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Volumn 64, Issue 6, 2012, Pages 521-528

Ribonucleases P/MRP and the expanding ribonucleoprotein world

Author keywords

ncRNA; ribozyme; RNase MRP; RNase P; RNP world; rRNA processing; tRNA processing

Indexed keywords

RIBONUCLEASE; RIBONUCLEASE MRP; RIBONUCLEASE P; RIBONUCLEOPROTEIN; UNCLASSIFIED DRUG;

EID: 84861326296     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.1052     Document Type: Review
Times cited : (18)

References (105)
  • 1
    • 0037123632 scopus 로고    scopus 로고
    • An expanding universe of noncoding RNAs
    • Storz, G., (2002) An expanding universe of noncoding RNAs. Science 296, 1260-1263.
    • (2002) Science , vol.296 , pp. 1260-1263
    • Storz, G.1
  • 2
    • 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
  • 3
    • 4644225942 scopus 로고    scopus 로고
    • In search of RNase P RNA from microbial genomes
    • Li, Y., and, Altman, S., (2004) In search of RNase P RNA from microbial genomes. RNA 10, 1533-1540.
    • (2004) RNA , vol.10 , pp. 1533-1540
    • Li, Y.1    Altman, S.2
  • 4
    • 23344445110 scopus 로고    scopus 로고
    • Identification and analysis of ribonuclease P and MRP RNA in a broad range of eukaryotes
    • Piccinelli, P., Rosenblad, M. A., and, Samuelsson, T., (2005) Identification and analysis of ribonuclease P and MRP RNA in a broad range of eukaryotes. Nucleic Acids Res. 33, 4485-4495.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 4485-4495
    • Piccinelli, P.1    Rosenblad, M.A.2    Samuelsson, T.3
  • 6
    • 44649177016 scopus 로고    scopus 로고
    • 5'-end maturation of tRNA in Aquifex aeolicus
    • Marszalkowski, M., Willkomm, D. K., and, Hartmann, R. K., (2008) 5'-end maturation of tRNA in Aquifex aeolicus. Biol. Chem. 389, 395-403.
    • (2008) Biol. Chem. , vol.389 , pp. 395-403
    • Marszalkowski, M.1    Willkomm, D.K.2    Hartmann, R.K.3
  • 7
    • 37449003265 scopus 로고    scopus 로고
    • RNA processing in Aquifex aeolicus involves RNase E/G and an RNase P-like activity
    • Lombo, T. B., and, Kaberdin, V. R., (2008) RNA processing in Aquifex aeolicus involves RNase E/G and an RNase P-like activity. Biochem. Biophys. Res. Commun. 366, 457-463.
    • (2008) Biochem. Biophys. Res. Commun. , vol.366 , pp. 457-463
    • Lombo, T.B.1    Kaberdin, V.R.2
  • 8
    • 33748863131 scopus 로고    scopus 로고
    • Bacterial RNase P: A new view of an ancient enzyme
    • Kazantsev, A. V., and, Pace, N. R., (2006) Bacterial RNase P: a new view of an ancient enzyme. Nat. Rev. Microbiol. 4, 729-740.
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 729-740
    • Kazantsev, A.V.1    Pace, N.R.2
  • 9
    • 34848863932 scopus 로고    scopus 로고
    • RNase P RNA mediated cleavage: Substrate recognition and catalysis
    • Kirsebom, L. A., (2007) RNase P RNA mediated cleavage: substrate recognition and catalysis. Biochimie 89, 1183-1194.
    • (2007) Biochimie , vol.89 , pp. 1183-1194
    • Kirsebom, L.A.1
  • 11
    • 77649336326 scopus 로고    scopus 로고
    • Trials, travails and triumphs: An account of RNA catalysis in RNase P
    • McClain, W. H., Lai, L. B., and, Gopalan, V., (2010) Trials, travails and triumphs: an account of RNA catalysis in RNase P. J. Mol. Biol. 397, 627-646.
    • (2010) J. Mol. Biol. , vol.397 , pp. 627-646
    • McClain, W.H.1    Lai, L.B.2    Gopalan, V.3
  • 12
    • 78650444089 scopus 로고    scopus 로고
    • Archaeal/eukaryal RNase P: Subunits, functions and RNA diversification
    • Jarrous, N., and, Gopalan, V., (2010) Archaeal/eukaryal RNase P: subunits, functions and RNA diversification. Nucleic Acids Res. 38, 7885-7894.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 7885-7894
    • Jarrous, N.1    Gopalan, V.2
  • 13
    • 77956049347 scopus 로고    scopus 로고
    • Of proteins and RNA: The RNase P/MRP family
    • Esakova, O., and, Krasilnikov, A. S., (2010) Of proteins and RNA: the RNase P/MRP family. RNA 16, 1725-1747.
