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Volumn 10, Issue 9, 2004, Pages 1423-1432

Crystal structure of archaeal ribonuclease P protein Ph1771p from Pyrococcus horikoshii OT3: An archaeal homolog of eukaryotic ribonuclease P protein Rpp29

Author keywords

Archaea; Pyrococcus horikoshii; RNA binding protein; RNase P; X ray crystallography

Indexed keywords

ENDONUCLEASE; PROTEIN L21E; RIBONUCLEASE P; RIBOSOME PROTEIN; RNA BINDING PROTEIN; SULFATE; TRANSFER RNA; UNCLASSIFIED DRUG;

EID: 4344638194     PISSN: 13558382     EISSN: None     Source Type: Journal    
DOI: 10.1261/rna.7560904     Document Type: Article
Times cited : (40)

References (43)
  • 1
    • 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. 2001. Characterization of RNase P holoenzymes from Methanococcus jannaschii and Methanothermobacter thermoautotrophicus. Biol. Chem. 382: 1171-1177.
    • (2001) Biol. Chem. , vol.382 , pp. 1171-1177
    • Andrews, A.J.1    Hall, T.A.2    Brown, J.W.3
  • 2
    • 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. 2000. The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution. Science 289: 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
  • 3
    • 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. 1989. Identification and characterization of an RNA molecule that copurifies with RNase P activity from HeLa cells. Genes & Dev. 3: 488-499.
    • (1989) Genes & Dev. , vol.3 , pp. 488-499
    • Bartkiewicz, M.1    Gold, H.2    Altman, S.3
  • 6
    • 0035876146 scopus 로고    scopus 로고
    • Crystal structure of a heptameric Sm-like protein complex from archaea: Implications for the structure and evolution of snRNPs
    • Collins, B.M., Harrop, S.J., Kornfeld, G.D., Dawes, I.W., Curmi, P.M.G., and Mabbutt, B.C. 2001. Crystal structure of a heptameric Sm-like protein complex from archaea: Implications for the structure and evolution of snRNPs. J. Mol. Biol. 309: 915-923.
    • (2001) J. Mol. Biol. , vol.309 , pp. 915-923
    • Collins, B.M.1    Harrop, S.J.2    Kornfeld, G.D.3    Dawes, I.W.4    Curmi, P.M.G.5    Mabbutt, B.C.6
  • 7
    • 0025357508 scopus 로고
    • Characterization of ribonuclease P from the archaebacterium Sulfolobus solfataricus
    • Darr, S.C., Pace, B., and Pace, N.R. 1990. Characterization of ribonuclease P from the archaebacterium Sulfolobus solfataricus. J. Biol. Chem. 265: 12927-12932.
    • (1990) J. Biol. Chem. , vol.265 , pp. 12927-12932
    • Darr, S.C.1    Pace, B.2    Pace, N.R.3
  • 8
    • 0031711821 scopus 로고    scopus 로고
    • Ribonuclease P: Unity and diversity in a tRNA processing ribozyme
    • Frank, D.N. and Pace, N.R. 1998. Ribonuclease P: Unity and diversity in a tRNA processing ribozyme. Annu. Rev. Biochem. 67: 153-180.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 153-180
    • Frank, D.N.1    Pace, N.R.2
  • 10
    • 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
  • 11
    • 4344684743 scopus 로고    scopus 로고
    • Interactions between RNase P protein subunits in Archaea
    • in press
    • Hall, T.A. and Brown, J.W. 2004. Interactions between RNase P protein subunits in Archaea. Archaea 1: (in press).
    • (2004) Archaea , vol.1
    • Hall, T.A.1    Brown, J.W.2
  • 12
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. and Sander, C. 1993. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233: 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 14
    • 0036210354 scopus 로고    scopus 로고
    • Human ribonuclease P: Subunits, function, and intranuclear localization
    • Jarrous, N. 2002. Human ribonuclease P: Subunits, function, and intranuclear localization. RNA 8: 1-7.
    • (2002) RNA , vol.8 , pp. 1-7
    • Jarrous, N.1
  • 15
    • 0035970014 scopus 로고    scopus 로고
    • Protein-protein interactions with subunits of human nuclear RNase P
    • Jiang, T. and Altman, S. 2001. Protein-protein interactions with subunits of human nuclear RNase P. Proc. Natl. Acad. Sci. 98: 920-925.
