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Volumn 17, Issue 10, 2011, Pages 1922-1931

Interactions of a Pop5/Rpp1 heterodimer with the catalytic domain of RNase MRP

Author keywords

Pop5; Ribonuclease MRP; Ribonuclease P; RNA protein interactions; Rpp1; Saccharomyces cerevisiae

Indexed keywords

BACTERIAL RNA; MEMBRANE PROTEIN; POP5 PROTEIN; RIBONUCLEASE; RIBONUCLEASE MRP; RPP1 PROTEIN; UNCLASSIFIED DRUG;

EID: 80053218807     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.2855511     Document Type: Article
Times cited : (8)

References (67)
  • 1
    • 77953426040 scopus 로고    scopus 로고
    • History of RNase P and overview of its catalytic activity
    • ed. F. Liu and and S. Altman, Springer, New York
    • Altman S. 2010. History of RNase P and overview of its catalytic activity. In Ribonuclease P, protein reviews 10 (ed. F. Liu and and S. Altman), pp. 1-15. Springer, New York.
    • (2010) Ribonuclease P, Protein Reviews 10 , pp. 1-15
    • Altman, S.1
  • 3
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: A useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • DOI 10.1002/(SICI)1097-0061(19980130)14:2<115::AID-YEA204>3.0.CO;2- 2
    • Brachmann CB, Davis A, Cost GJ, Caputo E, Li J, Hieter P, Boeke JD. 1998. Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR mediated gene disruption and other applications. Yeast 14: 115-132. (Pubitemid 28062863)
    • (1998) Yeast , vol.14 , Issue.2 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5    Hieter, P.6    Boeke, J.D.7
  • 4
    • 0344298926 scopus 로고    scopus 로고
    • The ribonuclease P database
    • Brown JW. 1999. The ribonuclease P database. Nucleic Acids Res 27: 314-314.
    • (1999) Nucleic Acids Res , vol.27 , pp. 314-314
    • Brown, J.W.1
  • 5
    • 0032696246 scopus 로고    scopus 로고
    • Mutagenesis of SNM1, which encodes a protein component of the yeast RNase MRP, reveals a role for this ribonucleoprotein endoribonuclease in plasmid segregation
    • Cai T, Reilly TR, Cerio M, Schmitt ME. 1999. Mutagenesis of SNM1, which encodes a protein component of the yeast RNase MRP, reveals a role for this ribonucleoprotein endoribonuclease in plasmid segregation. Mol Cell Biol 19: 7857-7869. (Pubitemid 29493449)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.11 , pp. 7857-7869
    • Cai, T.1    Reilly, T.R.2    Cerio, M.3    Schmitt, M.E.4
  • 6
    • 0036021365 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae RNase mitochondrial RNA processing is critical for cell cycle progression at the end of mitosis
    • Cai T, Aulds J, Gill T, Cerio M, Schmitt ME. 2002. The Saccharomyces cerevisiae RNase Mitochondrial RNA Processing is critical for cell cycle progression at the end of mitosis. Genetics 161: 1029-1042. (Pubitemid 34831429)
    • (2002) Genetics , vol.161 , Issue.3 , pp. 1029-1042
    • Cai, T.1    Aulds, J.2    Gill, T.3    Cerio, M.4    Schmitt, M.E.5
  • 7
    • 2642635832 scopus 로고    scopus 로고
    • Purification and characterization of the nuclear RNase P holoenzyme complex reveals extensive subunit overlap with RNase MRP
    • Chamberlain JR, Lee Y, Lane WS, Engelke DR. 1998. Purification and characterization of the nuclear RNase P holoenzyme complex reveals extensive subunit overlap with RNase MRP. Genes Dev 12: 1678-1690. (Pubitemid 28299518)
    • (1998) Genes and Development , vol.12 , Issue.11 , pp. 1678-1690
    • Chamberlain, J.R.1    Lee, Y.2    Lane, W.S.3    Engelke, D.R.4
  • 8
    • 0023283102 scopus 로고
    • A novel endoribonuclease cleaves at a priming site of mouse mitochondrial DNA replication
    • Chang DD, Clayton DA. 1987a. A novel endoribonuclease cleaves at a priming site of mouse mitochondrial DNA replication. EMBO J 6: 409-417.