    • (2010) RNA , vol.16 , pp. 1725-1747
    • Esakova, O.1    Krasilnikov, A.S.2
  • 14
    • 60149101421 scopus 로고    scopus 로고
    • Crawling out of the RNA world
    • Cech, T. R., (2009) Crawling out of the RNA world. Cell 136, 599-602.
    • (2009) Cell , vol.136 , pp. 599-602
    • Cech, T.R.1
  • 15
    • 60349104299 scopus 로고    scopus 로고
    • The spliceosome: Design principles of a dynamic RNP machine
    • Wahl, M. C., Will, C. L., and, Luhrmann, R., (2009) The spliceosome: design principles of a dynamic RNP machine. Cell 136, 701-718.
    • (2009) Cell , vol.136 , pp. 701-718
    • Wahl, M.C.1    Will, C.L.2    Luhrmann, R.3
  • 16
    • 79952003781 scopus 로고    scopus 로고
    • The RNP bridge between two worlds
    • Schimmel P., (2011) The RNP bridge between two worlds. Nat. Rev. Mol. Cell Biol. 12, 135.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 135
    • Schimmel, P.1
  • 17
    • 0018890919 scopus 로고
    • E. coli RNAase P has a required RNA component
    • Kole, R., Baer, M. F., Stark, B. C., and, Altman, S., (1980) E. coli RNAase P has a required RNA component. Cell 19, 881-887.
    • (1980) Cell , vol.19 , pp. 881-887
    • Kole, R.1    Baer, M.F.2    Stark, B.C.3    Altman, S.4
  • 18
    • 0023550946 scopus 로고
    • The RNA components of Schizosaccharomyces pombe RNase P are essential for cell viability
    • Cherayil, B., Krupp, G., Schuchert, P., Char, S., and, Soll, D., (1987) The RNA components of Schizosaccharomyces pombe RNase P are essential for cell viability. Gene 60, 157-161.
    • (1987) Gene , vol.60 , pp. 157-161
    • Cherayil, B.1    Krupp, G.2    Schuchert, P.3    Char, S.4    Soll, D.5
  • 19
    • 33749334411 scopus 로고    scopus 로고
    • Analysis of RNase P protein (rnpA) expression in Bacillus subtilis utilizing strains with suppressible rnpA expression
    • Gossringer, M., Kretschmer-Kazemi Far, R., and, Hartmann, R. K., (2006) Analysis of RNase P protein (rnpA) expression in Bacillus subtilis utilizing strains with suppressible rnpA expression. J. Bacteriol. 188, 6816-6823.
    • (2006) J. Bacteriol. , vol.188 , pp. 6816-6823
    • Gossringer, M.1    Kretschmer-Kazemi Far, R.2    Hartmann, R.K.3
  • 20
    • 0015523504 scopus 로고
    • Purification and properties of a specific Escherichia coli ribonuclease which cleaves a tyrosine transfer ribonucleic acid presursor
    • Robertson, H. D., Altman, S., and, Smith, J. D., (1972) Purification and properties of a specific Escherichia coli ribonuclease which cleaves a tyrosine transfer ribonucleic acid presursor. J. Biol. Chem. 247, 5243-5251.
    • (1972) J. Biol. Chem. , vol.247 , pp. 5243-5251
    • Robertson, H.D.1    Altman, S.2    Smith, J.D.3
  • 21
    • 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, K. A., and, 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
  • 22
    • 1842389177 scopus 로고
    • Ribonuclease P substrate specificity: Cleavage of a bacteriophage phi80-induced RNA
    • Bothwell, A. L., Stark, B. C., and, Altman, S., (1976) Ribonuclease P substrate specificity: cleavage of a bacteriophage phi80-induced RNA. Proc. Natl Acad. Sci. USA 73, 1912-1916.
    • (1976) Proc. Natl Acad. Sci. USA , vol.73 , pp. 1912-1916
    • Bothwell, A.L.1    Stark, B.C.2    Altman, S.3
  • 23
    • 0029074106 scopus 로고
    • Precursor of C4 antisense RNA of bacteriophages P1 and P7 is a substrate for RNase P of Escherichia coli
    • Hartmann, R. K., Heinrich, J., Schlegl, J., and, Schuster, H., (1995) Precursor of C4 antisense RNA of bacteriophages P1 and P7 is a substrate for RNase P of Escherichia coli. Proc. Natl Acad. Sci. USA 92, 5822-5826.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 5822-5826
    • Hartmann, R.K.1    Heinrich, J.2    Schlegl, J.3    Schuster, H.4
  • 24
    • 0028978046 scopus 로고
    • Immunity determinant of phage-plasmid P4 is a short processed RNA
    • Forti, F., Sabbattini, P., Sironi, G., Zangrossi, S., Deho, G., et al. (1995) Immunity determinant of phage-plasmid P4 is a short processed RNA. J. Mol. Biol. 249, 869-878.
