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Volumn 411, Issue 2, 2011, Pages 368-383

Cooperative RNP assembly: Complementary rescue of structural defects by protein and RNA subunits of archaeal RNase P

Author keywords

in vitro reconstitution; mutational rescue; pre tRNA processing

Indexed keywords

BACTERIAL ENZYME; MUTANT PROTEIN; RIBONUCLEASE P; TRYPSIN; TYROSINE TRANSFER RNA; URIDINE;

EID: 79960713037     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.05.012     Document Type: Article
Times cited : (12)

References (76)
  • 1
    • 33745166320 scopus 로고    scopus 로고
    • RNase P: Interface of the RNA and protein worlds
    • DOI 10.1016/j.tibs.2006.04.007, PII S0968000406001174
    • Evans D.; Marquez S.M.; and Pace N.R. RNase P: interface of the RNA and protein worlds Trends Biochem. Sci. 31 2006 333 341 (Pubitemid 43903240)
    • (2006) Trends in Biochemical Sciences , vol.31 , Issue.6 , pp. 333-341
    • Evans, D.1    Marquez, S.M.2    Pace, N.R.3
  • 2
    • 71549154663 scopus 로고    scopus 로고
    • Unexpected diversity of RNase P, an ancient tRNA processing enzyme: Challenges and prospects
    • Lai L.B.; Vioque A.; Kirsebom L.A.; and Gopalan V. Unexpected diversity of RNase P, an ancient tRNA processing enzyme: challenges and prospects FEBS Lett. 584 2010 287 296
    • (2010) FEBS Lett. , vol.584 , pp. 287-296
    • Lai, L.B.1    Vioque, A.2    Kirsebom, L.A.3    Gopalan, V.4
  • 4
    • 33645747326 scopus 로고    scopus 로고
    • Ribonuclease P: The evolution of an ancient RNA enzyme
    • Walker S.C.; and Engelke D.R. Ribonuclease P: the evolution of an ancient RNA enzyme Crit. Rev. Biochem. Mol. Biol. 41 2006 77 102
    • (2006) Crit. Rev. Biochem. Mol. Biol. , vol.41 , pp. 77-102
    • Walker, S.C.1    Engelke, D.R.2
  • 6
    • 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.; and Rossmanith W. RNase P without RNA: identification and functional reconstitution of the human mitochondrial tRNA processing enzyme Cell 135 2008 462 474
    • (2008) Cell , vol.135 , pp. 462-474
    • Holzmann, J.1    Frank, P.2    Loffler, E.3    Bennett, K.L.4    Gerner, C.5    Rossmanith, W.6
  • 7
    • 0036231352 scopus 로고    scopus 로고
    • Archaeal RNase P has multiple protein subunits homologous to eukaryotic nuclear RNase P proteins
    • DOI 10.1017/S1355838202028492
    • Hall T.A.; and Brown J.W. Archaeal RNase P has multiple protein subunits homologous to eukaryotic nuclear RNase P proteins RNA 8 2002 296 306 (Pubitemid 34311180)
    • (2002) RNA , vol.8 , Issue.3 , pp. 296-306
    • Hall, T.A.1    Brown, J.W.2
  • 8
    • 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. The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme Cell 35 1983 849 857 (Pubitemid 14168384)
    • (1983) Cell , vol.35 , pp. 849-857
    • Guerrier-Takada, C.1    Gardiner, K.2    Marsh, T.3
  • 11
    • 77953400424 scopus 로고    scopus 로고
    • Archael RNase P: A mosaic of its bacterial and eukaryal relatives
    • F. Liu, S. Altman, Springer Verlag New York
    • Lai L.B.; Cho I.M.; Chen W.Y.; and Gopalan V. Archael RNase P: a mosaic of its bacterial and eukaryal relatives F. Liu, S. Altman, Ribonuclease P 2010 Springer Verlag New York 153 172
    • (2010) Ribonuclease P , pp. 153-172
    • Lai, L.B.1    Cho, I.M.2    Chen, W.Y.3    Gopalan, V.4
  • 13
    • 77957157307 scopus 로고    scopus 로고