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 920-925
    • Jiang, T.1    Altman, S.2
  • 16
    • 0034960193 scopus 로고    scopus 로고
    • Protein-RNA interactions in the subunits of human nuclear RNase P
    • Jiang, T., Guerrier-Takada, C, and Altman, S. 2001. Protein-RNA interactions in the subunits of human nuclear RNase P. RNA 7: 937-941.
    • (2001) RNA , vol.7 , pp. 937-941
    • Jiang, T.1    Guerrier-Takada, C.2    Altman, S.3
  • 17
    • 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 Kjeldgaad, M. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47: 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaad, M.4
  • 18
    • 0033524941 scopus 로고    scopus 로고
    • Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs
    • Kambach, C., Walke, S., Young, R., Avis, J.M., de la Fortelle, E., Raker, V.A., Luhrmann, R., Li, J., and Nagai, K. 1999. Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs. Cell 96: 375-387.
    • (1999) Cell , vol.96 , pp. 375-387
    • Kambach, C.1    Walke, S.2    Young, R.3    Avis, J.M.4    De La Fortelle, E.5    Raker, V.A.6    Luhrmann, R.7    Li, J.8    Nagai, K.9
  • 21
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24: 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 22
    • 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. 1993. PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26: 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 23
    • 0345359925 scopus 로고    scopus 로고
    • Structure and nucleic-acid binding of the Drosophila Argonaute 2 PAZ domain
    • Lingel, A., Simon, B., Izaurralde, E., and Sattler, M. 2003. Structure and nucleic-acid binding of the Drosophila Argonaute 2 PAZ domain. Nature 426: 465-469.
    • (2003) Nature , vol.426 , pp. 465-469
    • Lingel, A.1    Simon, B.2    Izaurralde, E.3    Sattler, M.4
  • 24
    • 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. 2003. Eukaryotic RNase P: Role of RNA and protein subunits of a primordial catalytic ribonucleoprotein in RNA-based catalysis. Mol. Cell 12: 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
  • 25
    • 0028057108 scopus 로고
    • Raster3D version 2.0, a program for photorealistic molecular graphics
    • Merrit, E.A. and Murphy, M.E.P. 1994. Raster3D version 2.0, a program for photorealistic molecular graphics. Acta Crystallogr. D50: 869-873.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 869-873
    • Merrit, E.A.1    Murphy, M.E.P.2
  • 26
    • 0035826794 scopus 로고    scopus 로고
    • The crystal structure of a heptameric archaeal Sm protein: Implications for the eukaryotic snRNP core
    • Mura, C., Cascio, D., Sawaya, M.R., and Eisenberg, D.S. 2001. The crystal structure of a heptameric archaeal Sm protein: Implications for the eukaryotic snRNP core. Proc. Natl. Acad. Sci. 98: 5532-5537.
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 5532-5537
    • Mura, C.1    Cascio, D.2    Sawaya, M.R.3    Eisenberg, D.S.4
  • 27
    • 0027479161 scopus 로고
    • OB (oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences
    • Murzin, A.G. 1993. OB (oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences. EMBO J. 12: 861-867.
    • (1993) EMBO J. , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 28
    • 0028961335 scopus 로고
    • SCOP: A structural classification of protein database for the investigation of sequences and structures
    • Murzin, A.G., Brenner, S.E., Hubbard, T., and Chothia, C. 1995. SCOP: A structural classification of protein database for the investigation of sequences and structures. J. Mol. Biol. 247: 536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 29
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K., and Honig, B. 1991. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11: 281-296.
    • (1991) Proteins Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 30