    • (1987) EMBO J , vol.6 , pp. 409-417
    • Chang, D.D.1    Clayton, D.A.2
  • 9
    • 0023152084 scopus 로고
    • A mammalian mitochondrial RNA processing activity contains nucleus-encoded RNA
    • Chang DD, Clayton DA. 1987b. A mammalian mitochondrial RNA processing activity contains nucleus-encoded RNA. Science 235: 1178-1184. (Pubitemid 17034003)
    • (1987) Science , vol.235 , Issue.4793 , pp. 1178-1184
    • Chang, D.D.1    Clayton, D.A.2
  • 10
    • 0031156668 scopus 로고    scopus 로고
    • Identification of the universally conserved core of ribonuclease P RNA
    • Chen J-L, Pace NR. 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
  • 11
    • 77957157307 scopus 로고    scopus 로고
    • Dissecting functional cooperation among protein subunits in archaeal RNase P, a catalytic ribonucleoprotein complex
    • Chen W-Y, Pulukkunat DK, Cho I-M, Tsai H-Y, Gopalan V. 2010. Dissecting functional cooperation among protein subunits in archaeal RNase P, a catalytic ribonucleoprotein complex. Nucleic Acids Res 38: 8316-8327.
    • (2010) Nucleic Acids Res , vol.38 , pp. 8316-8327
    • Chen, W.-Y.1    Pulukkunat, D.K.2    Cho, I.-M.3    Tsai, H.-Y.4    Gopalan, V.5
  • 13
    • 77956049347 scopus 로고    scopus 로고
    • Of proteins and RNA: The RNase P/MRP family
    • Esakova O, Krasilnikov AS. 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
    • 47949097166 scopus 로고    scopus 로고
    • Footprinting analysis demonstrates extensive similarity between eukaryotic RNase P and RNase MRP holoenzymes
    • Esakova O, Perederina A, Quan C, Schmitt ME, Krasilnikov AS. 2008. Footprinting analysis demonstrates extensive similarity between eukaryotic RNase P and RNase MRP holoenzymes. RNA 14: 1558-1567.
    • (2008) RNA , vol.14 , pp. 1558-1567
    • Esakova, O.1    Perederina, A.2    Quan, C.3    Schmitt, M.E.4    Krasilnikov, A.S.5
  • 16
    • 33645745497 scopus 로고    scopus 로고
    • A specialized processing body that is temporally and asymmetrically regulated during the cell cycle in Saccharomyces cerevisiae
    • Gill T, Aulds J, Schmitt ME. 2006. A specialized processing body that is temporally and asymmetrically regulated during the cell cycle in Saccharomyces cerevisiae. J Cell Biol 173: 35-45.
    • (2006) J Cell Biol , vol.173 , pp. 35-45
    • Gill, T.1    Aulds, J.2    Schmitt, M.E.3
  • 17
    • 79953760198 scopus 로고    scopus 로고
    • Whole-exome re-sequencing in a family quartet identifies POP1 mutations as the cause of a novel skeletal dysplasia
    • doi: 10.1371/journal. pgen.1002027
    • Glazov EA, Zankl A, Donskoi M, Kenna TJ, Thomas GP, Clark GR, Duncan EL, Brown MA. 2011. Whole-exome re-sequencing in a family quartet identifies POP1 mutations as the cause of a novel skeletal dysplasia. PLoS Genet 7: e1002027. doi: 10.1371/journal. pgen.1002027.
    • (2011) PLoS Genet , vol.7
    • Glazov, E.A.1    Zankl, A.2    Donskoi, M.3    Kenna, T.J.4    Thomas, G.P.5    Clark, G.R.6    Duncan, E.L.7    Brown, M.A.8
  • 18
    • 77249144829 scopus 로고    scopus 로고
    • Archaeal homologs of human RNase P protein pairs Pop5 with Rpp30 and Rpp21 with Rpp29 work on distinct functional domains of the RNA subunit
    • Honda T, Hara T, Nan J, Zhang X, Kimura M. 2010. Archaeal homologs of human RNase P protein pairs Pop5 with Rpp30 and Rpp21 with Rpp29 work on distinct functional domains of the RNA subunit. Biosci Biotechnol Biochem 74: 266-273.
