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Volumn 343, Issue 3, 2006, Pages 956-964

A fifth protein subunit Ph1496p elevates the optimum temperature for the ribonuclease P activity from Pyrococcus horikoshii OT3

Author keywords

Archaea; Pyrococcus horikoshii; Ribonuclease P; Ribosomal protein

Indexed keywords

L7AE PROTEIN; NUCLEOTIDE; PROTEIN SUBUNIT; RIBONUCLEASE P; RIBONUCLEOPROTEIN; RIBOSOME PROTEIN; UNCLASSIFIED DRUG; ARCHAEAL PROTEIN;

EID: 33646832404     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.02.192     Document Type: Article
Times cited : (61)

References (42)
  • 1
    • 0031711821 scopus 로고    scopus 로고
    • Ribonuclase P: unity and diversity in tRNA processing enzyme
    • Frank D.N., and Pace N.R. Ribonuclase P: unity and diversity in tRNA processing enzyme. Annu. Rev. Biochem. 67 (1998) 153-180
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 153-180
    • Frank, D.N.1    Pace, N.R.2
  • 2
    • 0003120548 scopus 로고    scopus 로고
    • Ribonuclase P
    • Gesteland R.F., Cech T., and Atkins J.F. (Eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Altman S., and Kirsebom L. Ribonuclase P. In: Gesteland R.F., Cech T., and Atkins J.F. (Eds). The RNA World (1999), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York 351-380
    • (1999) The RNA World , pp. 351-380
    • Altman, S.1    Kirsebom, L.2
  • 3
    • 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
    • (1983) Cell , vol.35 , pp. 849-857
    • Guerrier-Takada, C.1    Gardiner, K.2    Marsh, T.3    Pace, N.4    Altman, S.5
  • 4
    • 0024654339 scopus 로고
    • Identification and characterization of an RNA molecule that copurifies with RNase P activity from HeLa cells
    • Bartkiewicz M., Gold H., and Altman S. Identification and characterization of an RNA molecule that copurifies with RNase P activity from HeLa cells. Genes Dev. 3 (1989) 488-499
    • (1989) Genes Dev. , vol.3 , pp. 488-499
    • Bartkiewicz, M.1    Gold, H.2    Altman, S.3
  • 5
    • 0028817431 scopus 로고
    • Substrate recognition by human RNase P: identification of small, model substrates for the enzyme
    • Yuan Y., and Altman S. Substrate recognition by human RNase P: identification of small, model substrates for the enzyme. EMBO J. 14 (1995) 159-168
    • (1995) EMBO J. , vol.14 , pp. 159-168
    • Yuan, Y.1    Altman, S.2
  • 6
    • 0035127579 scopus 로고    scopus 로고
    • Eukaryotic ribonuclease P: increased complexity to cope with the nuclear pre-tRNA pathway
    • Xiao S., Houser-Scott F., and Engelke D.R. Eukaryotic ribonuclease P: increased complexity to cope with the nuclear pre-tRNA pathway. J. Cell Physiol. 187 (2001) 11-20
    • (2001) J. Cell Physiol. , vol.187 , pp. 11-20
    • Xiao, S.1    Houser-Scott, F.2    Engelke, D.R.3
  • 7
    • 0025357508 scopus 로고
    • Characterization of ribonuclease P from the archaebacterium Sulfolobus solfataricus
    • Darr S.C., Pace B., and Pace N.R. Characterization of ribonuclease P from the archaebacterium Sulfolobus solfataricus. J. Biol. Chem. 265 (1990) 12927-12932
    • (1990) J. Biol. Chem. , vol.265 , pp. 12927-12932
    • Darr, S.C.1    Pace, B.2    Pace, N.R.3
  • 8
    • 0025992792 scopus 로고
    • The RNA component of RNase P from the archaebacterium Haloferax volcanii
    • Nieuwlandt D.T., Haas E.S., and Daniels C.J. The RNA component of RNase P from the archaebacterium Haloferax volcanii. J. Biol. Chem. 266 (1991) 5689-5695
    • (1991) J. Biol. Chem. , vol.266 , pp. 5689-5695
    • Nieuwlandt, D.T.1    Haas, E.S.2    Daniels, C.J.3
  • 9
    • 0034826649 scopus 로고    scopus 로고
    • Characterization of RNase P holoenzymes from Methanococcus jannaschii and Methanothermobacter thermoautotrophicus
    • Andrews A.J., Hall T.A., and Brown J.W. Characterization of RNase P holoenzymes from Methanococcus jannaschii and Methanothermobacter thermoautotrophicus. Biol. Chem. 382 (2001) 1171-1177
    • (2001) Biol. Chem. , vol.382 , pp. 1171-1177
    • Andrews, A.J.1    Hall, T.A.2    Brown, J.W.3
  • 11
    • 0347763706 scopus 로고    scopus 로고
    • Roles of protein subunits in RNA-protein complexes: lessons from ribonuclease P
    • Hsieh J., Andrews A.J., and Fierke C.A. Roles of protein subunits in RNA-protein complexes: lessons from ribonuclease P. Biopolymers 73 (2004) 79-89
    • (2004) Biopolymers , vol.73 , pp. 79-89
    • Hsieh, J.1    Andrews, A.J.2    Fierke, C.A.3
  • 12
    • 0029286551 scopus 로고
