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Volumn 18, Issue 4, 2012, Pages 720-728

Structural organizations of yeast RNase P and RNase MRP holoenzymes as revealed by UV-crosslinking studies of RNA-protein interactions

Author keywords

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

Indexed keywords

FUNGAL ENZYME; HOLOENZYME; RIBONUCLEASE; RIBONUCLEASE MRP; RIBONUCLEASE P; RIBONUCLEOPROTEIN; UNCLASSIFIED DRUG;

EID: 84858667382     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.030874.111     Document Type: Article
Times cited : (17)

References (73)
  • 1
    • 77953426040 scopus 로고    scopus 로고
    • History of RNase P and overview of its catalytic activity
    • Ribonuclease P (ed. F Liu and S Altman), Springer, New York
    • Altman S. 2010. History of RNase P and overview of its catalytic activity. In Ribonuclease P (ed. F Liu and S Altman), Protein Reviews 10, pp. 1-15. Springer, New York.
    • (2010) Protein Reviews , vol.10 , pp. 1-15
    • Altman, S.1
  • 3
    • 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
  • 4
    • 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
  • 5
    • 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
  • 6
    • 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
  • 7
    • 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
  • 8
    • 79960713037 scopus 로고    scopus 로고
    • Cooperative RNP assembly: Complementarity rescue of structural defects by protein and RNA subunits of archaeal RNase P
    • Chen W-Y, Xu Y, Cho I-M, Oruganti SV, Foster MP, Gopalan V. 2011. Cooperative RNP assembly: Complementarity rescue of structural defects by protein and RNA subunits of archaeal RNase P. J Mol Biol 411: 368-383.
    • (2011) J Mol Biol , vol.411 , pp. 368-383
    • Chen, W.-Y.1    Xu, Y.2    Cho, I.-M.3    Oruganti, S.V.4    Foster, M.P.5    Gopalan, V.6
  • 11
    • 0030948643 scopus 로고    scopus 로고
    • A novel protein shared by RNase MRP and RNase P
    • Chu S, Zengel JM, Lindahl L. 1997. A novel protein shared by RNase MRP and RNase P. RNA 3: 382-391. (Pubitemid 27157671)
    • (1997) RNA , vol.3 , Issue.4 , pp. 382-391
    • Chu, S.1    Zengel, J.M.2    Lindahl, L.3
  • 12
    • 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 DJ, Pleiss JA, Walker SC, Whitworth GB, Engelke DR. 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 105: 12218-12223.
    • (2008) Proc Natl Acad Sci , 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
  • 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
    • 1642430571 scopus 로고    scopus 로고
    • RNase MRP Cleaves the CLB2 mRNA to Promote Cell Cycle Progression: Novel Method of mRNA Degradation
    • DOI 10.1128/MCB.24.3.945-953.2004
    • Gill T, Cai T, Aulds J, Wierzbicki S, Schmitt ME. 2004. RNase MRP cleaves the CLB2 mRNA to promote cell cycle progression: Novel method of mRNA degradation. Mol Cell Biol 24: 945-953. (Pubitemid 38112160)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.3 , pp. 945-953
    • Gill, T.1    Cai, T.2    Aulds, J.3    Wierzbicki, S.4    Schmitt, M.E.5
  • 17
    • 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
  • 18
    • 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
  • 19
    • 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. 1983. The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme. Cell 35: 849-857. (Pubitemid 14168384)
    • (1983) Cell , vol.35 , Issue.3 II , pp. 849-857
    • Guerrier-Takada, C.1    Gardiner, K.2    Marsh, T.3
  • 20
    • 0036231352 scopus 로고    scopus 로고
    • Archaeal RNase P has multiple protein subunits homologous to eukaryotic nuclear RNase P proteins
    • DOI 10.1017/S1355838202028492
    • Hall TA, Brown JW. 2002. Archaeal RNase P has multiple protein subunits homologous to eukaryotic nuclear RNase P proteins. RNA 8: 296-306. (Pubitemid 34311180)
    • (2002) RNA , vol.8 , Issue.3 , pp. 296-306
    • Hall, T.A.1    Brown, J.W.2
  • 23
    • 78650444089 scopus 로고    scopus 로고
    • Archaeal/eukaryal RNase P: Subunits, functions and diversification
    • Jarrous N, Gopalan V. 2010. Archaeal/eukaryal RNase P: Subunits, functions and diversification. Nucleic Acids Res 39: 7885-7894.
    • (2010) Nucleic Acids Res , vol.39 , pp. 7885-7894
    • Jarrous, N.1    Gopalan, V.2