    • Dissecting functional cooperation among protein subunits in archaeal RNase P, a catalytic ribonucleoprotein complex
    • Chen W.Y.; Pulukkunat D.K.; Cho I.M.; Tsai H.Y.; and Gopalan V. Dissecting functional cooperation among protein subunits in archaeal RNase P, a catalytic ribonucleoprotein complex Nucleic Acids Res. 38 2010 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
  • 16
    • 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 D.K.; and Gopalan V. Studies on Methanocaldococcus jannaschii RNase P reveal insights into the roles of RNA and protein cofactors in RNase P catalysis Nucleic Acids Res. 36 2008 4172 4180 (Pubitemid 351984832)
    • (2008) Nucleic Acids Research , vol.36 , Issue.12 , pp. 4172-4180
    • Pulukkunat, D.K.1    Gopalan, V.2
  • 18
    • 55849120858 scopus 로고    scopus 로고
    • Solution structure of Pyrococcus furiosus RPP21, a component of the archaeal RNase P holoenzyme, and interactions with its RPP29 protein partner
    • Amero C.D.; Boomershine W.P.; Xu Y.; and Foster M. Solution structure of Pyrococcus furiosus RPP21, a component of the archaeal RNase P holoenzyme, and interactions with its RPP29 protein partner Biochemistry 47 2008 11704 11710
    • (2008) Biochemistry , vol.47 , pp. 11704-11710
    • Amero, C.D.1    Boomershine, W.P.2    Xu, Y.3    Foster, M.4
  • 19
    • 55349099821 scopus 로고    scopus 로고
    • Structure of an archaeal homolog of the human protein complex Rpp21-Rpp29 that is a key core component for the assembly of active ribonuclease P
    • Honda T.; Kakuta Y.; Kimura K.; Saho J.; and Kimura M. Structure of an archaeal homolog of the human protein complex Rpp21-Rpp29 that is a key core component for the assembly of active ribonuclease P J. Mol. Biol. 384 2008 652 662
    • (2008) J. Mol. Biol. , vol.384 , pp. 652-662
    • Honda, T.1    Kakuta, Y.2    Kimura, K.3    Saho, J.4    Kimura, M.5
  • 20
    • 24644469952 scopus 로고    scopus 로고
    • Crystal structure of a ribonuclease P protein Ph1601p from Pyrococcus horikoshii OT3: An archaeal homologue of human nuclear ribonuclease P protein Rpp21
    • DOI 10.1021/bi050738z
    • Kakuta Y.; Ishimatsu I.; Numata T.; Kimura K.; Yao M.; Tanaka I.; and Kimura M. Crystal structure of a ribonuclease P protein Ph1601p from Pyrococcus horikoshii OT3: an archaeal homologue of human nuclear ribonuclease P protein Rpp21 Biochemistry 44 2005 12086 12093 (Pubitemid 41285706)
    • (2005) Biochemistry , vol.44 , Issue.36 , pp. 12086-12093
    • Kakuta, Y.1    Ishimatsu, I.2    Numata, T.3    Kimura, K.4    Yao, M.5    Tanaka, I.6    Kimura, M.7
  • 21
    • 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.; and Kimura M. 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 2006 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
  • 22
    • 8344266164 scopus 로고    scopus 로고
    • Crystal structure of archaeal ribonuclease P protein aRpp29 from Archaeoglobus fulgidus
    • DOI 10.1021/bi048578z
    • Sidote D.J.; Heideker J.; and Hoffman D.W. Crystal structure of archaeal ribonuclease P protein aRpp29 from Archaeoglobus fulgidus Biochemistry 43 2004 14128 14138 (Pubitemid 39482763)
    • (2004) Biochemistry , vol.43 , Issue.44 , pp. 14128-14138
    • Sidote, D.J.1    Heideker, J.2    Hoffman, D.W.3
  • 23
    • 0344823672 scopus 로고    scopus 로고
    • NMR Structure of an Archaeal Homologue of Ribonuclease P Protein Rpp29
    • DOI 10.1021/bi030170z