    • (2010) Biosci Biotechnol Biochem , vol.74 , pp. 266-273
    • Honda, T.1    Hara, T.2    Nan, J.3    Zhang, X.4    Kimura, M.5
  • 20
    • 78650444089 scopus 로고    scopus 로고
    • Archaeal/eukaryal RNase P: Subunits, functions and RNA diversification
    • Jarrous N, 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
  • 22
    • 0034960193 scopus 로고    scopus 로고
    • Protein-RNA interactions in the subunits of human nuclear RNase P
    • DOI 10.1017/S1355838201010299
    • Jiang T, Guerrier-Takada C, Altman S. 2001. Protein-RNA interactions in the subunits of human nuclear RNase P. RNA 7: 937-941. (Pubitemid 32612471)
    • (2001) RNA , vol.7 , Issue.7 , pp. 937-941
    • Jiang, T.1    Guerrier-Takada, C.2    Altman, S.3
  • 23
    • 0025733594 scopus 로고
    • Nuclear RNase MRP processes RNA at multiple discrete sites: Interaction with an upstream G box is required for subsequent downstream cleavages
    • Karwan R, Bennett JL, Clayton DA. 1991. Nuclear RNase MRP processes RNA at multiple discrete sites: Interaction with an upstream G box is required for subsequent downstream cleavages. Genes Dev 5: 1264-1276. (Pubitemid 21906036)
    • (1991) Genes and Development , vol.5 , Issue.7 , pp. 1264-1276
    • Karwan, R.1    Bennett, J.L.2    Clayton, D.A.3
  • 24
    • 33344479270 scopus 로고    scopus 로고
    • Crystal structure of protein Ph1481p in complex with protein Ph1877p of archaeal RNase P from Pyrococcus horikoshii OT3: Implication of dimer formation of the holoenzyme
    • DOI 10.1016/j.jmb.2005.12.086, PII S0022283605016761
    • Kawano S, Nakashima T, Kakuta Y, Tanaka I, Kimura M. 2006. Crystal structure of protein Ph1481p in complex with protein Ph1877p of archaeal RNase P from Pyrococcus horikoshii OT3: Implication of dimer formation of the holoenzyme. J Mol Biol 357: 583-591. (Pubitemid 43290757)
    • (2006) Journal of Molecular Biology , vol.357 , Issue.2 , pp. 583-591
    • Kawano, S.1    Nakashima, T.2    Kakuta, Y.3    Tanaka, I.4    Kimura, M.5
  • 28
    • 0037434709 scopus 로고    scopus 로고
    • Crystal structure of the specificity domain of ribonuclease P
    • DOI 10.1038/nature01386
    • Krasilnikov AS, Yang X, Pan T, Mondragon A. 2003. Crystal structure of the specificity domain of ribonuclease P. Nature 421: 760-764. (Pubitemid 36227629)
    • (2003) Nature , vol.421 , Issue.6924 , pp. 760-764
    • Krasilnikov, A.S.1    Yang, X.2    Pan, T.3    Mondragon, A.4
  • 29
    • 6044275739 scopus 로고    scopus 로고
    • Basis for structural diversity in homologous RNAs
    • DOI 10.1126/science.1101489
    • Krasilnikov AS, Xiao Y, Pan T, Mondragon A. 2004. Basis for structural diversity in homologous RNAs. Science 306: 104-107. (Pubitemid 39451948)
    • (2004) Science , vol.306 , Issue.5693 , pp. 104-107
    • Krasilnikov, A.S.1    Xiao, Y.2    Pan, T.3    Mondragon, A.4
  • 30
    • 3142714285 scopus 로고    scopus 로고
    • Identification of a functional core in the RNA component of RNase MRP of budding yeasts
    • DOI 10.1093/nar/gkh689
    • Li X, Zaman S, Langdon Y, Zengel JM, Lindahl L. 2004. Identification of a functional core in the RNA component of RNase MRP of budding yeast. Nucleic Acids Res 32: 3703-3711. (Pubitemid 39157718)
    • (2004) Nucleic Acids Research , vol.32 , Issue.12 , pp. 3703-3711
    • Li, X.1    Zaman, S.2    Langdon, Y.3    Zengel, J.M.4    Lindahl, L.5
  • 31
    • 79959694817 scopus 로고    scopus 로고
    • Archaeal-bacterial chimeric RNase P RNAs: Towards understanding RNA's architecture, function and evolution
    • Li D, Gößringer M, Hartmann RK. 2011. Archaeal-bacterial chimeric RNase P RNAs: Towards understanding RNA's architecture, function and evolution. ChemBioChem 12: 1536-1543.