  • 24
    • 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
  • 25
    • 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
  • 28
    • 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
  • 29
    • 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
  • 30
    • 58549095469 scopus 로고    scopus 로고
    • Minor changes largely restore catalytic activity of archaeal RNase P RNA from Methanothermobacter thermoautotrophicus
    • Li D, Willkomm DK, Hartmann RK. 2009. Minor changes largely restore catalytic activity of archaeal RNase P RNA from Methanothermobacter thermoautotrophicus. Nucleic Acids Res 37: 231-242.
    • (2009) Nucleic Acids Res , vol.37 , pp. 231-242
    • Li, D.1    Willkomm, D.K.2    Hartmann, R.K.3
  • 31
    • 0034118018 scopus 로고    scopus 로고
    • Functional equivalence of hairpins in the RNA subunits of RNase MRP and RNase P in Saccharomyces cerevisiae
    • DOI 10.1017/S1355838200992574
    • Lindahl L, Fretz S, Epps N, Zengel JM. 2000. Functional equivalence of hairpins in the RNA subunits of RNase MRP and RNase P in Saccharomyces cerevisiae. RNA 6: 653-658. (Pubitemid 30318460)
    • (2000) RNA , vol.6 , Issue.5 , pp. 653-658
    • Lindahl, L.1    Fretz, S.2    Epps, N.3    Zengel, J.M.4
  • 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
    • 0028244439 scopus 로고
    • The POP1 gene encodes a protein component common to the RNase MRP and RNase P ribonucleoproteins
    • Lygerou Z, Mitchell P, Petfalski E, Seraphin B, Tollervey D. 1994. The POP1 gene encodes a protein component common to the RNase MRP and RNase P ribonucleoproteins. Genes Dev 8: 1423-1433. (Pubitemid 24189809)
    • (1994) Genes and Development , vol.8 , Issue.12 , pp. 1423-1433
    • Lygerou, Z.1    Mitchell, P.2    Petfalski, E.3    Seraphin, B.4    Tollervey, D.5
  • 36
    • 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. 1996a. 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
  • 37
    • 0029954106 scopus 로고    scopus 로고
    • hPop1: An autoantigenic protein subunit shared by the human RNase P and RNase MRP ribonucleoproteins
    • Lygerou Z, Pluk H, van Venrooij WJ, Seraphin B. 1996b. hPop1: An autoantigenic protein subunit shared by the human RNase P and RNase MRP ribonucleoproteins. EMBO J 15: 5936-5948. (Pubitemid 26375515)
    • (1996) EMBO Journal , vol.15 , Issue.21 , pp. 5936-5948
    • Lygerou, Z.1    Pluk, H.2    Van Venrooij, W.J.3    Seraphin, B.4
  • 38
    • 71749105940 scopus 로고    scopus 로고
    • Broadening the mission of an RNA enzyme
    • Marvin MC, Engelke DR. 2009. Broadening the mission of an RNA enzyme. J Cell Biochem 108: 1244-1251.
    • (2009) J Cell Biochem , vol.108 , pp. 1244-1251
    • Marvin, M.C.1    Engelke, D.R.2
  • 40
    • 79960452027 scopus 로고    scopus 로고
    • Binding and cleavage of unstructured RNA by nuclear RNase P
    • Marvin MC, Walker SC, Fierke CA, Engelke DR. 2011b. Binding and cleavage of unstructured RNA by nuclear RNase P. RNA 17: 1429-1440.
    • (2011) RNA , vol.17 , pp. 1429-1440
    • Marvin, M.C.1    Walker, S.C.2    Fierke, C.A.3    Engelke, D.R.4
  • 42
    • 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
  • 43
    • 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
  • 44
    • 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
  • 45
    • 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
  • 46
    • 80053218807 scopus 로고    scopus 로고
    • Interactions of a Pop5/Rpp1 heterodimer with the catalytic domain of RNase MRP
    • Perederina A, Khanova E, Quan C, Berezin I, Esakova O, Krasilnikov AS. 2011. Interactions of a Pop5/Rpp1 heterodimer with the catalytic domain of RNase MRP. RNA 17: 1922-1931.
    • (2011) RNA , vol.17 , pp. 1922-1931
    • Perederina, A.1    Khanova, E.2    Quan, C.3    Berezin, I.4    Esakova, O.5    Krasilnikov, A.S.6
  • 47
    • 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
  • 48
    • 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
  • 49
    • 33745123379 scopus 로고    scopus 로고
    • A role for the catalytic ribonucleoprotein RNase P in RNA polymerase III transcription
    • DOI 10.1101/gad.386706
    • Reiner R, Ben-Asouli Y, Krilovetzky I, Jarrous N. 2006. A role for the catalytic ribonucleoprotein RNase P in RNA polymerase III transcription. Genes Dev 20: 1621-1635. (Pubitemid 43901101)
