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Volumn 36, Issue 18, 2008, Pages 5800-5811

The putative RNase P motif in the DEAD box helicase Hera is dispensable for efficient interaction with RNA and helicase activity

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BACTERIAL RNA; DEAD BOX PROTEIN; RIBONUCLEASE P; RIBOSOME RNA; RNA 23S;

EID: 54549123661     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkn581     Document Type: Article
Times cited : (35)

References (49)
  • 1
    • 33344473656 scopus 로고    scopus 로고
    • The DEAD-box protein family of RNA helicases
    • Cordin,O., Banroques,J., Tanner,N.K. and Linder,P. (2006) The DEAD-box protein family of RNA helicases. Gene, 367, 17-37.
    • (2006) Gene , vol.367 , pp. 17-37
    • Cordin, O.1    Banroques, J.2    Tanner, N.K.3    Linder, P.4
  • 2
    • 0027182114 scopus 로고
    • Helicases: Amino acid sequence comparisons and structure-function relationships
    • Gorbalenya,A.E. and Koonin,E.V. (1993) Helicases: Amino acid sequence comparisons and structure-function relationships. Curr. Opin. Struct. Biol., 3, 419-429.
    • (1993) Curr. Opin. Struct. Biol , vol.3 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 3
    • 0036927393 scopus 로고    scopus 로고
    • The carboxy-terminal domain of the DExDH protein YxiN is sufficient to confer specificity for 23S rRNA
    • Kossen,K., Karginov,F.V. and Uhlenbeck,O.C. (2002) The carboxy-terminal domain of the DExDH protein YxiN is sufficient to confer specificity for 23S rRNA. J. Mol. Biol., 324, 625-636.
    • (2002) J. Mol. Biol , vol.324 , pp. 625-636
    • Kossen, K.1    Karginov, F.V.2    Uhlenbeck, O.C.3
  • 4
    • 27444442034 scopus 로고    scopus 로고
    • YxiN is a modular protein combining a DEx(D/H) core and a specific RNA-binding domain
    • Karginov,F.V., Caruthers,J.M., Hu,Y., McKay,D.B. and Uhlenbeck,O.C. (2005) YxiN is a modular protein combining a DEx(D/H) core and a specific RNA-binding domain. J. Biol. Chem., 280, 35499-35505.
    • (2005) J. Biol. Chem , vol.280 , pp. 35499-35505
    • Karginov, F.V.1    Caruthers, J.M.2    Hu, Y.3    McKay, D.B.4    Uhlenbeck, O.C.5
  • 5
    • 33646883060 scopus 로고    scopus 로고
    • The domain of the Bacillus subtilis DEAD-box helicase YxiN that is responsible for specific binding of 23S rRNA has an RNA recognition motif fold
    • Wang,S., Hu,Y., Overgaard,M.T., Karginov,F.V., Uhlenbeck,O.C. and McKay,D.B. (2006) The domain of the Bacillus subtilis DEAD-box helicase YxiN that is responsible for specific binding of 23S rRNA has an RNA recognition motif fold. RNA.
    • (2006) RNA
    • Wang, S.1    Hu, Y.2    Overgaard, M.T.3    Karginov, F.V.4    Uhlenbeck, O.C.5    McKay, D.B.6
  • 6
    • 0033214564 scopus 로고    scopus 로고
    • Interaction of the Escherichia coli DEAD box protein DbpA with 23 S ribosomal RNA
    • Pugh,G.E., Nicol,S.M. and Fuller-Pace,F.V. (1999) Interaction of the Escherichia coli DEAD box protein DbpA with 23 S ribosomal RNA. J. Mol. Biol., 292, 771-778.
    • (1999) J. Mol. Biol , vol.292 , pp. 771-778
    • Pugh, G.E.1    Nicol, S.M.2    Fuller-Pace, F.V.3
  • 7
    • 37749022256 scopus 로고    scopus 로고
    • Function of the C-terminal domain of the DEAD-box protein Mss116p analyzed in vivo and in vitro
    • Mohr,G. and Del Campo,M. (2008) Function of the C-terminal domain of the DEAD-box protein Mss116p analyzed in vivo and in vitro. J. Mol. Biol. 375, 1344-1364.