    • (1995) J. Mol. Biol. , vol.249 , pp. 869-878
    • Forti, F.1    Sabbattini, P.2    Sironi, G.3    Zangrossi, S.4    Deho, G.5
  • 25
    • 0028568179 scopus 로고
    • Ribonuclease e provides substrates for ribonuclease P-dependent processing of a polycistronic mRNA
    • Alifano, P., Rivellini, F., Piscitelli, C., Arraiano, C. M., Bruni, C. B., et al. (1994) Ribonuclease E provides substrates for ribonuclease P-dependent processing of a polycistronic mRNA. Genes Dev. 8, 3021-3031.
    • (1994) Genes Dev. , vol.8 , pp. 3021-3031
    • Alifano, P.1    Rivellini, F.2    Piscitelli, C.3    Arraiano, C.M.4    Bruni, C.B.5
  • 26
    • 0345255620 scopus 로고    scopus 로고
    • A specific endoribonuclease, RNase P, affects gene expression of polycistronic operon mRNAs
    • Li, Y., and, Altman, S., (2003) A specific endoribonuclease, RNase P, affects gene expression of polycistronic operon mRNAs. Proc. Natl Acad. Sci. USA 100, 13213-13218.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 13213-13218
    • Li, Y.1    Altman, S.2
  • 27
    • 2342513377 scopus 로고    scopus 로고
    • Polarity effects in the lactose operon of Escherichia coli
    • Li, Y., and, Altman, S., (2004) Polarity effects in the lactose operon of Escherichia coli. J. Mol. Biol. 339, 31-39.
    • (2004) J. Mol. Biol. , vol.339 , pp. 31-39
    • Li, Y.1    Altman, S.2
  • 29
    • 44149107344 scopus 로고    scopus 로고
    • RNase P cleaves the adenine riboswitch and stabilizes pbuE mRNA in Bacillus subtilis
    • Seif, E., and, 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
  • 30
    • 0024294369 scopus 로고
    • Novel reactions of RNAase P with a tRNA-like structure in turnip yellow mosaic virus RNA
    • Guerrier-Takada, C., van Belkum, A., Pleij, C. W., and, Altman, S., (1988) Novel reactions of RNAase P with a tRNA-like structure in turnip yellow mosaic virus RNA. Cell 53, 267-272.
    • (1988) Cell , vol.53 , pp. 267-272
    • Guerrier-Takada, C.1    Van Belkum, A.2    Pleij, C.W.3    Altman, S.4
  • 31
    • 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., and, Inokuchi, H., (1994) A tRNA-like structure is present in 10Sa RNA, a small stable RNA from Escherichia coli. Proc. Natl Acad. Sci. USA 91, 9223-9227.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 9223-9227
    • Komine, Y.1    Kitabatake, M.2    Yokogawa, T.3    Nishikawa, K.4    Inokuchi, H.5
  • 32
    • 0026970022 scopus 로고
    • Alteration of RNA i metabolism in a temperature-sensitive Escherichia coli rnpA mutant strain
    • Jung, Y. H., Park, I., and, Lee, Y., (1992) Alteration of RNA I metabolism in a temperature-sensitive Escherichia coli rnpA mutant strain. Biochem. Biophys. Res. Commun. 186, 1463-1470.
    • (1992) Biochem. Biophys. Res. Commun. , vol.186 , pp. 1463-1470
    • Jung, Y.H.1    Park, I.2    Lee, Y.3
  • 33
    • 0242699496 scopus 로고
    • RNases in ColE1 DNA metabolism
    • Jung, Y. H., and, Lee, Y., (1995) RNases in ColE1 DNA metabolism. Mol. Biol. Rep. 22, 195-200.
    • (1995) Mol. Biol. Rep. , vol.22 , pp. 195-200
    • Jung, Y.H.1    Lee, Y.2
  • 34
    • 0027172329 scopus 로고
    • RNase MRP and RNase P share a common substrate
    • Potuschak, T., Rossmanith, W., and, Karwan, R., (1993) RNase MRP and RNase P share a common substrate. Nucleic Acids Res. 21, 3239-3243.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 3239-3243
    • Potuschak, T.1    Rossmanith, W.2    Karwan, R.3
  • 35
    • 34249931851 scopus 로고    scopus 로고
    • OLE RNA, an RNA motif that is highly conserved in several extremophilic bacteria, is a substrate for and can be regulated by RNase P RNA
    • Ko, J.-H., and, Altman, S., (2007) OLE RNA, an RNA motif that is highly conserved in several extremophilic bacteria, is a substrate for and can be regulated by RNase P RNA. Proc. Natl Acad. Sci. USA 104, 7815-7820.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 7815-7820
    • Ko, J.-H.1    Altman, S.2
  • 37
    • 0025357508 scopus 로고
    • Characterization of ribonuclease P from the archaebacterium Sulfolobus solfataricus
    • Darr, S. C., Pace, B., and, Pace, N. R., (1990) Characterization of ribonuclease P from the archaebacterium Sulfolobus solfataricus. J. Biol. Chem. 265, 12927-12932.