    • Identification of phosphates involved in catalysis by the ribozyme RNase P RNA
    • Harris M.E., and Pace N.R. Identification of phosphates involved in catalysis by the ribozyme RNase P RNA. RNA 1 (1995) 210-218
    • (1995) RNA , vol.1 , pp. 210-218
    • Harris, M.E.1    Pace, N.R.2
  • 13
    • 0031827292 scopus 로고    scopus 로고
    • Identification by modification-interference of purine N-7 and ribose 2′-OH groups critical for catalysis by bacterial ribonuclease P
    • Kazantsev A.V., and Pace N.R. Identification by modification-interference of purine N-7 and ribose 2′-OH groups critical for catalysis by bacterial ribonuclease P. RNA 4 (1998) 937-947
    • (1998) RNA , vol.4 , pp. 937-947
    • Kazantsev, A.V.1    Pace, N.R.2
  • 14
    • 0034002685 scopus 로고    scopus 로고
    • Helix P4 is a divalent metal ion briding site in the conserved core of the ribonuclease P ribozyme
    • Christian E., Kaye N.M., and Harris M.E. Helix P4 is a divalent metal ion briding site in the conserved core of the ribonuclease P ribozyme. RNA 6 (2000) 511-519
    • (2000) RNA , vol.6 , pp. 511-519
    • Christian, E.1    Kaye, N.M.2    Harris, M.E.3
  • 15
    • 0036071392 scopus 로고    scopus 로고
    • Specific phosphorothioate substitutions probe the active site of Bacillus subtilis ribonuclease P
    • Crary S.M., Curz J.C., and Fierke C.A. Specific phosphorothioate substitutions probe the active site of Bacillus subtilis ribonuclease P. RNA 8 (2002) 933-947
    • (2002) RNA , vol.8 , pp. 933-947
    • Crary, S.M.1    Curz, J.C.2    Fierke, C.A.3
  • 16
    • 0038475910 scopus 로고    scopus 로고
    • Recognition of the 5′ leader of pre-tRNA substrates by the active site of ribonuclease P
    • 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
    • (2003) RNA , vol.9 , pp. 734-745
    • Zahler, N.H.1    Christian, E.L.2    Harris, M.E.3
  • 17
    • 27144527101 scopus 로고    scopus 로고
    • Protein activation of a ribozyme: the role of bacterial RNase P protein
    • Buck A.H., Dalby A.B., Poole A.W., Kazantsev A.V., and Pace N.R. Protein activation of a ribozyme: the role of bacterial RNase P protein. EMBO J. 24 (2005) 3360-3368
    • (2005) EMBO J. , vol.24 , pp. 3360-3368
    • Buck, A.H.1    Dalby, A.B.2    Poole, A.W.3    Kazantsev, A.V.4    Pace, N.R.5
  • 18
    • 0032076249 scopus 로고    scopus 로고
    • Ribonuclease P protein structure: evolutionary origins in the translational apparatus
    • Stams T., Niranjanakumari S., Fierke C.A., and Christianson D.W. Ribonuclease P protein structure: evolutionary origins in the translational apparatus. Science 280 (1998) 752-755
    • (1998) Science , vol.280 , pp. 752-755
    • Stams, T.1    Niranjanakumari, S.2    Fierke, C.A.3    Christianson, D.W.4
  • 19
    • 0034614360 scopus 로고    scopus 로고
    • The structure of ribonuclease P protein from Staphylococcus aureus reveals a unique binding site for single-stranded RNA
    • Spitzfaden C., Nicholson N., Jones J.J., Guth S., Lehr R., Prescott C.D., Hegg L.A., and Eggleston D.S. The structure of ribonuclease P protein from Staphylococcus aureus reveals a unique binding site for single-stranded RNA. J. Mol. Biol. 295 (2000) 105-115
    • (2000) J. Mol. Biol. , vol.295 , pp. 105-115
    • Spitzfaden, C.1    Nicholson, N.2    Jones, J.J.3    Guth, S.4    Lehr, R.5    Prescott, C.D.6    Hegg, L.A.7    Eggleston, D.S.8
  • 21
    • 0037434709 scopus 로고    scopus 로고
    • Crystal structure of the specificity domain of ribonuclease P
    • Krasilnikov A.S., Yang T., Pan T., and Mondragon A. Crystal structure of the specificity domain of ribonuclease P. Nature 421 (2003) 760-764
    • (2003) Nature , vol.421 , pp. 760-764
    • Krasilnikov, A.S.1    Yang, T.2    Pan, T.3    Mondragon, A.4
  • 22
    • 6044275739 scopus 로고    scopus 로고
    • Basis for structural diversity in homologous RNAs
    • Krasilnikov A.S., Xiao Y., Pan T., and Mondragon A. Basis for structural diversity in homologous RNAs. Science 306 (2004) 104-107
    • (2004) Science , vol.306 , pp. 104-107
    • Krasilnikov, A.S.1    Xiao, Y.2    Pan, T.3    Mondragon, A.4
  • 26
    • 0242266622 scopus 로고    scopus 로고
    • Eukaryotic RNase P: role of RNA and protein subunits of a primordial catalytic ribonucleoprotein in RNA-based catalysis
    • Mann H., Ben-Asouli Y., Schein A., Moussa S., and Jarrous N. Eukaryotic RNase P: role of RNA and protein subunits of a primordial catalytic ribonucleoprotein in RNA-based catalysis. Mol. Cell 12 (2003) 925-935