    • (2011) ChemBioChem , vol.12 , pp. 1536-1543
    • Li, D.1    Gößringer, M.2    Hartmann, R.K.3
  • 32
    • 67649386833 scopus 로고    scopus 로고
    • RNase MRP is required for entry of 35S precursor rRNA into the canonical processing pathway
    • Lindahl L, Bommankanti A, Li X, Hayden L, Jones A, Khan M, Oni T, Zengel JM. 2009. RNase MRP is required for entry of 35S precursor rRNA into the canonical processing pathway. RNA 15: 1407-1416.
    • (2009) RNA , vol.15 , pp. 1407-1416
    • Lindahl, L.1    Bommankanti, A.2    Li, X.3    Hayden, L.4    Jones, A.5    Khan, M.6    Oni, T.7    Zengel, J.M.8
  • 33
    • 77958512514 scopus 로고    scopus 로고
    • Conserved and variable domains of RNase MRP RNA
    • Lopez MD, Rosenblad MA, Samuelsson T. 2009. Conserved and variable domains of RNase MRP RNA. RNA Biol 6: 208-220.
    • (2009) RNA Biol , vol.6 , pp. 208-220
    • Lopez, M.D.1    Rosenblad, M.A.2    Samuelsson, T.3
  • 34
    • 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 AS, Schmitt ME. 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
  • 35
    • 0029981894 scopus 로고    scopus 로고
    • Accurate processing of a eukaryotic precursor ribosomal RNA by ribonuclease MRP in vitro
    • Lygerou Z, Allmang C, Tollervey D, Seraphin B. 1996. Accurate processing of a eukaryotic precursor ribosomal RNA by Ribonuclease MRP in vitro. Science 272: 268-270. (Pubitemid 26119139)
    • (1996) Science , vol.272 , Issue.5259 , pp. 268-270
    • Lygerou, Z.1    Allmang, C.2    Tollervey, D.3    Seraphin, B.4
  • 36
    • 33947314376 scopus 로고    scopus 로고
    • RNase MRP RNA and human genetic diseases
    • DOI 10.1038/sj.cr.7310120, PII 7310120
    • Martin AN, Li Y. 2007. RNase MRP RNA and human genetic diseases. Cell Res 17: 219-226. (Pubitemid 46438719)
    • (2007) Cell Research , vol.17 , Issue.3 , pp. 219-226
    • Martin, A.N.1    Li, Y.2
  • 37
    • 78649347991 scopus 로고    scopus 로고
    • The P3 domain of eukaryotic RNases P/MRP: Making a protein-rich RNA-based enzyme
    • Perederina A, Krasilnikov AS. 2010. The P3 domain of eukaryotic RNases P/MRP: Making a protein-rich RNA-based enzyme. RNA Biol 7: 534-539.
    • (2010) RNA Biol , vol.7 , pp. 534-539
    • Perederina, A.1    Krasilnikov, A.S.2
  • 38
    • 34748821927 scopus 로고    scopus 로고
    • Specific binding of a Pop6/Pop7 heterodimer to the P3 stem of the yeast RNase MRP and RNase P RNAs
    • DOI 10.1261/rna.654407
    • Perederina A, Esakova O, Koc H, Schmitt ME, Krasilnikov AS. 2007. Specific binding of a Pop6/Pop7 heterodimer to the P3 stem of the yeast RNase MRP and RNase P RNAs. RNA 13: 1648-1655. (Pubitemid 47481673)
    • (2007) RNA , vol.13 , Issue.10 , pp. 1648-1655
    • Perederina, A.1    Esakova, O.2    Koc, H.3    Schmitt, M.E.4    Krasilnikov, A.S.5
  • 39
    • 75149197944 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of the P3 RNA domain of yeast ribonuclease MRP in a complex with RNase P/MRP protein components Pop6 and Pop7
    • Perederina A, Esakova O, Quan C, Khanova E, Krasilnikov AS. 2010a. Crystallization and preliminary X-ray diffraction analysis of the P3 RNA domain of yeast ribonuclease MRP in a complex with RNase P/MRP protein components Pop6 and Pop7. Acta Crystallogr Sect F Struct Biol Cryst Commun 66: 76-80.