    • (1990) J. Biol. Chem. , vol.265 , pp. 12927-12932
    • Darr, S.C.1    Pace, B.2    Pace, N.R.3
  • 38
    • 0034826649 scopus 로고    scopus 로고
    • Characterization of RNase P holoenzymes from Methanococcus jannaschii and Methanothermobacter thermoautotrophicus
    • Andrews, A. J., Hall, T. A., and, Brown, J. W., (2001) Characterization of RNase P holoenzymes from Methanococcus jannaschii and Methanothermobacter thermoautotrophicus. Biol. Chem. 382, 1171-1177.
    • (2001) Biol. Chem. , vol.382 , pp. 1171-1177
    • Andrews, A.J.1    Hall, T.A.2    Brown, J.W.3
  • 39
    • 0021894203 scopus 로고
    • Nucleolytic processing of a tRNAArg-tRNAAsp dimeric precursor by a homologous component from Saccharomyces cerevisiae
    • Engelke, D. R., Gegenheimer, P., and, Abelson, J., (1985) Nucleolytic processing of a tRNAArg-tRNAAsp dimeric precursor by a homologous component from Saccharomyces cerevisiae. J. Biol. Chem. 260, 1271-1279.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1271-1279
    • Engelke, D.R.1    Gegenheimer, P.2    Abelson, J.3
  • 40
    • 0022743903 scopus 로고
    • Two RNA species co-purify with RNase P from the fission yeast Schizosaccharomyces pombe
    • Krupp, G., Cherayil, B., Frendewey, D., Nishikawa, S., and, Soll, D., (1986) Two RNA species co-purify with RNase P from the fission yeast Schizosaccharomyces pombe. EMBO J. 5, 1697-1703.
    • (1986) EMBO J. , vol.5 , pp. 1697-1703
    • Krupp, G.1    Cherayil, B.2    Frendewey, D.3    Nishikawa, S.4    Soll, D.5
  • 41
    • 56349113455 scopus 로고    scopus 로고
    • 3' end processing of a long nuclear-retained noncoding RNA yields a tRNA-like cytoplasmic RNA
    • Wilusz, J. E., Freier, S. M., and, Spector, D.L., (2008) 3' end processing of a long nuclear-retained noncoding RNA yields a tRNA-like cytoplasmic RNA. Cell 135, 919-932.
    • (2008) Cell , vol.135 , pp. 919-932
    • Wilusz, J.E.1    Freier, S.M.2    Spector, D.L.3
  • 42
    • 61849113891 scopus 로고    scopus 로고
    • MEN epsilon/beta nuclear-retained non-coding RNAs are up-regulated upon muscle differentiation and are essential components of paraspeckles
    • Sunwoo, H., Dinger, M. E., Wilusz, J. E., Amaral, P. P., Mattick, J. S., et al. (2009) MEN epsilon/beta nuclear-retained non-coding RNAs are up-regulated upon muscle differentiation and are essential components of paraspeckles. Genome Res. 19, 347-359.
    • (2009) Genome Res. , vol.19 , pp. 347-359
    • Sunwoo, H.1    Dinger, M.E.2    Wilusz, J.E.3    Amaral, P.P.4    Mattick, J.S.5
  • 43
    • 34247350827 scopus 로고    scopus 로고
    • A noncoding RNA in Saccharomyces cerevisiae is an RNase P substrate
    • Yang, L., and, Altman, S., (2007) A noncoding RNA in Saccharomyces cerevisiae is an RNase P substrate. RNA 13, 682-690.
    • (2007) RNA , vol.13 , pp. 682-690
    • Yang, L.1    Altman, S.2
  • 44
    • 0035172605 scopus 로고    scopus 로고
    • In vitro and in vivo processing of cyanelle tmRNA by RNase P
    • Gimple, O., and, Schön, A., (2001) In vitro and in vivo processing of cyanelle tmRNA by RNase P. Biol. Chem. 382, 1421-1429.
    • (2001) Biol. Chem. , vol.382 , pp. 1421-1429
    • Gimple, O.1    Schön, A.2
  • 45
    • 79960935970 scopus 로고    scopus 로고
    • Viperin mRNA is a novel target for the human RNase MRP/RNase P endoribonuclease
    • Mattijssen, S., Hinson, E. R., Onnekink, C., Hermanns, P., Zabel, B., et al. (2011) Viperin mRNA is a novel target for the human RNase MRP/RNase P endoribonuclease. Cell Mol. Life Sci. 68, 2469-2480.
