.F., Gray, M.W., and Burger, G. 1999. Mitochondrial genome evolution and the origin of eukaryotes. Annu. Rev. Genet. 33: 351-397.
    • (1999) Annu. Rev. Genet. , vol.33 , pp. 351-397
    • Lang, B.F.1    Gray, M.W.2    Burger, G.3
  • 33
    • 0030027214 scopus 로고    scopus 로고
    • Purification and characterization of mitochondrial ribonuclease P from Aspergillus nidulans
    • Lee, Y.C., Lee, B.J., Hwang, D.S., and Kang, H.S. 1996a. Purification and characterization of mitochondrial ribonuclease P from Aspergillus nidulans. Eur. J. Biochem. 235: 289-296.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 289-296
    • Lee, Y.C.1    Lee, B.J.2    Hwang, D.S.3    Kang, H.S.4
  • 34
    • 0030023377 scopus 로고    scopus 로고
    • The RNA component of mitochondrial ribonuclease P from Aspergillus nidulans
    • Lee, Y.C., Lee, B.J., and Kang, H.S. 1996b. The RNA component of mitochondrial ribonuclease P from Aspergillus nidulans. Eur. J. Biochem. 235: 297-303.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 297-303
    • Lee, Y.C.1    Lee, B.J.2    Kang, H.S.3
  • 35
    • 0029949699 scopus 로고    scopus 로고
    • Domain structure of the ribozyme from eubacterial ribonuclease P
    • Loria, A. and Pan, T. 1996. Domain structure of the ribozyme from eubacterial ribonuclease P. RNA 2: 551-563.
    • (1996) RNA , vol.2 , pp. 551-563
    • Loria, A.1    Pan, T.2
  • 36
    • 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
    • _. 2001. 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. 29: 1892-1897.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1892-1897
  • 37
    • 0028484051 scopus 로고
    • Characterization and partial purification of tRNA processing activities from potato mitochondria
    • Marchfelder, A. and Brennicke, A. 1994. Characterization and partial purification of tRNA processing activities from potato mitochondria. Plant Physiol. 105: 1247-1254.
    • (1994) Plant Physiol. , vol.105 , pp. 1247-1254
    • Marchfelder, A.1    Brennicke, A.2
  • 38
    • 0031158312 scopus 로고    scopus 로고
    • Phylogenetic evidence for a new tertiary interaction in bacterial RNase P RNAs
    • Massire, C., Jaeger, L., and Westhof, E. 1997. Phylogenetic evidence for a new tertiary interaction in bacterial RNase P RNAs. RNA 3: 553-556.
    • (1997) RNA , vol.3 , pp. 553-556
    • Massire, C.1    Jaeger, L.2    Westhof, E.3
  • 39
    • 0032546728 scopus 로고    scopus 로고
    • Derivation of the three-dimensional architecture of bacterial ribonuclease P RNAs from comparative sequence analysis
    • _. 1998. Derivation of the three-dimensional architecture of bacterial ribonuclease P RNAs from comparative sequence analysis. J. Mol. Biol. 279: 773-793.
    • (1998) J. Mol. Biol. , vol.279 , pp. 773-793
  • 40
    • 0026646109 scopus 로고
    • A 105-kDa protein is required for yeast mitochondrial RNase P activity
    • Morales, M.J., Dang, Y.L., Lou, Y.C., Sulo, P., and Martin, N.C. 1992. A 105-kDa protein is required for yeast mitochondrial RNase P activity. Proc. Natl. Acad. Sci. 89: 9875-9879.
    • (1992) Proc. Natl. Acad. Sci. , vol.89 , pp. 9875-9879
    • Morales, M.J.1    Dang, Y.L.2    Lou, Y.C.3    Sulo, P.4    Martin, N.C.5
  • 41
    • 0028301674 scopus 로고
    • GAAA tetraloop and conserved bulge stabilize tertiary structure of a group I intron domain
    • Murphy, F.L. and Cech, T.R. 1994. GAAA tetraloop and conserved bulge stabilize tertiary structure of a group I intron domain. J. Mol. Biol. 236: 49-63.
    • (1994) J. Mol. Biol. , vol.236 , pp. 49-63
    • Murphy, F.L.1    Cech, T.R.2
  • 43
    • 2142676545 scopus 로고    scopus 로고
    • Verification of phylogenetic predictions in vivo and the importance of the tetraloop motif in a catalytic RNA
    • Pomeranz-Krummel, D.A. and Altman, S. 1999. Verification of phylogenetic predictions in vivo and the importance of the tetraloop motif in a catalytic RNA. Proc. Natl. Acad. Sci. 96: 11200-11205.