    • Sidote D.J.; and Hoffman D.W. NMR structure of an archaeal homologue of ribonuclease P protein Rpp29 Biochemistry 42 2003 13541 13550 (Pubitemid 37444905)
    • (2003) Biochemistry , vol.42 , Issue.46 , pp. 13541-13550
    • Sidote, D.J.1    Hoffman, D.W.2
  • 25
    • 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 C.D.; Pulukkunat D.K.; Gopalan V.; and Foster M.P. 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 2009 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
  • 26
    • 4344638194 scopus 로고    scopus 로고
    • Crystal structure of archaeal ribonuclease P protein Ph1771p from Pyrococcus horikoshii OT3: An archaeal homolog of eukaryotic ribonuclease P protein Rpp29
    • DOI 10.1261/rna.7560904
    • Numata T.; Ishimatsu I.; Kakuta Y.; Tanaka I.; and Kimura M. Crystal structure of archaeal ribonuclease P protein Ph1771p from Pyrococcus horikoshii OT3: an archaeal homolog of eukaryotic ribonuclease P protein Rpp29 RNA 10 2004 1423 1432 (Pubitemid 39122112)
    • (2004) RNA , vol.10 , Issue.9 , pp. 1423-1432
    • Numata, T.1    Ishimatsu, I.2    Kakuta, Y.3    Tanaka, I.4    Kimura, M.5
  • 27
    • 0344298926 scopus 로고    scopus 로고
    • The ribonuclease P database
    • DOI 10.1093/nar/27.1.314
    • Brown J.W. The Ribonuclease P Database Nucleic Acids Res. 27 1999 314 (Pubitemid 29209471)
    • (1999) Nucleic Acids Research , vol.27 , Issue.1 , pp. 314
    • Brown, J.W.1
  • 29
    • 0032546728 scopus 로고    scopus 로고
    • Derivation of the three-dimensional architecture of bacterial ribonuclease P RNAs from comparative sequence analysis
    • DOI 10.1006/jmbi.1998.1797
    • Massire C.; Jaeger L.; and Westhof E. Derivation of the three-dimensional architecture of bacterial ribonuclease P RNAs from comparative sequence analysis J. Mol. Biol. 279 1998 773 793 (Pubitemid 28284694)
    • (1998) Journal of Molecular Biology , vol.279 , Issue.4 , pp. 773-793
    • Massire, C.1    Jaeger, L.2    Westhof, E.3
  • 30
    • 0036445585 scopus 로고    scopus 로고
    • Conservation of helical structure contributes to functional metal ion interactions in the catalytic domain of ribonuclease P RNA
    • DOI 10.1016/S0022-2836(02)01094-X
    • Kaye N.M.; Zahler N.H.; Christian E.L.; and Harris M.E. Conservation of helical structure contributes to functional metal ion interactions in the catalytic domain of ribonuclease P RNA J. Mol. Biol. 324 2002 429 442 (Pubitemid 35430510)
    • (2002) Journal of Molecular Biology , vol.324 , Issue.3 , pp. 429-442
    • Kaye, N.M.1    Zahler, N.H.2    Christian, E.L.3    Harris, M.E.4
  • 31
    • 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. Helix P4 is a divalent metal ion binding site in the conserved core of the ribonuclease P ribozyme RNA 6 2000 511 519 (Pubitemid 30212229)
    • (2000) RNA , vol.6 , Issue.4 , pp. 511-519
    • Christian, E.L.1    Kaye, N.M.2    Harris, M.E.3
  • 32
    • 0036566051 scopus 로고    scopus 로고
    • Evidence for a polynuclear metal ion binding site in the catalytic domain of ribonuclease P RNA
    • DOI 10.1093/emboj/21.9.2253
    • Christian E.L.; Kaye N.M.; and Harris M.E. Evidence for a polynuclear metal ion binding site in the catalytic domain of ribonuclease P RNA EMBO J. 21 2002 2253 2262 (Pubitemid 34516784)
    • (2002) EMBO Journal , vol.21 , Issue.9 , pp. 2253-2262
    • Christian, E.L.1    Kaye, N.M.2    Harris, M.E.3
  • 33
    • 0036071392 scopus 로고    scopus 로고