    • (2010) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.66 , pp. 76-80
    • Perederina, A.1    Esakova, O.2    Quan, C.3    Khanova, E.4    Krasilnikov, A.S.5
  • 40
    • 77149172542 scopus 로고    scopus 로고
    • Eukaryotic ribonucleases P/MRP: The crystal structure of the P3 domain
    • Perederina A, Esakova O, Quan C, Khanova E, Krasilnikov AS. 2010b. Eukaryotic ribonucleases P/MRP: the crystal structure of the P3 domain. EMBO J 29: 761-769.
    • (2010) EMBO J , vol.29 , pp. 761-769
    • Perederina, A.1    Esakova, O.2    Quan, C.3    Khanova, E.4    Krasilnikov, A.S.5
  • 41
    • 23344445110 scopus 로고    scopus 로고
    • Identification and analysis of ribonuclease P and MRP RNA in a broad range of eukaryotes
    • DOI 10.1093/nar/gki756
    • Piccinelli P, Rosenblad MA, Samuelsson T. 2005. Identification and analysis of Ribonuclease P and MRP RNA in a broad range of eukaryotes. Nucleic Acids Res 33: 4485-4495. (Pubitemid 41222563)
    • (2005) Nucleic Acids Research , vol.33 , Issue.14 , pp. 4485-4495
    • Piccinelli, P.1    Rosenblad, M.A.2    Samuelsson, T.3
  • 42
    • 0032899186 scopus 로고    scopus 로고
    • RNA-protein interactions in the human RNase MRP ribonucleoprotein complex
    • DOI 10.1017/S1355838299982079
    • Pluk H, van Eenennaam H, Rutjes SA, Pruijn GJM, van Venrooij WJ. 1999. RNA-protein interactions in the human RNase MRP ribonucleoprotein complex. RNA 5: 512-524. (Pubitemid 29169202)
    • (1999) RNA , vol.5 , Issue.4 , pp. 512-524
    • Pluk, H.1    Van Eenennaam, H.2    Rutjes, S.A.3    Pruijn, G.J.M.4    Van Venrooij, W.J.5
  • 43
    • 47249122660 scopus 로고    scopus 로고
    • Studies on Methanocaldococcus jannaschii RNase P reveal insights into the roles of RNA and protein cofactors in RNase P catalysis
    • DOI 10.1093/nar/gkn360
    • Pulukkunat DK, Gopalan V. 2008. Studies on Methanocaldococcus jannaschii RNase P reveal insights into the roles of RNA and protein cofactors in RNase P catalysis. Nucleic Acids Res 36: 4172-4180. (Pubitemid 351984832)
    • (2008) Nucleic Acids Research , vol.36 , Issue.12 , pp. 4172-4180
    • Pulukkunat, D.K.1    Gopalan, V.2
  • 47
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • DOI 10.1038/13732
    • Rigaut G, Shevchenko A, Rutz B, Wilm M, Mann M, Seraphin B. 1999. A generic protein purification method for protein complex characterization and proteome exploration. Nat Biotechnol 17: 1030-1032. (Pubitemid 29474865)
    • (1999) Nature Biotechnology , vol.17 , Issue.10 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Seraphin, B.6
  • 48
    • 33750988507 scopus 로고    scopus 로고
    • Inventory and analysis of the protein subunits of the ribonucleases P and MRP provides further evidence of homology between the yeast and human enzymes
    • DOI 10.1093/nar/gkl626
    • Rosenblad MA, Lopez MD, Piccinelli P, Samuelsson T. 2006. Inventory and analysis of the protein subunits of the ribonucleases P and MRP provides further evidence of homology between the yeast and human enzymes. Nucleic Acids Res 34: 5145-5156. (Pubitemid 44742479)
    • (2006) Nucleic Acids Research , vol.34 , Issue.18 , pp. 5145-5156
    • Rosenblad, M.A.1    Lopez, M.D.2    Piccinelli, P.3    Samuelsson, T.4
  • 49
    • 15744375062 scopus 로고    scopus 로고