    • 0025992792 scopus 로고
    • The RNA component of RNase P from the archaebacterium Haloferax volcanii
    • Nieuwlandt, D.T., Haas, E.S., and Daniels, C.J. 1991. The RNA component of RNase P from the archaebacterium Haloferax volcanii. J. Biol. Chem. 266: 5689-5695.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5689-5695
    • Nieuwlandt, D.T.1    Haas, E.S.2    Daniels, C.J.3
  • 31
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. 1997. Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276: 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 32
    • 0028962136 scopus 로고
    • Evolutionary perspective on the structure and function of ribonuclease P, a ribozyme
    • Pace, N.R. and Brown, J.W. 1995. Evolutionary perspective on the structure and function of ribonuclease P, a ribozyme. J. Bacteriol. 177: 1919-1928.
    • (1995) J. Bacteriol. , vol.177 , pp. 1919-1928
    • Pace, N.R.1    Brown, J.W.2
  • 34
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis, A., Morris, R., and Lamzin, V.S. 1999. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol 6: 458-463.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 35
    • 0036645689 scopus 로고    scopus 로고
    • Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: A bacterial Sm-like protein
    • Schumacher, M.A., Pearson, R.F., Moller, T., Valentin-Hansen, P., and Brennan, R.G. 2002. Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: A bacterial Sm-like protein. EMBO J. 21: 3546-3556.
    • (2002) EMBO J. , vol.21 , pp. 3546-3556
    • Schumacher, M.A.1    Pearson, R.F.2    Moller, T.3    Valentin-Hansen, P.4    Brennan, R.G.5
  • 36
    • 0344823672 scopus 로고    scopus 로고
    • NMR structure of an archaeal homologue of ribonuclease P protein Rpp29
    • Sidote, D.J. and Huffman, D.W. 2003. NMR structure of an archaeal homologue of ribonuclease P protein Rpp29. Biochemistry 42: 13541-13550.
    • (2003) Biochemistry , vol.42 , pp. 13541-13550
    • Sidote, D.J.1    Huffman, D.W.2
  • 37
    • 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. 2000. The structure of ribonuclease P protein from Staphylococcus aureus reveals a unique binding site for single-stranded RNA. J. Mol. Biol. 295: 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
  • 38
    • 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. 1998. Ribonuclease P protein structure: Evolutionary origins in the translational apparatus. Science 280: 752-755.
    • (1998) Science , vol.280 , pp. 752-755
    • Stams, T.1    Niranjanakumari, S.2    Fierke, C.A.3    Christianson, D.W.4
  • 40
    • 2942627587 scopus 로고    scopus 로고
    • Crystal structure of the ribonuclease P protein Ph1877p from hyperthermophilic archaeon Pyrococcus horikoshii OT3
    • Takagi, H., Watanabe, M., Kakuta, Y., Kamachi, R., Numata, T., Tanaka, I., and Kimura, M. 2004. Crystal structure of the ribonuclease P protein Ph1877p from hyperthermophilic archaeon Pyrococcus horikoshii OT3. Biochem. Biophys. Res. Commun. 319: 787-794.
    • (2004) Biochem. Biophys. Res. Commun. , vol.319 , pp. 787-794
    • Takagi, H.1    Watanabe, M.2    Kakuta, Y.3    Kamachi, R.4    Numata, T.5    Tanaka, I.6    Kimura, M.7
  • 41
  • 42
    • 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. 2001. Eukaryotic ribonuclease P: Increased complexity to cope with the nuclear pre-tRNA pathway. J. Cell Physiol. 187: 11-20.
    • (2001) J. Cell Physiol. , vol.187 , pp. 11-20
    • Xiao, S.1    Houser-Scott, F.2    Engelke, D.R.3
  • 43
    • 0028817431 scopus 로고
    • Substrate recognition by human RNase P: Identification of small, model substrates for the enzyme
    • Yuan, Y. and Altman, S. 1995. Substrate recognition by human RNase P: Identification of small, model substrates for the enzyme. EMBO J. 14: 159-168.
    • (1995) EMBO J. , vol.14 , pp. 159-168
    • Yuan, Y.1    Altman, S.2


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