    • (2008) J. Mol. Biol , vol.375 , pp. 1344-1364
    • Mohr, G.1    Del Campo, M.2
  • 8
    • 33845738802 scopus 로고    scopus 로고
    • Involvement of DEAD-box proteins in group I and group II intron splicing. Biochemical characterization of Mss116p, ATP hydrolysis-dependent and -independent mechanisms, and general RNA chaperone activity
    • Halls,C., Mohr,S., Del Campo,M., Yang,Q., Jankowsky,E. and Lambowitz,A.M. (2007) Involvement of DEAD-box proteins in group I and group II intron splicing. Biochemical characterization of Mss116p, ATP hydrolysis-dependent and -independent mechanisms, and general RNA chaperone activity. J. Mol. Biol., 365, 835-855.
    • (2007) J. Mol. Biol , vol.365 , pp. 835-855
    • Halls, C.1    Mohr, S.2    Del Campo, M.3    Yang, Q.4    Jankowsky, E.5    Lambowitz, A.M.6
  • 9
    • 33947362880 scopus 로고    scopus 로고
    • Probing the mechanisms of DEAD-box proteins as general RNA chaperones: The C-terminal domain of CYT-19 mediates general recognition of RNA
    • Grohman,J.K., Campo,M.D., Bhaskaran,H., Tijerina,P., Lambowitz,A.M. and Russell,R. (2007) Probing the mechanisms of DEAD-box proteins as general RNA chaperones: The C-terminal domain of CYT-19 mediates general recognition of RNA. Biochemistry, 46, 3013-3022.
    • (2007) Biochemistry , vol.46 , pp. 3013-3022
    • Grohman, J.K.1    Campo, M.D.2    Bhaskaran, H.3    Tijerina, P.4    Lambowitz, A.M.5    Russell, R.6
  • 10
    • 33644852160 scopus 로고    scopus 로고
    • A DEAD-box protein alone promotes group II intron splicing and reverse splicing by acting as an RNA chaperone
    • Mohr,S., Matsuura,M., Perlman,P.S. and Lambowitz,A.M. (2006) A DEAD-box protein alone promotes group II intron splicing and reverse splicing by acting as an RNA chaperone. Proc. Natl Acad. Sci. USA, 103, 3569-3574.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 3569-3574
    • Mohr, S.1    Matsuura, M.2    Perlman, P.S.3    Lambowitz, A.M.4
  • 11
    • 11844297811 scopus 로고    scopus 로고
    • The splicing of yeast mitochondrial group I and group II introns requires a DEAD-box protein with RNA chaperone function
    • Huang,H.R., Rowe,C.E., Mohr,S., Jiang,Y., Lambowitz,A.M. and Perlman,P.S. (2005) The splicing of yeast mitochondrial group I and group II introns requires a DEAD-box protein with RNA chaperone function. Proc. Natl Acad. Sci. USA, 102, 163-168.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 163-168
    • Huang, H.R.1    Rowe, C.E.2    Mohr, S.3    Jiang, Y.4    Lambowitz, A.M.5    Perlman, P.S.6
  • 12
    • 33750936780 scopus 로고    scopus 로고
    • Nonspecific binding to structured RNA and preferential unwinding of an exposed helix by the CYT-19 protein, a DEAD-box RNA chaperone
    • Tijerina,P., Bhaskaran,H. and Russell,R. (2006) Nonspecific binding to structured RNA and preferential unwinding of an exposed helix by the CYT-19 protein, a DEAD-box RNA chaperone. Proc. Natl Acad Sci. USA 103, 16698-16703.
    • (2006) Proc. Natl Acad Sci. USA , vol.103 , pp. 16698-16703
    • Tijerina, P.1    Bhaskaran, H.2    Russell, R.3
  • 13
    • 0037077127 scopus 로고    scopus 로고
    • A DEAD-box protein functions as an ATP-dependent RNA chaperone in group I intron splicing
    • Mohr,S., Stryker,J.M. and Lambowitz,A.M. (2002) A DEAD-box protein functions as an ATP-dependent RNA chaperone in group I intron splicing. Cell, 109, 769-779.
    • (2002) Cell , vol.109 , pp. 769-779
    • Mohr, S.1    Stryker, J.M.2    Lambowitz, A.M.3
  • 14
    • 0344129033 scopus 로고    scopus 로고
    • Hera from Thermus thermophilus: The first thermostable DEAD-box helicase with an RNase P protein motif
    • Morlang,S., Weglohner,W. and Franceschi,F. (1999) Hera from Thermus thermophilus: The first thermostable DEAD-box helicase with an RNase P protein motif. J. Mol. Biol., 294, 795-805.