    • Characterization and purification of Saccharomyces cerevisiae RNase MRP reveals a new unique protein component
    • DOI 10.1074/jbc.M409568200
    • Salinas K, Wierzbicki S, Zhou L, Schmitt ME. 2005. Characterization and purification of Saccharomyces cerevisiae RNase MRP reveals a new unique protein component. J Biol Chem 280: 11352-11360. (Pubitemid 40418443)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.12 , pp. 11352-11360
    • Salinas, K.1    Wierzbicki, S.2    Zhou, L.3    Schmitt, M.E.4
  • 50
    • 0026699593 scopus 로고
    • Yeast site-specific ribonucleoprotein endoribonuclease MRP contains an RNA component homologous to mammalian RNase MRP RNA and essential for cell viability
    • Schmitt ME, Clayton DA. 1992. Yeast site-specific ribonucleoprotein endoribonuclease MRP contains an RNA component homologous to mammalian RNase MRP RNA and essential for cell viability. Genes Dev 6: 1975-1985.
    • (1992) Genes Dev , vol.6 , pp. 1975-1985
    • Schmitt, M.E.1    Clayton, D.A.2
  • 51
    • 0027367147 scopus 로고
    • Nuclear RNase MRP is required for correct processing of pre-5.8S rRNA in Saccharomyces cerevisiae
    • Schmitt ME, Clayton DA. 1993. Nuclear RNase MRP is required for correct processing of pre-5.8S rRNA in Saccharomyces cerevisiae. Mol Cell Biol 13: 7935-7941. (Pubitemid 23354318)
    • (1993) Molecular and Cellular Biology , vol.13 , Issue.12 , pp. 7935-7941
    • Schmitt, M.E.1    Clayton, D.A.2
  • 53
    • 0034615627 scopus 로고    scopus 로고
    • Mutational analysis of the RNA component of Saccharomyces cerevisiae RNase MRP reveals distinct nuclear phenotypes
    • DOI 10.1016/S0378-1119(00)00013-5, PII S0378111900000135
    • Shadel GS, Buckenmeyer GA, Clayton DA, Schmitt ME. 2000. Mutational analysis of the RNA component of Saccharomyces cerevisiae RNase MRP reveals distinct nuclear phenotypes. Gene 245: 175-184. (Pubitemid 30125377)
    • (2000) Gene , vol.245 , Issue.1 , pp. 175-184
    • Shadel, G.S.1    Buckenmeyer, G.A.2    Clayton, D.A.3    Schmitt, M.E.4
  • 55
    • 0032076249 scopus 로고    scopus 로고
    • Ribonuclease P protein structure: Evolutionary origins in the translational apparatus
    • DOI 10.1126/science.280.5364.752
    • Stams T, Niranjanakumari S, Fierke CA, Christianson DW. 1998. Ribonuclease P protein structure: Evolutionary origins in the translational apparatus. Science 280: 752-755. (Pubitemid 28243353)
    • (1998) Science , vol.280 , Issue.5364 , pp. 752-755
    • Stams, T.1    Niranjanakumari, S.2    Fierke, C.A.3    Christianson, D.W.4
  • 56
    • 0030886172 scopus 로고    scopus 로고
    • Rpp1, an essential protein subunit of nuclear RNase P required for processing of precursor tRNA and 35S precursor rRNA in Saccharomyces cerevisiae
    • Stolc V, Altman S. 1997. Rpp1, an essential protein subunit of nuclear RNase P required for processing of precursor tRNA and 35S precursor rRNA in Saccharomyces cerevisiae. Genes Dev 11: 2414-2425. (Pubitemid 27408537)
    • (1997) Genes and Development , vol.11 , Issue.18 , pp. 2414-2425
    • Stolc, V.1    Altman, S.2
  • 59
    • 25644433566 scopus 로고    scopus 로고
    • Crystal structure of the RNA component of bacterial ribonuclease P
    • DOI 10.1038/nature04074, PII N04074