    • (2011) Cell Mol. Life Sci. , vol.68 , pp. 2469-2480
    • Mattijssen, S.1    Hinson, E.R.2    Onnekink, C.3    Hermanns, P.4    Zabel, B.5
  • 47
    • 50449087360 scopus 로고    scopus 로고
    • Genome-wide search for yeast RNase P substrates reveals role in maturation of intron-encoded box C/D small nucleolar RNAs
    • Coughlin, D. J., Pleiss, J. A., Walker, S. C., Whitworth, G. B., and, Engelke, D. R., (2008) Genome-wide search for yeast RNase P substrates reveals role in maturation of intron-encoded box C/D small nucleolar RNAs. Proc. Natl Acad. Sci. USA 105, 12218-12223.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 12218-12223
    • Coughlin, D.J.1    Pleiss, J.A.2    Walker, S.C.3    Whitworth, G.B.4    Engelke, D.R.5
  • 48
    • 79960472362 scopus 로고    scopus 로고
    • Accumulation of noncoding RNA due to an RNase P defect in Saccharomyces cerevisiae
    • Marvin, M. C., Clauder-Munster, S., Walker, S. C., Sarkeshik, A., Yates, J. R., 3rd, et al. (2011) Accumulation of noncoding RNA due to an RNase P defect in Saccharomyces cerevisiae. RNA 17, 1441-1450.
    • (2011) RNA , vol.17 , pp. 1441-1450
    • Marvin, M.C.1    Clauder-Munster, S.2    Walker, S.C.3    Sarkeshik, A.4    Yates III, J.R.5
  • 49
    • 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
  • 51
    • 33847784925 scopus 로고    scopus 로고
    • Eukaryotic RNase P RNA mediates cleavage in the absence of protein
    • Kikovska, E., Svard, S. G., and, Kirsebom, L. A., (2007) Eukaryotic RNase P RNA mediates cleavage in the absence of protein. Proc. Natl. Acad. Sci. USA 104, 2062-2067.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2062-2067
    • Kikovska, E.1    Svard, S.G.2    Kirsebom, L.A.3
  • 52
    • 17744393618 scopus 로고    scopus 로고
    • Mutations in the RNA component of RNase MRP cause a pleiotropic human disease, cartilage-hair hypoplasia
    • Ridanpaa, M., van Eenennaam, H., Pelin, K., Chadwick, R., Johnson, C., et al. (2001) Mutations in the RNA component of RNase MRP cause a pleiotropic human disease, cartilage-hair hypoplasia. Cell 104, 195-203.
    • (2001) Cell , vol.104 , pp. 195-203
    • Ridanpaa, M.1    Van Eenennaam, H.2    Pelin, K.3    Chadwick, R.4    Johnson, C.5
  • 53
    • 80054781000 scopus 로고    scopus 로고
    • RMRP is a non-coding RNA essential for early murine development
    • Rosenbluh, J., Nijhawan, D., Chen, Z., Wong, K. K., Masutomi, K., et al. (2011) RMRP is a non-coding RNA essential for early murine development. PLoS One 6, e26270.
    • (2011) PLoS One , vol.6
    • Rosenbluh, J.1    Nijhawan, D.2    Chen, Z.3    Wong, K.K.4    Masutomi, K.5
  • 54
    • 0027367147 scopus 로고
    • Nuclear RNase MRP is required for correct processing of pre-5.8S rRNA in Saccharomyces cerevisiae
    • Schmitt, M. E., and, Clayton, D. A., (1993) Nuclear RNase MRP is required for correct processing of pre-5.8S rRNA in Saccharomyces cerevisiae. Mol. Cell. Biol. 13, 7935-7941.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7935-7941
    • Schmitt, M.E.1    Clayton, D.A.2
  • 55
    • 0029981894 scopus 로고    scopus 로고
    • Accurate processing of a eukaryotic precursor ribosomal RNA by ribonuclease MRP in vitro
    • Lygerou, Z., Allmang, C., Tollervey, D., and, Séraphin, B., (1996) Accurate processing of a eukaryotic precursor ribosomal RNA by ribonuclease MRP in vitro. Science 272, 268-270.
    • (1996) Science , vol.272 , pp. 268-270
    • Lygerou, Z.1    Allmang, C.2    Tollervey, D.3    Séraphin, B.4
  • 56
    • 1642430571 scopus 로고    scopus 로고
    • RNase MRP cleaves the CLB2 mRNA to promote cell cycle progression: Novel method of mRNA degradation
    • Gill, T., Cai, T., Aulds, J., Wierzbicki, S., and, Schmitt, M. E., (2004) RNase MRP cleaves the CLB2 mRNA to promote cell cycle progression: novel method of mRNA degradation. Mol. Cell. Biol. 24, 945-953.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 945-953
    • Gill, T.1    Cai, T.2    Aulds, J.3    Wierzbicki, S.4    Schmitt, M.E.5
  • 57
    • 0026651858 scopus 로고
    • Saccharomyces cerevisiae contains an RNase MRP that cleaves at a conserved mitochondrial RNA sequence implicated in replication priming
    • Stohl, L. L., and, Clayton, D. A., (1992) Saccharomyces cerevisiae contains an RNase MRP that cleaves at a conserved mitochondrial RNA sequence implicated in replication priming. Mol. Cell. Biol. 12, 2561-2569.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2561-2569
    • Stohl, L.L.1    Clayton, D.A.2
  • 58
    • 70249114371 scopus 로고    scopus 로고
    • An RNA-dependent RNA polymerase formed by TERT and the RMRP RNA
    • Maida, Y., Yasukawa, M., Furuuchi, M., Lassmann, T., Possemato, R., et al. (2009) An RNA-dependent RNA polymerase formed by TERT and the RMRP RNA. Nature 461, 230-235.