    • (2003) Mol. Cell , vol.12 , pp. 925-935
    • Mann, H.1    Ben-Asouli, Y.2    Schein, A.3    Moussa, S.4    Jarrous, N.5
  • 28
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • Ban N., Nissen P., Hansen J., Moore P.B., and Steitz T.A. The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution. Science 289 (2000) 905-920
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 29
    • 0030614558 scopus 로고    scopus 로고
    • Characterization of two scleroderma autoimmune antigens that copurify with human ribonuclease P
    • Eder P.S., Kekuda R., Stolc V., and Altman S. Characterization of two scleroderma autoimmune antigens that copurify with human ribonuclease P. Proc. Natl. Acad. Sci. USA 94 (1997) 1101-1106
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1101-1106
    • Eder, P.S.1    Kekuda, R.2    Stolc, V.3    Altman, S.4
  • 30
    • 0035196322 scopus 로고    scopus 로고
    • the structure of the archaebacterial ribosomal protein S7 and its possible interaction with 16S rRNA
    • Hosaka H., Yao M., Kimura M., and Tanaka I. the structure of the archaebacterial ribosomal protein S7 and its possible interaction with 16S rRNA. J. Biochem. 130 (2001) 695-701
    • (2001) J. Biochem. , vol.130 , pp. 695-701
    • Hosaka, H.1    Yao, M.2    Kimura, M.3    Tanaka, I.4
  • 31
    • 0024241761 scopus 로고
    • Structural analysis of RNA using chemical and enzymatic probing monitored by primer extension
    • Stern S., Moazed D., and Noller H.F. Structural analysis of RNA using chemical and enzymatic probing monitored by primer extension. Methods Enzymol. 164 (1988) 481-489
    • (1988) Methods Enzymol. , vol.164 , pp. 481-489
    • Stern, S.1    Moazed, D.2    Noller, H.F.3
  • 32
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 34
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47 (1991) 110-119
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 35
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26 (1993) 283-291
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 36
    • 0034509631 scopus 로고    scopus 로고
    • Crystal structure of the splicesomal 15.5 kDa protein bound to a U4 snRNA fragment
    • Vidovic I., Nottrott S., Hartmuth K., Luhrmann R., and Ficner R. Crystal structure of the splicesomal 15.5 kDa protein bound to a U4 snRNA fragment. Mol. Cell 6 (2000) 1331-1342
    • (2000) Mol. Cell , vol.6 , pp. 1331-1342
    • Vidovic, I.1    Nottrott, S.2    Hartmuth, K.3    Luhrmann, R.4    Ficner, R.5
  • 37
    • 0035423087 scopus 로고    scopus 로고
    • The kink-turn: a new RNA secondary structure motif
    • Klein D.J., Schmeing T.M., Moore P.B., and Steitz T.A. The kink-turn: a new RNA secondary structure motif. EMBO J. 20 (2001) 4214-4221
    • (2001) EMBO J. , vol.20 , pp. 4214-4221
    • Klein, D.J.1    Schmeing, T.M.2    Moore, P.B.3    Steitz, T.A.4
  • 38
    • 0037324527 scopus 로고    scopus 로고
    • Binding of L7Ae protein to the K-turn of archaeal snoRNAs: a shared RNA binding motif for C/D and H/ACA box snoRNAs in archaea
    • Rozhdestvensky T.S., Tang T.H., Tchirkova I.V., Brosius J., Bachellerie J.-P., and Huttenhofer A. Binding of L7Ae protein to the K-turn of archaeal snoRNAs: a shared RNA binding motif for C/D and H/ACA box snoRNAs in archaea. Nucleic Acids Res. 31 (2003) 869-877
    • (2003) Nucleic Acids Res. , vol.31 , pp. 869-877
    • Rozhdestvensky, T.S.1    Tang, T.H.2    Tchirkova, I.V.3    Brosius, J.4    Bachellerie, J.-P.5    Huttenhofer, A.6
  • 39
    • 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
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 40
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bounded and geometrical features
    • Kabsch W., and Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bounded and geometrical features. Biopolymers 22 (1983) 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 41
    • 0026244229 scopus 로고
    • MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24 (1991) 946-950
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 42
    • 0028057108 scopus 로고
    • Raster3D version 2.0, a program for photorealistic molecular graphics
    • Merrit E.A., and Murphy M.E.P. Raster3D version 2.0, a program for photorealistic molecular graphics. Acta Crystallogr. D 50 (1994) 860-873
    • (1994) Acta Crystallogr. D , vol.50 , pp. 860-873
    • Merrit, E.A.1    Murphy, M.E.P.2


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