    • (2006) Genes and Development , vol.20 , Issue.12 , pp. 1621-1635
    • Reiner, R.1    Ben-Asouli, Y.2    Krilovetzky, I.3    Jarrous, N.4
  • 50
    • 58149189840 scopus 로고    scopus 로고
    • Function and assembly of a chromatin-associated RNase P that is required for efficient transcription by RNA polymerase I
    • doi: 10.1371/journal.pone.0004072
    • Reiner R, Krasnov-Yoeli N, Dehtiar Y, Jarrous N. 2008. Function and assembly of a chromatin-associated RNase P that is required for efficient transcription by RNA polymerase I. PLoS ONE 3: e4072. doi: 10.1371/journal.pone. 0004072.
    • (2008) PLoS ONE , vol.3
    • Reiner, R.1    Krasnov-Yoeli, N.2    Dehtiar, Y.3    Jarrous, N.4
  • 54
    • 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
  • 55
    • 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
  • 56
    • 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
  • 57
    • 0027942999 scopus 로고
    • Characterization of a unique protein component of yeast RNase MRP: An RNA-binding protein with a zinc-cluster domain
    • Schmitt ME, Clayton DA. 1994. Characterization of a unique protein component of yeast RNase MRP: An RNA-binding protein with a zinc-cluster domain. Genes Dev 8: 2617-2628.
    • (1994) Genes Dev , vol.8 , pp. 2617-2628
    • Schmitt, M.E.1    Clayton, D.A.2
  • 59
    • 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
  • 60
    • 79951570571 scopus 로고    scopus 로고
    • Cleavage of model substrates by archaeal RNase P: Role of protein cofactors in cleavage-site selection
    • Sinapah S, Wu S, Chen Y, Pettersson BM, Gopalan V, Kirsebom LA. 2011. Cleavage of model substrates by archaeal RNase P: Role of protein cofactors in cleavage-site selection. Nucleic Acids Res 39: 1105-1116.
    • (2011) Nucleic Acids Res , vol.39 , pp. 1105-1116
    • Sinapah, S.1    Wu, S.2    Chen, Y.3    Pettersson, B.M.4    Gopalan, V.5    Kirsebom, L.A.6
  • 62
    • 0034004463 scopus 로고    scopus 로고
    • Evidence for an RNA-based catalytic mechanism in eukaryotic nuclear ribonuclease P
    • DOI 10.1017/S1355838200991477
    • Thomas BC, Chamberlain J, Engelke DR, Gegenheimer P. 2000. Evidence for an RNA-based catalytic mechanism in eukaryotic nuclear ribonuclease P. RNA 6: 554-562. (Pubitemid 30212233)
    • (2000) RNA , vol.6 , Issue.4 , pp. 554-562
    • Thomas, B.C.1    Chamberlain, J.2    Engelke, D.R.3    Gegenheimer, P.4
  • 63
    • 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
  • 67
    • 84858641797 scopus 로고    scopus 로고
    • Protein-RNA crosslinking in native ribonucleoprotein particles
    • (ed. RK Hartmann et al.). Wiley-VCH Verlag GmbH, Weinheim, Germany
    • Urlaub H, Hartmuth K, Lührmann R. 2008. Protein-RNA crosslinking in native ribonucleoprotein particles. In Handbook of RNA biochemistry (ed. RK Hartmann et al.). Wiley-VCH Verlag GmbH, Weinheim, Germany.
    • (2008) Handbook of RNA Biochemistry
    • Urlaub, H.1    Hartmuth, K.2    Lührmann, R.3
  • 68
    • 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
  • 70
    • 33646887365 scopus 로고    scopus 로고
    • Functional characterization of the conserved amino acids in Pop1p, the largest common protein subunit of yeast RNases P and MRP
    • DOI 10.1261/rna.23206
    • Xiao SH, Hsien J, Nugent RL, Coughlin DJ, Fierke CA, Engelke DR. 2006. Functional characterization of the concerved amino acids in Pop1p, the largest common protein subunit of yeast RNases P and MRP. RNA 12: 1023-1037. (Pubitemid 43788121)
    • (2006) RNA , vol.12 , Issue.6 , pp. 1023-1037
    • Xiao, S.1    Hsieh, J.2    Nugent, R.L.3    Coughlin, D.J.4    Fierke, C.A.5    Engelke, D.R.6
  • 71
    • 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
  • 72
    • 0035010212 scopus 로고    scopus 로고
    • An essential protein-binding domain of nuclear RNase P RNA
    • DOI 10.1017/S1355838201001996
    • Ziehler WA, Morris J, Scott FH, Millikin C, Engelke DR. 2001. An essential protein-binding domain of nuclear RNase P RNA. RNA 7: 565-575. (Pubitemid 32416814)
    • (2001) RNA , vol.7 , Issue.4 , pp. 565-575
    • Ziehler, W.A.1    Morris, J.2    Scott, F.H.3    Millikin, C.4    Engelke, D.R.5


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