    • (2009) Nature , vol.461 , pp. 230-235
    • Maida, Y.1    Yasukawa, M.2    Furuuchi, M.3    Lassmann, T.4    Possemato, R.5
  • 59
    • 0023152084 scopus 로고
    • A mammalian mitochondrial RNA processing activity contains nucleus-encoded RNA
    • Chang, D. D., and, Clayton, D. A., (1987) A mammalian mitochondrial RNA processing activity contains nucleus-encoded RNA. Science 235, 1178-1184.
    • (1987) Science , vol.235 , pp. 1178-1184
    • Chang, D.D.1    Clayton, D.A.2
  • 60
    • 0025308501 scopus 로고
    • Secondary structure of the RNA component of a nuclear/mitochondrial ribonucleoprotein
    • Topper, J. N., and, Clayton, D. A., (1990) Secondary structure of the RNA component of a nuclear/mitochondrial ribonucleoprotein. J. Biol. Chem. 265, 13254-13262.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13254-13262
    • Topper, J.N.1    Clayton, D.A.2
  • 61
    • 0026670514 scopus 로고
    • 7-2/MRP RNAs in plant and mammalian cells: Association with higher order structures in the nucleolus
    • Kiss, T., Marshallsay, C., and, Filipowicz, W., (1992) 7-2/MRP RNAs in plant and mammalian cells: association with higher order structures in the nucleolus. EMBO J. 11, 3737-3746.
    • (1992) EMBO J. , vol.11 , pp. 3737-3746
    • Kiss, T.1    Marshallsay, C.2    Filipowicz, W.3
  • 62
    • 78650071286 scopus 로고    scopus 로고
    • Role of RNase MRP in viral RNA degradation and RNA recombination
    • Jaag, H. M., Lu, Q., Schmitt, M. E., and, Nagy, P. D., (2011) Role of RNase MRP in viral RNA degradation and RNA recombination. J. Virol. 85, 243-253.
    • (2011) J. Virol. , vol.85 , pp. 243-253
    • Jaag, H.M.1    Lu, Q.2    Schmitt, M.E.3    Nagy, P.D.4
  • 63
    • 80355131527 scopus 로고    scopus 로고
    • Characterization of RNase MRP RNA and novel snoRNAs from Giardia intestinalis and Trichomonas vaginalis
    • Chen, X. S., Penny, D., and, Collins, L. J., (2011) Characterization of RNase MRP RNA and novel snoRNAs from Giardia intestinalis and Trichomonas vaginalis. BMC Genomics 12, 550.
    • (2011) BMC Genomics , vol.12 , pp. 550
    • Chen, X.S.1    Penny, D.2    Collins, L.J.3
  • 65
    • 84860198151 scopus 로고    scopus 로고
    • Modular architecture of eukaryotic RNase P and RNase MRP revealed by electron microscopy
    • Hipp, K., Galani, K., Batisse, C., Prinz, S., and, Bottcher, B., (2012) Modular architecture of eukaryotic RNase P and RNase MRP revealed by electron microscopy. Nucleic Acids Res 40, 3275-3288.
    • (2012) Nucleic Acids Res , vol.40 , pp. 3275-3288
    • Hipp, K.1    Galani, K.2    Batisse, C.3    Prinz, S.4    Bottcher, B.5
  • 67
    • 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
  • 68
    • 0026639881 scopus 로고
    • Unusual resistance of peptidyl transferase to protein extraction procedures
    • Noller, H. F., Hoffarth, V., and, Zimniak, L., (1992) Unusual resistance of peptidyl transferase to protein extraction procedures. Science 256, 1416-1419.
    • (1992) Science , vol.256 , pp. 1416-1419
    • Noller, H.F.1    Hoffarth, V.2    Zimniak, L.3
  • 69
    • 33646200077 scopus 로고    scopus 로고
    • Sequence analysis of RNase MRP RNA reveals its origination from eukaryotic RNase P RNA
    • Zhu, Y., Stribinskis, V., Ramos, K. S., and, Li, Y., (2006) Sequence analysis of RNase MRP RNA reveals its origination from eukaryotic RNase P RNA. RNA 12, 699-706.
    • (2006) RNA , vol.12 , pp. 699-706
    • Zhu, Y.1    Stribinskis, V.2    Ramos, K.S.3    Li, Y.4
  • 70
    • 0028945859 scopus 로고
    • Higher order folding and domain analysis of the ribozyme from Bacillus subtilis ribonuclease P
    • Pan, T., (1995) Higher order folding and domain analysis of the ribozyme from Bacillus subtilis ribonuclease P. Biochemistry 34, 902-909.