    • (1999) J. Mol. Biol , vol.294 , pp. 795-805
    • Morlang, S.1    Weglohner, W.2    Franceschi, F.3
  • 15
    • 33746853440 scopus 로고    scopus 로고
    • Crystal structure and nucleotide binding of the Thermus thermophilus RNA helicase Hera N-terminal domain
    • Rudolph,M.G., Heissmann,R., Wittmann,J.G. and Klostermeier,D. (2006) Crystal structure and nucleotide binding of the Thermus thermophilus RNA helicase Hera N-terminal domain. J. Mol. Biol., 361, 731-743.
    • (2006) J. Mol. Biol , vol.361 , pp. 731-743
    • Rudolph, M.G.1    Heissmann, R.2    Wittmann, J.G.3    Klostermeier, D.4
  • 16
    • 0021013526 scopus 로고
    • The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme
    • Guerrier-Takada,C., Gardiner,K., Marsh,T., Pace,N. and Altman,S. (1983) The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme. Cell, 35, 849-857.
    • (1983) Cell , vol.35 , pp. 849-857
    • Guerrier-Takada, C.1    Gardiner, K.2    Marsh, T.3    Pace, N.4    Altman, S.5
  • 17
    • 0141450351 scopus 로고    scopus 로고
    • The enigma of ribonuclease P evolution
    • Hartmann,E. and Hartmann,R.K. (2003) The enigma of ribonuclease P evolution. Trends Genet., 19, 561-569.
    • (2003) Trends Genet , vol.19 , pp. 561-569
    • Hartmann, E.1    Hartmann, R.K.2
  • 18
    • 0026606958 scopus 로고
    • Ribonuclease P RNA and protein subunits from bacteria
    • Brown,J.W. and Pace,N.R. (1992) Ribonuclease P RNA and protein subunits from bacteria. Nucleic Acids Res., 20, 1451-1456.
    • (1992) Nucleic Acids Res , vol.20 , pp. 1451-1456
    • Brown, J.W.1    Pace, N.R.2
  • 19
    • 33645008830 scopus 로고    scopus 로고
    • Structural perspective on the activation of RNAse P RNA by protein
    • Buck,A.H., Kazantsev,A.V., Dalby,A.B. and Pace,N.R. (2005) Structural perspective on the activation of RNAse P RNA by protein. Nat. Struct. Mol. Biol., 12, 958-964.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 958-964
    • Buck, A.H.1    Kazantsev, A.V.2    Dalby, A.B.3    Pace, N.R.4
  • 20
    • 33947716757 scopus 로고    scopus 로고
    • Probing the architecture of the B. subtilis RNase P holoenzyme active site by cross-linking and affinity cleavage
    • Niranjanakumari,S., Day-Storms,J.J., Ahmed,M., Hsieh,J., Zahler,N.H., Venters,R.A. and Fierke,C.A. (2007) Probing the architecture of the B. subtilis RNase P holoenzyme active site by cross-linking and affinity cleavage. RNA, 13, 521-535.
    • (2007) RNA , vol.13 , pp. 521-535
    • Niranjanakumari, S.1    Day-Storms, J.J.2    Ahmed, M.3    Hsieh, J.4    Zahler, N.H.5    Venters, R.A.6    Fierke, C.A.7
  • 21
    • 38649106732 scopus 로고    scopus 로고
    • Cooperative binding of ATP and RNA induces a closed conformation in a DEAD box RNA helicase
    • Theissen,B., Karow,A.R., Kohler,J., Gubaev,A. and Klostermeier,D. (2008) Cooperative binding of ATP and RNA induces a closed conformation in a DEAD box RNA helicase. Proc. Natl Acad. Sci. USA, 105, 548-553.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 548-553
    • Theissen, B.1    Karow, A.R.2    Kohler, J.3    Gubaev, A.4    Klostermeier, D.5
  • 22
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier,F.W. (2005) Protein production by auto-induction in high density shaking cultures. Protein Expr. Purif., 41, 207-234.
    • (2005) Protein Expr. Purif , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 23
    • 33845270966 scopus 로고    scopus 로고
    • The precursor tRNA 3′-CCA interaction with Escherichia coli RNase P RNA is essential for catalysis by RNase P in vivo
    • Wegscheid,B. and Hartmann,R.K. (2006) The precursor tRNA 3′-CCA interaction with Escherichia coli RNase P RNA is essential for catalysis by RNase P in vivo. RNA, 12, 2135-2148.