    • Specific phosphorothioate substitutions probe the active site of Bacillus subtilis ribonuclease P
    • DOI 10.1017/S1355838202025025
    • Crary S.M.; Kurz J.C.; and Fierke C.A. Specific phosphorothioate substitutions probe the active site of Bacillus subtilis ribonuclease P RNA 8 2002 933 947 (Pubitemid 34787690)
    • (2002) RNA , vol.8 , Issue.7 , pp. 933-947
    • Crary, S.M.1    Kurz, J.C.2    Fierke, C.A.3
  • 35
    • 0035259427 scopus 로고    scopus 로고
    • New insight into RNase P RNA structure from comparative analysis of the archaeal RNA
    • DOI 10.1017/S1355838201001777
    • Harris J.K.; Haas E.S.; Williams D.; Frank D.N.; and Brown J.W. New insight into RNase P RNA structure from comparative analysis of the archaeal RNA RNA 7 2001 220 232 (Pubitemid 33590505)
    • (2001) RNA , vol.7 , Issue.2 , pp. 220-232
    • Harris, J.K.1    Haas, E.S.2    Williams, D.3    Frank, D.N.4    Brown, J.W.5
  • 36
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D.; Higgins D.G.; and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 22 1994 4673 4680 (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 37
    • 0032581021 scopus 로고    scopus 로고
    • The protein component of Bacillus subtilis ribonuclease P increases catalytic efficiency by enhancing interactions with the 5' leader sequence of pre-tRNA(Asp)
    • DOI 10.1021/bi980613c
    • Crary S.M.; Niranjanakumari S.; and Fierke C.A. The protein component of Bacillus subtilis ribonuclease P increases catalytic efficiency by enhancing interactions with the 5′ leader sequence of pre-tRNAAsp Biochemistry 37 1998 9409 9416 (Pubitemid 28307696)
    • (1998) Biochemistry , vol.37 , Issue.26 , pp. 9409-9416
    • Crary, S.M.1    Niranjanakumari, S.2    Fierke, C.A.3
  • 38
    • 0024851604 scopus 로고
    • Specific interactions in RNA enzyme-substrate complexes
    • Guerrier-Takada C.; Lumelsky N.; and Altman S. Specific interactions in RNA enzyme-substrate complexes Science 246 1989 1578 1584 (Pubitemid 20036689)
    • (1989) Science , vol.246 , Issue.4937 , pp. 1578-1584
    • Guerrier-Takada, C.1    Lumelsky, N.2    Altman, S.3
  • 39
    • 0037199416 scopus 로고    scopus 로고
    • The affinity of magnesium binding sites in the Bacillus subtilis RNase PPre-tRNA complex is enhanced by the protein subunit
    • DOI 10.1021/bi025553w
    • Kurz J.C.; and Fierke C.A. The affinity of magnesium binding sites in the Bacillus subtilis RNase P × pre-tRNA complex is enhanced by the protein subunit Biochemistry 41 2002 9545 9558 (Pubitemid 34810030)
    • (2002) Biochemistry , vol.41 , Issue.30 , pp. 9545-9558
    • Kurz, J.C.1    Fierke, C.A.2
  • 40
    • 0032562128 scopus 로고    scopus 로고
    • Protein component of Bacillus subtilis RNase P specifically enhances the affinity for precursor-tRNA(Asp)
    • DOI 10.1021/bi972530m
    • Kurz J.C.; Niranjanakumari S.; and Fierke C.A. Protein component of Bacillus subtilis RNase P specifically enhances the affinity for precursor-tRNAAsp Biochemistry 37 1998 2393 2400 (Pubitemid 28119314)
    • (1998) Biochemistry , vol.37 , Issue.8 , pp. 2393-2400
    • Kurz, J.C.1    Niranjanakumari, S.2    Fierke, C.A.3
  • 41
    • 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. 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 1991 1 5 (Pubitemid 121003548)
    • (1991) Journal of Molecular Biology , vol.221 , Issue.1 , pp. 1-5
    • Peck-Miller, K.A.1    Altman, S.2
  • 42
    • 73649122748 scopus 로고    scopus 로고