    • (1995) Biochemistry , vol.34 , pp. 902-909
    • Pan, T.1
  • 71
    • 0037115872 scopus 로고    scopus 로고
    • Comparative analysis of ribosomal proteins in complete genomes: An example of reductive evolution at the domain scale
    • Lecompte, O., Ripp, R., Thierry, J. C., Moras, D., and, Poch, O., (2002) Comparative analysis of ribosomal proteins in complete genomes: an example of reductive evolution at the domain scale. Nucleic Acids Res. 30, 5382-5390.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 5382-5390
    • Lecompte, O.1    Ripp, R.2    Thierry, J.C.3    Moras, D.4    Poch, O.5
  • 73
    • 0014378880 scopus 로고
    • The origin of the genetic code
    • Crick, F. H., (1968) The origin of the genetic code. J. Mol. Biol. 38, 367-379.
    • (1968) J. Mol. Biol. , vol.38 , pp. 367-379
    • Crick, F.H.1
  • 74
    • 0014369024 scopus 로고
    • Evolution of the genetic apparatus
    • Orgel, L. E., (1968) Evolution of the genetic apparatus. J. Mol. Biol. 38, 381-393.
    • (1968) J. Mol. Biol. , vol.38 , pp. 381-393
    • Orgel, L.E.1
  • 75
    • 77957743184 scopus 로고    scopus 로고
    • Evolution of biological catalysis: Ribozyme to RNP enzyme
    • Cech, T. R., (2009) Evolution of biological catalysis: ribozyme to RNP enzyme. Cold Spring Harb. Symp. Quant. Biol. 74, 11-16.
    • (2009) Cold Spring Harb. Symp. Quant. Biol. , vol.74 , pp. 11-16
    • Cech, T.R.1
  • 76
    • 34247645736 scopus 로고    scopus 로고
    • RNase MRP and the RNA processing cascade in the eukaryotic ancestor
    • Woodhams, M. D., Stadler, P. F., Penny, D., and, Collins, L. J., (2007) RNase MRP and the RNA processing cascade in the eukaryotic ancestor. BMC Evol. Biol. 7 (Suppl 1), S13.
    • (2007) BMC Evol. Biol. , vol.7 , Issue.SUPPL. 1
    • Woodhams, M.D.1    Stadler, P.F.2    Penny, D.3    Collins, L.J.4
  • 77
    • 0037434709 scopus 로고    scopus 로고
    • Crystal structure of the specificity domain of ribonuclease P
    • Krasilnikov, A. S., Yang, X., Pan, T., and, Mondragon, A., (2003) Crystal structure of the specificity domain of ribonuclease P. Nature 421, 760-764.
    • (2003) Nature , vol.421 , pp. 760-764
    • Krasilnikov, A.S.1    Yang, X.2    Pan, T.3    Mondragon, A.4
  • 78
    • 6044275739 scopus 로고    scopus 로고
    • Basis for structural diversity in homologous RNAs
    • Krasilnikov, A. S., Xiao, Y., Pan, T., and, Mondragon, A., (2004) Basis for structural diversity in homologous RNAs. Science 306, 104-107.
    • (2004) Science , vol.306 , pp. 104-107
    • Krasilnikov, A.S.1    Xiao, Y.2    Pan, T.3    Mondragon, A.4
  • 79
    • 25644433566 scopus 로고    scopus 로고
    • Crystal structure of the RNA component of bacterial ribonuclease P
    • Torres-Larios, A., Swinger, K. K., Krasilnikov, A. S., Pan, T., and, Mondragon, A., (2005) Crystal structure of the RNA component of bacterial ribonuclease P. Nature 437, 584-587.
    • (2005) Nature , vol.437 , pp. 584-587
    • Torres-Larios, A.1    Swinger, K.K.2    Krasilnikov, A.S.3    Pan, T.4    Mondragon, A.5
  • 80
    • 79951826865 scopus 로고    scopus 로고
    • The crystal structure of the signal recognition particle in complex with its receptor
    • Ataide, S. F., Schmitz, N., Shen, K., Ke, A., Shan, S. O., et al. (2011) The crystal structure of the signal recognition particle in complex with its receptor. Science 331, 881-886.
    • (2011) Science , vol.331 , pp. 881-886
    • Ataide, S.F.1    Schmitz, N.2    Shen, K.3    Ke, A.4    Shan, S.O.5
  • 81
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 A resolution
    • Ban, N., Nissen, P., Hansen, J., Moore P. B., and, Steitz, T.A., (2000) The complete atomic structure of the large ribosomal subunit at 2.4 A resolution. Science 289, 905-920.