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 11200-11205
    • Pomeranz-Krummel, D.A.1    Altman, S.2
  • 44
    • 0037055279 scopus 로고    scopus 로고
    • G350 of Escherichia coli RNase P RNA contributes to Mg2+ binding near the active site of the enzyme
    • Rasmussen, T.A. and Nolan, J.M. 2002. G350 of Escherichia coli RNase P RNA contributes to Mg2+ binding near the active site of the enzyme. Gene 294: 177-185.
    • (2002) Gene , vol.294 , pp. 177-185
    • Rasmussen, T.A.1    Nolan, J.M.2
  • 45
    • 0042333223 scopus 로고    scopus 로고
    • Mitochondrial RNase P RNAs in ascomycete fungi: Lineage-specific variations in RNA secondary structure
    • Seif, E.R., Forget, L., Martin, N.C., and Lang, B.F. 2003. Mitochondrial RNase P RNAs in ascomycete fungi: Lineage-specific variations in RNA secondary structure. RNA 9: 1073-1083.
    • (2003) RNA , vol.9 , pp. 1073-1083
    • Seif, E.R.1    Forget, L.2    Martin, N.C.3    Lang, B.F.4
  • 46
    • 13844319861 scopus 로고    scopus 로고
    • Comparative mitochondrial genomics in zygomycetes: Bacterialike RNase P RNAs, mobile elements and a close source of the group I intron invasion in angiosperms
    • Seif, E., Leigh, J., Liu, Y., Roewer, I., Forget, L., and Lang, B.F. 2005. Comparative mitochondrial genomics in zygomycetes: Bacterialike RNase P RNAs, mobile elements and a close source of the group I intron invasion in angiosperms. Nucleic Acids Res. 33: 734-744.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 734-744
    • Seif, E.1    Leigh, J.2    Liu, Y.3    Roewer, I.4    Forget, L.5    Lang, B.F.6
  • 47
    • 0025938886 scopus 로고
    • RNase P RNA in Candida glabrata mitochondria is transcribed with substrate tRNAs
    • Shu, H.H. and Martin, N.C. 1991. RNase P RNA in Candida glabrata mitochondria is transcribed with substrate tRNAs. Nucleic Acids Res. 19: 6221-6226.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 6221-6226
    • Shu, H.H.1    Martin, N.C.2
  • 48
    • 0029853929 scopus 로고    scopus 로고
    • Mycoplasma fermentans simplifies our view of the catalytic core of ribonuclease P RNA
    • Siegel, R.W., Banta, A.B., Haas, E.S., Brown, J.W., and Pace, N.R. 1996. Mycoplasma fermentans simplifies our view of the catalytic core of ribonuclease P RNA. RNA 2: 452-462.
    • (1996) RNA , vol.2 , pp. 452-462
    • Siegel, R.W.1    Banta, A.B.2    Haas, E.S.3    Brown, J.W.4    Pace, N.R.5
  • 49
    • 0017855369 scopus 로고
    • Ribonuclease P: An enzyme with an essential RNA component
    • Stark, B.C., Kole, R., Bowman, E.J., and Altman, S. 1978. Ribonuclease P: An enzyme with an essential RNA component. Proc. Natl. Acad. Sci. 75: 3717-3721.
    • (1978) Proc. Natl. Acad. Sci. , vol.75 , pp. 3717-3721
    • Stark, B.C.1    Kole, R.2    Bowman, E.J.3    Altman, S.4
  • 50
    • 0034843686 scopus 로고    scopus 로고
    • Extensive deproteinization of Dictyostelium discoideum RNase P reveals a new catalytic activity
    • Stathopoulos, C., Tekos, A., Zarkadis, I.K., and Drainas, D. 2001. Extensive deproteinization of Dictyostelium discoideum RNase P reveals a new catalytic activity. Eur. J. Biochem. 268: 2134-2140.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2134-2140
    • Stathopoulos, C.1    Tekos, A.2    Zarkadis, I.K.3    Drainas, D.4
  • 51
    • 11144353440 scopus 로고    scopus 로고
    • The complete mitochondrial genome of the yeast Kluyveromyces thermotolerans
    • Talla, E., Anthouard, V., Bouchier, C., Frangeul, L., and Dujon, B. 2005. The complete mitochondrial genome of the yeast Kluyveromyces thermotolerans. FEBS Lett. 579: 30-40.