    • (2006) RNA , vol.12 , pp. 2135-2148
    • Wegscheid, B.1    Hartmann, R.K.2
  • 24
    • 33845967782 scopus 로고    scopus 로고
    • Authentic interdomain communication in an RNA helicase reconstituted by expressed protein ligation of two helicase domains
    • Karow,A.R., Theissen,B. and Klostermeier,D. (2007) Authentic interdomain communication in an RNA helicase reconstituted by expressed protein ligation of two helicase domains. FEBS J., 274, 463-473.
    • (2007) FEBS J , vol.274 , pp. 463-473
    • Karow, A.R.1    Theissen, B.2    Klostermeier, D.3
  • 25
    • 0034674157 scopus 로고    scopus 로고
    • Differential role of the intermolecular base-pairs G292-C(75) and G293-C(74) in the reaction catalyzed by Escherichia coli RNase P RNA
    • Busch,S., Kirsebom,L.A., Notbohm,H. and Hartmann,R.K. (2000) Differential role of the intermolecular base-pairs G292-C(75) and G293-C(74) in the reaction catalyzed by Escherichia coli RNase P RNA. J. Mol. Biol., 299, 941-951.
    • (2000) J. Mol. Biol , vol.299 , pp. 941-951
    • Busch, S.1    Kirsebom, L.A.2    Notbohm, H.3    Hartmann, R.K.4
  • 26
    • 0032590013 scopus 로고    scopus 로고
    • Guanosine 2-NH2 groups of Escherichia coli RNase P RNA involved in intramolecular tertiary contacts and direct interactions with tRNA
    • Heide,C., Pfeiffer,T., Nolan,J.M. and Hartmann,R.K. (1999) Guanosine 2-NH2 groups of Escherichia coli RNase P RNA involved in intramolecular tertiary contacts and direct interactions with tRNA. RNA, 5, 102-116.
    • (1999) RNA , vol.5 , pp. 102-116
    • Heide, C.1    Pfeiffer, T.2    Nolan, J.M.3    Hartmann, R.K.4
  • 27
    • 2042536226 scopus 로고
    • Bergmeyer,H.U.Hrsg, Verlag Chemie, Weinheim, pp
    • Adam,H. (1962) In Bergmeyer,H.U.(Hrsg.), Methoden der Enzymatischen Analyse. Verlag Chemie, Weinheim, pp. 573-577.
    • (1962) Methoden der Enzymatischen Analyse , pp. 573-577
    • Adam, H.1
  • 28
    • 33847682952 scopus 로고
    • Correction of fluorescence spectra and measurement of fluorescence quantum efficiency
    • Parker,C.A. and Rees,W.T. (1960) Correction of fluorescence spectra and measurement of fluorescence quantum efficiency. Analyst, 85, 587-600.
    • (1960) Analyst , vol.85 , pp. 587-600
    • Parker, C.A.1    Rees, W.T.2
  • 29
    • 0001433022 scopus 로고    scopus 로고
    • Fluorescence quantum yields and their relation to lifetimes of rhodamine 6G and fluorescein in nine solvents: Improved absolute standards for quantum yields
    • Magde,D., Wong,R. and Seybold,P.G. (2002) Fluorescence quantum yields and their relation to lifetimes of rhodamine 6G and fluorescein in nine solvents: Improved absolute standards for quantum yields. Photochem. Photobiol., 75, 327-334.
    • (2002) Photochem. Photobiol , vol.75 , pp. 327-334
    • Magde, D.1    Wong, R.2    Seybold, P.G.3
  • 30
    • 27744599888 scopus 로고
    • Transfer mechanisms of electronic excitation
    • Forster,T. (1959) Transfer mechanisms of electronic excitation. Discuss. Faraday Soc., 27, 7-17.
    • (1959) Discuss. Faraday Soc , vol.27 , pp. 7-17
    • Forster, T.1
  • 31
    • 0035852638 scopus 로고    scopus 로고
    • Crystal structure of a DEAD box protein from the hyperthermophile Methanococcus jannaschii
    • Story,R.M., Li,H. and Abelson,J.N. (2001) Crystal structure of a DEAD box protein from the hyperthermophile Methanococcus jannaschii. Proc. Natl Acad. Sci. USA, 98, 1465-1470.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 1465-1470
    • Story, R.M.1    Li, H.2    Abelson, J.N.3
  • 32
    • 33646017369 scopus 로고    scopus 로고
    • Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa
    • Sengoku,T., Nureki,O., Nakamura,A., Kobayashi,S. and Yokoyama,S. (2006) Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa. Cell, 125, 287-300.