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 83
    • 63649099704 scopus 로고    scopus 로고
    • Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution
    • Pomeranz Krummel, D. A., Oubridge, C., Leung, A. K., Li, J., and, Nagai, K., (2009) Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution. Nature 458, 475-480.
    • (2009) Nature , vol.458 , pp. 475-480
    • Pomeranz Krummel, D.A.1    Oubridge, C.2    Leung, A.K.3    Li, J.4    Nagai, K.5
  • 84
    • 78650175123 scopus 로고    scopus 로고
    • Structure of a bacterial ribonuclease P holoenzyme in complex with
    • Reiter, N. J., Osterman, A., Torres-Larios, A., Swinger, K. K., Pan, T., et al. (2010) Structure of a bacterial ribonuclease P holoenzyme in complex with. Nature 2010 468 784-789.
    • (2010) Nature , vol.468 , pp. 784-789
    • Reiter, N.J.1    Osterman, A.2    Torres-Larios, A.3    Swinger, K.K.4    Pan, T.5
  • 86
    • 43049088477 scopus 로고    scopus 로고
    • Life without RNase P
    • Randau, L., Schroder, I., and, Soll, D., (2008) Life without RNase P.
    • (2008) Nature , vol.453 , pp. 120-123
  • 88
    • 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
    • (1996) RNA , vol.2 , pp. 452-462
  • 90
    • 54549088876 scopus 로고    scopus 로고
    • RNase P without RNA: Identification and functional reconstitution of the human mitochondrial tRNA processing enzyme
    • Holzmann, J., Frank, P., Loffler, E., Bennett, K. L., Gerner, C., et al. (2008) RNase P without RNA: identification and functional reconstitution of the
    • (2008) Cell , vol.135 , pp. 462-474
  • 91
    • 78449299224 scopus 로고    scopus 로고
    • Mosaic origin of the mitochondrial proteome
    • Szklarczyk, R., and, Huynen, M. A., (2010) Mosaic origin of the
    • (2010) Proteomics , vol.10 , pp. 4012-4024
  • 92
    • 85177000672 scopus 로고
    • Rossmanith, W., Tullo, A., Potuschak, T., Karwan, R., and, Sbisa, E., (1995) Human mitochondrial tRNA processing. J. Biol. Chem. 270, 12885-12891.
    • (1995) Human mitochondrial tRNA processing , vol.270 , pp. 12885-12891
  • 95
    • 84855678085 scopus 로고    scopus 로고
    • A functional RNase P protein subunit of bacterial origin in some eukaryotes
    • Lai, L. B., Bernal-Bayard, P., Mohannath, G., Lai, S. M., Gopalan, V., et al. (2011) A functional RNase P protein subunit of bacterial origin in some
    • (2011) Mol. Genet. Genomics , vol.286 , pp. 359-369
  • 97
    • 77955320529 scopus 로고    scopus 로고
    • PNPASE regulates RNA import into mitochondria
    • Wang, G., Chen, H. W., Oktay, Y., Zhang, J., Allen, E. L., et al. (2010)
    • (2010) Cell , vol.142 , pp. 456-467
  • 98
    • 47249160767 scopus 로고    scopus 로고
    • Structural basis for specific substrate recognition by the chloroplast signal recognition particle protein cpSRP43
    • Stengel, K. F., Holdermann, I., Cain, P., Robinson, C., Wild, K., et al. (2008) Structural basis for specific substrate recognition by the chloroplast
    • (2008) Science , vol.321 , pp. 253-256
  • 99
    • 80052007901 scopus 로고    scopus 로고
    • The human mitochondrial transcriptome
    • Mercer, T. R., Neph, S., Dinger, M. E., Crawford, J., Smith, M. A., et
    • (2011) Cell , vol.146 , pp. 645-658
  • 101
    • 48249128388 scopus 로고    scopus 로고
    • Mammalian mitochondria have the innate ability to import tRNAs by a mechanism distinct from protein import
    • Rubio, M. A., Rinehart, J. J., Krett, B., Duvezin-Caubet, S., Reichert, A. S., et al. (2008) Mammalian mitochondria have the innate ability to import tRNAs by a mechanism distinct from protein import. Proc. Natl Acad. Sci. USA
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 9186-9191
    • Rubio, M.A.1    Rinehart, J.J.2    Krett, B.3    Duvezin-Caubet, S.4    Reichert, A.S.5
  • 105
    • 77149176920 scopus 로고    scopus 로고
    • Comparison of mitochondrial and nucleolar RNase MRP reveals identical RNA components with distinct enzymatic activities and protein components
    • Lu, Q., Wierzbicki, S., Krasilnikov, A. S., and, Schmitt, M. E., (2010) Comparison of mitochondrial and nucleolar RNase MRP reveals identical RNA components with distinct enzymatic activities and protein components. RNA 16, 529-537.
    • (2010) RNA , vol.16 , pp. 529-537
    • Lu, Q.1    Wierzbicki, S.2    Krasilnikov, A.S.3    Schmitt, M.E.4


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