    • Binding of C5 protein to P RNA enhances the rate constant for catalysis for P RNA processing of pre-tRNAs lacking a consensus (+ 1)/C(+ 72) pair
    • Sun L.; Campbell F.E.; Yandek L.E.; and Harris M.E. Binding of C5 protein to P RNA enhances the rate constant for catalysis for P RNA processing of pre-tRNAs lacking a consensus (+ 1)/C(+ 72) pair J. Mol. Biol. 395 2010 1019 1037
    • (2010) J. Mol. Biol. , vol.395 , pp. 1019-1037
    • Sun, L.1    Campbell, F.E.2    Yandek, L.E.3    Harris, M.E.4
  • 43
    • 34548371821 scopus 로고    scopus 로고
    • Evidence that binding of C5 protein to P RNA enhances ribozyme catalysis by influencing active site metal ion affinity
    • DOI 10.1261/rna.571007
    • Sun L.; and Harris M.E. Evidence that binding of C5 protein to P RNA enhances ribozyme catalysis by influencing active site metal ion affinity RNA 13 2007 1505 1515 (Pubitemid 47347421)
    • (2007) RNA , vol.13 , Issue.9 , pp. 1505-1515
    • Sun, L.1    Harris, M.E.2
  • 44
    • 0037462929 scopus 로고    scopus 로고
    • Molecular modeling of the three-dimensional structure of the bacterial RNase P holoenzyme
    • DOI 10.1016/S0022-2836(02)01267-6
    • Tsai H.Y.; Masquida B.; Biswas R.; Westhof E.; and Gopalan V. Molecular modeling of the three-dimensional structure of the bacterial RNase P holoenzyme J. Mol. Biol. 325 2003 661 675 (Pubitemid 36268690)
    • (2003) Journal of Molecular Biology , vol.325 , Issue.4 , pp. 661-675
    • Tsai, H.-Y.1    Masquida, B.2    Biswas, R.3    Westhof, E.4    Gopalan, V.5
  • 45
    • 79960718013 scopus 로고    scopus 로고
    • PhD thesis, The Ohio State University, Columbus, OH
    • Xu, Y. (2009). PhD thesis, The Ohio State University, Columbus, OH.
    • (2009)
    • Xu, Y.1
  • 46
    • 77953699478 scopus 로고    scopus 로고
    • A divalent cation stabilizes the active conformation of the B. subtilis RNase P × pre-tRNA complex: A role for an inner-sphere metal ion in RNase P
    • Hsieh J.; Koutmou K.S.; Rueda D.; Koutmos M.; Walter N.G.; and Fierke C.A. A divalent cation stabilizes the active conformation of the B. subtilis RNase P × pre-tRNA complex: a role for an inner-sphere metal ion in RNase P J. Mol. Biol. 400 2010 38 51
    • (2010) J. Mol. Biol. , vol.400 , pp. 38-51
    • Hsieh, J.1    Koutmou, K.S.2    Rueda, D.3    Koutmos, M.4    Walter, N.G.5    Fierke, C.A.6
  • 47
    • 67651007225 scopus 로고    scopus 로고
    • Conformational change in the Bacillus subtilis RNase P holoenzyme-pre-tRNA complex enhances substrate affinity and limits cleavage rate
    • Hsieh J.; and Fierke C.A. Conformational change in the Bacillus subtilis RNase P holoenzyme-pre-tRNA complex enhances substrate affinity and limits cleavage rate RNA 15 2009 1565 1577
    • (2009) RNA , vol.15 , pp. 1565-1577
    • Hsieh, J.1    Fierke, C.A.2
  • 48
    • 0032516438 scopus 로고    scopus 로고
    • Recognition of the 5' leader and the acceptor stem of a pre-tRNA substrate by the ribozyme from Bacillus subtilis RNase P
    • DOI 10.1021/bi980220d
    • Loria A.; and Pan T. Recognition of the 5′ leader and the acceptor stem of a pre-tRNA substrate by the ribozyme from Bacillus subtilis RNase P Biochemistry 37 1998 10126 10133 (Pubitemid 28366367)
    • (1998) Biochemistry , vol.37 , Issue.28 , pp. 10126-10133
    • Loria, A.1    Pan, T.2
  • 49
    • 0001191811 scopus 로고    scopus 로고