    • Torres-Larios A, Swinger KK, Krasilnikov AS, Pan T, Mondragon A. 2005. Crystal structure of the RNA component of bacterial ribonuclease P. Nature 437: 584-587. (Pubitemid 41613559)
    • (2005) Nature , vol.437 , Issue.7058 , pp. 584-587
    • Torres-Larios, A.1    Swinger, K.K.2    Krasilnikov, A.S.3    Pan, T.4    Mondragon, A.5
  • 61
    • 3342969661 scopus 로고    scopus 로고
    • A conserved element in the yeast RNase MRP RNA subunit can participate in a long-range base-pairing interaction
    • DOI 10.1016/j.jmb.2004.05.076, PII S0022283604006928
    • Walker SC, Avis JM. 2004. A conserved element in the yeast RNase MRP RNA subunit can participate in a long-range base-pairing interaction. J Mol Biol 341: 375-388. (Pubitemid 38987776)
    • (2004) Journal of Molecular Biology , vol.341 , Issue.2 , pp. 375-388
    • Walker, S.C.1    Avis, J.M.2
  • 62
    • 77953396580 scopus 로고    scopus 로고
    • Eukaryote RNase P and RNase MRP
    • ed. F. Liu and and S. Altman, Springer, New York
    • Walker SC, Marvin MC, Engelke DR. 2010. Eukaryote RNase P and RNase MRP. In Ribonuclease P, protein reviews 10 (ed. F. Liu and and S. Altman), pp. 173-202. Springer, New York.
    • (2010) Ribonuclease P, Protein Reviews 10 , pp. 173-202
    • Walker, S.C.1    Marvin, M.C.2    Engelke, D.R.3
  • 63
    • 2342599644 scopus 로고    scopus 로고
    • Mutual interactions between subunits of the human RNase MRP ribonucleoprotein complex
    • DOI 10.1093/nar/gkh539
    • Welting TJM, van Venrooij WJ, Pruijn GJM. 2004. Mutual interactions between subunits of the human RNase MRP ribonucleoprotein complex. Nucleic Acids Res 32: 2138-2146. (Pubitemid 38854769)
    • (2004) Nucleic Acids Research , vol.32 , Issue.7 , pp. 2138-2146
    • Welting, T.J.M.1    Van Verooij, W.J.2    Pruijn, G.J.M.3
  • 65
    • 34247645736 scopus 로고    scopus 로고
    • RNase MRP and the RNA processing cascade in the eukaryotic ancestor
    • doi: 10.1186/1471-2148-7-S1-S13
    • Woodhams MD, Stadler PF, Penny D, Collins LJ. 2007. RNase MRP and the RNA processing cascade in the eukaryotic ancestor. BMC Evol Biol 7: S13. doi: 10.1186/1471-2148-7-S1-S13.
    • (2007) BMC Evol Biol , vol.7
    • Woodhams, M.D.1    Stadler, P.F.2    Penny, D.3    Collins, L.J.4
  • 66
    • 70350020742 scopus 로고    scopus 로고
    • Solution structure of an archaeal RNase P binary protein complex: Formation of the 30-kDa complex between Pyrococcus furiosus RPP21 and RPP29 is accompanied by coupled protein folding and highlights critical features for protein-protein and protein-RNA interactions
    • Xu Y, Amero CD, Pulukkunat DK, Gopalan V, Foster MP. 2009. Solution structure of an archaeal RNase P binary protein complex: Formation of the 30-kDa complex between Pyrococcus furiosus RPP21 and RPP29 is accompanied by coupled protein folding and highlights critical features for protein-protein and protein-RNA interactions. J Mol Biol 393: 1043-1055.
    • (2009) J Mol Biol , vol.393 , pp. 1043-1055
    • Xu, Y.1    Amero, C.D.2    Pulukkunat, D.K.3    Gopalan, V.4    Foster, M.P.5
  • 67
    • 33646200077 scopus 로고    scopus 로고
    • Sequence analysis of RNase MRP RNA reveals its origination from eukaryotic RNase P RNA
    • Zhu Y, Stribinskis V, Ramos KS, 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


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