    • (2006) Cell , vol.125 , pp. 287-300
    • Sengoku, T.1    Nureki, O.2    Nakamura, A.3    Kobayashi, S.4    Yokoyama, S.5
  • 34
    • 33747182255 scopus 로고    scopus 로고
    • The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA
    • Bono,F., Ebert,J., Lorentzen,E. and Conti,E. (2006) The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA. Cell, 126, 713-725.
    • (2006) Cell , vol.126 , pp. 713-725
    • Bono, F.1    Ebert, J.2    Lorentzen, E.3    Conti, E.4
  • 35
    • 0033214805 scopus 로고    scopus 로고
    • Cloning and biochemical characterization of Bacillus subtilis YxiN, a DEAD protein specifically activated by 23S rRNA: Delineation of a novel sub-family of bacterial DEAD proteins
    • Kossen,K. and Uhlenbeck,O.C. (1999) Cloning and biochemical characterization of Bacillus subtilis YxiN, a DEAD protein specifically activated by 23S rRNA: Delineation of a novel sub-family of bacterial DEAD proteins. Nucleic Acids Res., 27, 3811-3820.
    • (1999) Nucleic Acids Res , vol.27 , pp. 3811-3820
    • Kossen, K.1    Uhlenbeck, O.C.2
  • 36
    • 0034635354 scopus 로고    scopus 로고
    • Mapping RNA-protein interactions in ribonuclease P from Escherichia coli using disulfide-linked EDTA-Fe
    • Biswas,R., Ledman,D.W., Fox,R.O., Altman,S. and Gopalan,V. (2000) Mapping RNA-protein interactions in ribonuclease P from Escherichia coli using disulfide-linked EDTA-Fe. J. Mol. Biol., 296, 19-31.
    • (2000) J. Mol. Biol , vol.296 , pp. 19-31
    • Biswas, R.1    Ledman, D.W.2    Fox, R.O.3    Altman, S.4    Gopalan, V.5
  • 37
    • 0036306006 scopus 로고    scopus 로고
    • Potential contact sites between the protein and RNA subunit in the Bacillus subtilis RNase P holoenzyme
    • Rox,C., Feltens,R., Pfeiffer,T. and Hartmann,R.K. (2002) Potential contact sites between the protein and RNA subunit in the Bacillus subtilis RNase P holoenzyme. J. Mol. Biol., 315, 551-560.
    • (2002) J. Mol. Biol , vol.315 , pp. 551-560
    • Rox, C.1    Feltens, R.2    Pfeiffer, T.3    Hartmann, R.K.4
  • 38
    • 0037462929 scopus 로고    scopus 로고
    • Molecular modeling of the three-dimensional structure of the bacterial RNase P holoenzyme
    • Tsai,H.Y., Masquida,B., Biswas,R., Westhof,E. and Gopalan,V. (2003) Molecular modeling of the three-dimensional structure of the bacterial RNase P holoenzyme. J. Mol. Biol., 325, 661-675.
    • (2003) J. Mol. Biol , vol.325 , pp. 661-675
    • Tsai, H.Y.1    Masquida, B.2    Biswas, R.3    Westhof, E.4    Gopalan, V.5
  • 39
    • 0025166185 scopus 로고
    • Complementation of an RNase P RNA (rnpB) gene deletion in Escherichia coli by homologous genes from distantly related eubacteria
    • Waugh,D.S. and Pace,N.R. (1990) Complementation of an RNase P RNA (rnpB) gene deletion in Escherichia coli by homologous genes from distantly related eubacteria. J. Bacteriol., 172, 6316-6322.
    • (1990) J. Bacteriol , vol.172 , pp. 6316-6322
    • Waugh, D.S.1    Pace, N.R.2
  • 40
    • 35448968985 scopus 로고    scopus 로고
    • Function of heterologous and truncated RNase P proteins in Bacillus subtilis
    • Gossringer,M. and Hartmann,R.K. (2007) Function of heterologous and truncated RNase P proteins in Bacillus subtilis. Mol. Microbiol., 66, 801-813.
    • (2007) Mol. Microbiol , vol.66 , pp. 801-813
    • Gossringer, M.1    Hartmann, R.K.2
  • 41
    • 38049073261 scopus 로고    scopus 로고
    • Structural basis of a ribozyme's thermostability: P1-L9 interdomain interaction in RNase P RNA
    • Marszalkowski,M., Willkomm,D.K. and Hartmann,R.K. (2008) Structural basis of a ribozyme's thermostability: P1-L9 interdomain interaction in RNase P RNA. RNA, 14, 127-133.