    • Multiple binding modes of substrate to the catalytic RNA subunit of RNase P from Escherichia coli
    • DOI 10.1017/S1355838299990416
    • Pomeranz Krummel D.A.; and Altman S. Multiple binding modes of substrate to the catalytic RNA subunit of RNase P from Escherichia coli RNA 5 1999 1021 1033 (Pubitemid 29365332)
    • (1999) RNA , vol.5 , Issue.8 , pp. 1021-1033
    • Pomeranz Krummel, D.A.1    Altman, S.2
  • 50
    • 33748361597 scopus 로고    scopus 로고
    • Evidence that substrate-specific effects of C5 protein lead to uniformity in binding and catalysis by RNase P
    • DOI 10.1038/sj.emboj.7601290, PII 7601290
    • Sun L.; Campbell F.E.; Zahler N.H.; and Harris M.E. Evidence that substrate-specific effects of C5 protein lead to uniformity in binding and catalysis by RNase P EMBO J. 25 2006 3998 4007 (Pubitemid 44338742)
    • (2006) EMBO Journal , vol.25 , Issue.17 , pp. 3998-4007
    • Sun, L.1    Campbell, F.E.2    Zahler, N.H.3    Harris, M.E.4
  • 51
    • 0036940303 scopus 로고    scopus 로고
    • Metal ions in the structure and function of RNA
    • DOI 10.1007/s00775-002-0387-6
    • Pyle A.M. Metal ions in the structure and function of RNA J. Biol. Inorg. Chem. 7 2002 679 690 (Pubitemid 36056354)
    • (2002) Journal of Biological Inorganic Chemistry , vol.7 , Issue.7-8 , pp. 679-690
    • Pyle, A.M.1
  • 53
    • 58749105663 scopus 로고    scopus 로고
    • RNA folding: Thermodynamic and molecular descriptions of the roles of ions
    • Draper D.E. RNA folding: thermodynamic and molecular descriptions of the roles of ions Biophys. J. 95 2008 5489 5495
    • (2008) Biophys. J. , vol.95 , pp. 5489-5495
    • Draper, D.E.1
  • 54
    • 4043057879 scopus 로고    scopus 로고
    • Analysis of solvent nucleophile isotope effects: Evidence for concerted mechanisms and nucleophilic activation by metal coordination in nonenzymatic and ribozyme-catalyzed phosphodiester hydrolysis
    • DOI 10.1021/bi049188f
    • Cassano A.G.; Anderson V.E.; and Harris M.E. Analysis of solvent nucleophile isotope effects: evidence for concerted mechanisms and nucleophilic activation by metal coordination in nonenzymatic and ribozyme-catalyzed phosphodiester hydrolysis Biochemistry 43 2004 10547 10559 (Pubitemid 39079325)
    • (2004) Biochemistry , vol.43 , Issue.32 , pp. 10547-10559
    • Cassano, A.G.1    Anderson, V.E.2    Harris, M.E.3
  • 55
    • 0027256149 scopus 로고
    • Multiple magnesium ions in the ribonuclease P reaction mechanism
    • Smith D.; and Pace N.R. Multiple magnesium ions in the ribonuclease P reaction mechanism Biochemistry 32 1993 5273 5281 (Pubitemid 23167967)
    • (1993) Biochemistry , vol.32 , Issue.20 , pp. 5273-5281
    • Smith, D.1    Pace, N.R.2
  • 56
    • 34548501510 scopus 로고    scopus 로고
    • Evidence for Induced Fit in Bacterial RNase P RNA-mediated Cleavage
    • DOI 10.1016/j.jmb.2007.07.030, PII S0022283607009436
    • Brannvall M.; Kikovska E.; Wu S.; and Kirsebom L.A. Evidence for induced fit in bacterial RNase P RNA-mediated cleavage J. Mol. Biol. 372 2007 1149 1164 (Pubitemid 47374716)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.5 , pp. 1149-1164
    • Brannvall, M.1    Kikovska, E.2    Wu, S.3    Kirsebom, L.A.4
  • 58
    • 0027973546 scopus 로고
    • Base pairing between Escherichia coli RNase P RNA and its substrate
    • Kirsebom L.A.; and Svard S.G. Base pairing between Escherichia coli RNase P RNA and its substrate EMBO J. 13 1994 4870 4876 (Pubitemid 24319370)