    • (2005) FEBS Lett. , vol.579 , pp. 30-40
    • Talla, E.1    Anthouard, V.2    Bouchier, C.3    Frangeul, L.4    Dujon, B.5
  • 52
    • 4544384889 scopus 로고    scopus 로고
    • Examining the bases of the J3/4 domain of Escherichia coli ribonuclease P
    • Tanaka, T., Ando, T., Haga, S., and Kikuchi, Y. 2004a. Examining the bases of the J3/4 domain of Escherichia coli ribonuclease P. Biosci. Biotechnol. Biochem. 68: 1388-1392.
    • (2004) Biosci. Biotechnol. Biochem. , vol.68 , pp. 1388-1392
    • Tanaka, T.1    Ando, T.2    Haga, S.3    Kikuchi, Y.4
  • 53
    • 7544238297 scopus 로고    scopus 로고
    • The P3 domain of E. coli ribonuclease P RNA can be truncated and replaced
    • Tanaka, T., Kanda, N., and Kikuchi, Y. 2004b. The P3 domain of E. coli ribonuclease P RNA can be truncated and replaced. FEBS Lett. 577: 101-104.
    • (2004) FEBS Lett. , vol.577 , pp. 101-104
    • Tanaka, T.1    Kanda, N.2    Kikuchi, Y.3
  • 54
    • 0034004463 scopus 로고    scopus 로고
    • Evidence for an RNA-based catalytic mechanism in eukaryotic nuclear ribonuclease P
    • Thomas, B.C., Chamberlain, J., Engelke, D.R., and Gegenheimer, P. 2000. Evidence for an RNA-based catalytic mechanism in eukaryotic nuclear ribonuclease P. RNA 6: 554-562.
    • (2000) RNA , vol.6 , pp. 554-562
    • Thomas, B.C.1    Chamberlain, J.2    Engelke, D.R.3    Gegenheimer, P.4
  • 56
    • 0033197514 scopus 로고    scopus 로고
    • The complete mitochondrial DNA sequences of Nephroselmis olivacea and Pedinomonas minor. Two radically different evolutionary patterns within green algae
    • Turmel, M., Lemieux, C., Burger, G., Lang, B.F., Otis, C., Plante, I., and Gray, M.W. 1999. The complete mitochondrial DNA sequences of Nephroselmis olivacea and Pedinomonas minor. Two radically different evolutionary patterns within green algae. Plant Cell 11: 1717-1730.
    • (1999) Plant Cell , vol.11 , pp. 1717-1730
    • Turmel, M.1    Lemieux, C.2    Burger, G.3    Lang, B.F.4    Otis, C.5    Plante, I.6    Gray, M.W.7
  • 57
    • 0032463935 scopus 로고    scopus 로고
    • Partial characterization of the ribonuclease P from Tetrahymena pyriformis
    • Vainauskas, S., Stribinskis, V., Padegimas, L., and Juodka, B. 1998. Partial characterization of the ribonuclease P from Tetrahymena pyriformis. Biochimie 80: 595-604.
    • (1998) Biochimie , vol.80 , pp. 595-604
    • Vainauskas, S.1    Stribinskis, V.2    Padegimas, L.3    Juodka, B.4
  • 58
    • 0035875539 scopus 로고    scopus 로고
    • The first phytoplasma RNase P RNA provides new insights into the sequence requirements of this ribozyme
    • Wagner, M., Fingerhut, C., Gross, H.J., and Schon, A. 2001. The first phytoplasma RNase P RNA provides new insights into the sequence requirements of this ribozyme. Nucleic Acids Res. 29: 2661-2665.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2661-2665
    • Wagner, M.1    Fingerhut, C.2    Gross, H.J.3    Schon, A.4
  • 59
    • 0029866752 scopus 로고    scopus 로고
    • Mapping in three dimensions of regions in a catalytic RNA protected from attack by an Fe(II)-EDTA reagent
    • Westhof, E., Wesolowski, D., and Altman, S. 1996. Mapping in three dimensions of regions in a catalytic RNA protected from attack by an Fe(II)-EDTA reagent. J. Mol. Biol. 258: 600-613.
    • (1996) J. Mol. Biol. , vol.258 , pp. 600-613
    • Westhof, E.1    Wesolowski, D.2    Altman, S.3
  • 60
    • 0025933235 scopus 로고
    • Dramatic size variation of yeast mitochondrial RNAs suggests that RNase P RNAs can be quite small
    • Wise, C.A. and Martin, N.C. 1991. Dramatic size variation of yeast mitochondrial RNAs suggests that RNase P RNAs can be quite small. J. Biol. Chem. 266: 19154-19157.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19154-19157
    • Wise, C.A.1    Martin, N.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.