    • (2008) RNA , vol.14 , pp. 127-133
    • Marszalkowski, M.1    Willkomm, D.K.2    Hartmann, R.K.3
  • 42
    • 0028268090 scopus 로고
    • Kinetic and thermodynamic analysis of RNA-protein interactions in the RNase P holoenzyme from Escherichia coli
    • Talbot,S.J. and Altman,S. (1994) Kinetic and thermodynamic analysis of RNA-protein interactions in the RNase P holoenzyme from Escherichia coli. Biochemistry, 33, 1406-1411.
    • (1994) Biochemistry , vol.33 , pp. 1406-1411
    • Talbot, S.J.1    Altman, S.2
  • 43
    • 4644305092 scopus 로고    scopus 로고
    • Ionic interactions between PRNA and P protein in Bacillus subtilis RNase P characterized using a magnetocapture-based assay
    • Day-Storms,J.J., Niranjanakumari,S. and Fierke,C.A. (2004) Ionic interactions between PRNA and P protein in Bacillus subtilis RNase P characterized using a magnetocapture-based assay. RNA, 10, 1595-1608.
    • (2004) RNA , vol.10 , pp. 1595-1608
    • Day-Storms, J.J.1    Niranjanakumari, S.2    Fierke, C.A.3
  • 44
    • 34250621718 scopus 로고    scopus 로고
    • Cuzic,S. and Hartmann,R.K. (2007) A 2′-methyl or 2′-methylene group at G + 1 in precursor tRNA interferes with Mg2+ binding at the enzyme-substrate interface in E-S complexes of E. coh RNase P. Biol. Chem., 388, 717-726.
    • Cuzic,S. and Hartmann,R.K. (2007) A 2′-methyl or 2′-methylene group at G + 1 in precursor tRNA interferes with Mg2+ binding at the enzyme-substrate interface in E-S complexes of E. coh RNase P. Biol. Chem., 388, 717-726.
  • 46
    • 0036920388 scopus 로고    scopus 로고
    • Elucidation of structure-function relationships in the protein subunit of bacterial RNase P using a genetic complementation approach
    • Jovanovic,M., Sanchez,R., Altman,S. and Gopalan,V. (2002) Elucidation of structure-function relationships in the protein subunit of bacterial RNase P using a genetic complementation approach. Nucleic Acids Res. 30, 5065--5073.
    • (2002) Nucleic Acids Res , vol.30 , pp. 5065-5073
    • Jovanovic, M.1    Sanchez, R.2    Altman, S.3    Gopalan, V.4
  • 47
    • 0025950162 scopus 로고
    • Analysis of the gene encoding the RNA subunit of ribonuclease P from T. thermophilus HB8
    • Hartmann,R.K. and Erdmann,V.A. (1991) Analysis of the gene encoding the RNA subunit of ribonuclease P from T. thermophilus HB8. Nucleic Acids Res., 19, 5957-5964.
    • (1991) Nucleic Acids Res , vol.19 , pp. 5957-5964
    • Hartmann, R.K.1    Erdmann, V.A.2
  • 48
    • 36749064979 scopus 로고    scopus 로고
    • Folding of noncoding RNAs during transcription facilitated by pausing-induced nonnative structures
    • Wong,T.N., Sosnick,T.R. and Pan,T. (2007) Folding of noncoding RNAs during transcription facilitated by pausing-induced nonnative structures. Proc. Natl Acad. Sci. USA, 104, 17995-18000.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 17995-18000
    • Wong, T.N.1    Sosnick, T.R.2    Pan, T.3
  • 49
    • 0038625034 scopus 로고    scopus 로고
    • An unusual mechanism of bacterial gene expression revealed for the RNase P protein of Thermus strains
    • Feltens,R., Gossringer,M., Willkomm,D.K., Urlaub,H. and Hartmann,R.K. (2003) An unusual mechanism of bacterial gene expression revealed for the RNase P protein of Thermus strains. Proc. Natl Acad Sci. USA, 100, 5724-5729.
    • (2003) Proc. Natl Acad Sci. USA , vol.100 , pp. 5724-5729
    • Feltens, R.1    Gossringer, M.2    Willkomm, D.K.3    Urlaub, H.4    Hartmann, R.K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.