    • (1994) EMBO Journal , vol.13 , Issue.20 , pp. 4870-4876
    • Kirsebom, L.A.1    Svard, S.G.2
  • 59
    • 71549119274 scopus 로고    scopus 로고
    • RNase P RNA-mediated cleavage
    • Kirsebom L.A.; and Trobro S. RNase P RNA-mediated cleavage IUBMB Life 61 2009 189 200
    • (2009) IUBMB Life , vol.61 , pp. 189-200
    • Kirsebom, L.A.1    Trobro, S.2
  • 60
    • 0029949699 scopus 로고    scopus 로고
    • Domain structure of the ribozyme from eubacterial ribonuclease P
    • Loria A.; and Pan T. Domain structure of the ribozyme from eubacterial ribonuclease P RNA 2 1996 551 563 (Pubitemid 26374227)
    • (1996) RNA , vol.2 , Issue.6 , pp. 551-563
    • Loria, A.1    Pan, T.2
  • 61
    • 0029556990 scopus 로고
    • Probing of tertiary interactions in RNA: 2′-hydroxyl-base contacts between the RNase P RNA and pre-tRNA
    • Pan T.; Loria A.; and Zhong K. Probing of tertiary interactions in RNA: 2′-hydroxyl-base contacts between the RNase P RNA and pre-tRNA Proc. Natl Acad. Sci. USA 92 1995 12510 12514
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 12510-12514
    • Pan, T.1    Loria, A.2    Zhong, K.3
  • 62
    • 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 K.K.; Krasilnikov A.S.; Pan T.; and Mondragon A. Crystal structure of the RNA component of bacterial ribonuclease P Nature 437 2005 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
  • 63
    • 0038475910 scopus 로고    scopus 로고
    • Recognition of the 5′ leader of pre-tRNA substrates by the active site of ribonuclease P
    • DOI 10.1261/rna.5220703
    • Zahler N.H.; Christian E.L.; and Harris M.E. Recognition of the 5′ leader of pre-tRNA substrates by the active site of ribonuclease P RNA 9 2003 734 745 (Pubitemid 36618201)
    • (2003) RNA , vol.9 , Issue.6 , pp. 734-745
    • Zahler, N.H.1    Christian, E.L.2    Harris, M.E.3
  • 64
    • 0028131972 scopus 로고
    • Interaction of the 3′-end of tRNA with ribonuclease P RNA
    • Oh B.K.; and Pace N.R. Interaction of the 3′-end of tRNA with ribonuclease P RNA Nucleic Acids Res. 22 1994 4087 4094
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4087-4094
    • Oh, B.K.1    Pace, N.R.2
  • 65
    • 36148982232 scopus 로고    scopus 로고
    • Identification of nucleotide residues essential for RNase P activity from the hyperthermophilic archaeon Pyrococcus horikoshii OT3
    • DOI 10.1271/bbb.70145
    • Terada A.; Yoshida T.; and Kimura M. Identification of nucleotide residues essential for RNase P activity from the hyperthermophilic archaeon Pyrococcus horikoshii OT3 Biosci. Biotechnol. Biochem. 71 2007 1940 1945 (Pubitemid 350113135)
    • (2007) Bioscience, Biotechnology and Biochemistry , vol.71 , Issue.8 , pp. 1940-1945
    • Terada, A.1    Yoshida, T.2    Kimura, M.3
  • 66
    • 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 B.M.F.; Gopalan V.; and Kirsebom L.A. Cleavage of model substrates by archaeal RNase P: role of protein cofactors in cleavage-site selection Nucleic Acids Res. 39 2011 1105 1116
    • (2011) Nucleic Acids Res. , vol.39 , pp. 1105-1116
    • Sinapah, S.1    Wu, S.2    Chen, Y.3    Pettersson, B.M.F.4    Gopalan, V.5    Kirsebom, L.A.6
  • 67
    • 0034896788 scopus 로고    scopus 로고
    • Function and subnuclear distribution of Rpp21, a protein subunit of the human ribonucleoprotein ribonuclease P
    • DOI 10.1017/S1355838201010469
    • Jarrous N.; Reiner R.; Wesolowski D.; Mann H.; Guerrier-Takada C.; and Altman S. Function and subnuclear distribution of Rpp21, a protein subunit of the human ribonucleoprotein ribonuclease P RNA 7 2001 1153 1164 (Pubitemid 32726913)
    • (2001) RNA , vol.7 , Issue.8 , pp. 1153-1164
    • Jarrous, N.1    Reiner, R.2    Wesolowski, D.3    Mann, H.4    Guerrier-Takada, C.5    Altman, S.6
  • 68
    • 0035838382 scopus 로고    scopus 로고
    • Current topics in RNA-protein recognition: Control of specificity and biological function through induced fit and conformational capture
    • DOI 10.1021/bi010680y
    • Leulliot N.; and Varani G. Current topics in RNA-protein recognition: control of specificity and biological function through induced fit and conformational capture Biochemistry 40 2001 7947 7956 (Pubitemid 32641191)
    • (2001) Biochemistry , vol.40 , Issue.27 , pp. 7947-7956
    • Leulliot, N.1    Varani, G.2
  • 69
    • 47649126376 scopus 로고    scopus 로고
    • Cooperativity in macromolecular assembly
    • DOI 10.1038/nchembio.102, PII NCHEMBIO102
    • Williamson J.R. Cooperativity in macromolecular assembly Nat. Chem. Biol. 4 2008 458 465 (Pubitemid 352019762)
    • (2008) Nature Chemical Biology , vol.4 , Issue.8 , pp. 458-465
    • Williamson, J.R.1
  • 70
    • 77955059323 scopus 로고    scopus 로고
    • Heterodimerization of the human RNase P/MRP subunits Rpp20 and Rpp25 is a prerequisite for interaction with the P3 arm of RNase MRP RNA
    • Hands-Taylor K.L.; Martino L.; Tata R.; Babon J.J.; Bui T.T.; and Drake A.F. Heterodimerization of the human RNase P/MRP subunits Rpp20 and Rpp25 is a prerequisite for interaction with the P3 arm of RNase MRP RNA Nucleic Acids Res. 38 2010 4052 4066
    • (2010) Nucleic Acids Res. , vol.38 , pp. 4052-4066
    • Hands-Taylor, K.L.1    Martino, L.2    Tata, R.3    Babon, J.J.4    Bui, T.T.5    Drake, A.F.6
  • 71
    • 77149172542 scopus 로고    scopus 로고
    • Eukaryotic ribonucleases P/MRP: The crystal structure of the P3 domain
    • Perederina A.; Esakova O.; Quan C.; Khanova E.; and Krasilnikov A.S. Eukaryotic ribonucleases P/MRP: the crystal structure of the P3 domain EMBO J. 29 2010 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
  • 72
    • 55249084867 scopus 로고    scopus 로고
    • Concurrent nucleation of 16S folding and induced fit in 30S ribosome assembly
    • Adilakshmi T.; Bellur D.L.; and Woodson S.A. Concurrent nucleation of 16S folding and induced fit in 30S ribosome assembly Nature 455 2008 1268 1272
    • (2008) Nature , vol.455 , pp. 1268-1272
    • Adilakshmi, T.1    Bellur, D.L.2    Woodson, S.A.3
  • 73
  • 74
    • 0037089548 scopus 로고    scopus 로고
    • A modified pBluescript-based vector for facile cloning and transcription of RNAs
    • DOI 10.1006/abio.2001.5567
    • Tsai H.Y.; Lai L.B.; and Gopalan V. A modified pBluescript-based vector for facile cloning and transcription of RNAs Anal. Biochem. 303 2002 214 217 (Pubitemid 34407588)
    • (2002) Analytical Biochemistry , vol.303 , Issue.2 , pp. 214-217
    • Tsai, H.-Y.1    Lai, L.B.2    Gopalan, V.3
  • 76
    • 4644259437 scopus 로고    scopus 로고
    • Using NMRView to visualize and analyze the NMR spectra of macromolecules
    • Johnson B.A. Using NMRView to visualize and analyze the NMR spectra of macromolecules Methods Mol. Biol. 278 2004 313 352
    • (2004) Methods Mol. Biol. , vol.278 , pp. 313-352
    • Johnson, B.A.1


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