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Volumn 140, Issue 2, 2006, Pages 293-298

Characterization of the archaeal ribonuclease P proteins from Pyrococcus horikoshii OT3

Author keywords

Pre tRNA; Pyrococcus horokoshii; Ribonuclease P; Ribonuclease P proteins

Indexed keywords

ARCHAEAL PROTEIN; MAGNESIUM ION; PROTEIN PHOPOP5; PROTEIN PHORPP21; PROTEIN PHORPP29; PROTEIN PHORPP30; PROTEIN PHORPP38; RIBONUCLEASE P; RIBONUCLEOPROTEIN; RNA; UNCLASSIFIED DRUG;

EID: 33750377546     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvj144     Document Type: Article
Times cited : (24)

References (31)
  • 1
    • 0031711821 scopus 로고    scopus 로고
    • Ribonuclase P: Unity and diversity in tRNA processing enzyme
    • Frank, D.N. and Pace, N.R. (1998) Ribonuclase P: unity and diversity in tRNA processing enzyme. Annu. Rev. Biochem. 67, 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, NY
    • Altman, S. and Kirsebom, L. (1999) Ribonuclase P. In The RNA World (Gesteland, R.F., Cech, T., and Atkins, J.F., eds.) pp. 351-380, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • (1999) The RNA World , pp. 351-380
    • Altman, S.1    Kirsebom, L.2
  • 3
    • 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. (2004) Roles of protein subunits in RNA-protein complexes: lessons from ribonuclease P. Biopolymers 73, 79-89
    • (2004) Biopolymers , vol.73 , pp. 79-89
    • Hsieh, J.1    Andrews, A.J.2    Fierke, C.A.3
  • 4
    • 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
  • 5
    • 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
    • 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
  • 7
    • 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
  • 8
    • 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
  • 11
    • 24644469952 scopus 로고    scopus 로고
    • Crystal structure of a ribonuclease P protein Ph1601p from Pyrococcus horikoshii OT3: An archaeal homolog of human nuclear ribonuclease P protein Rpp21
    • Kakuta, Y., Ishimatsu, I., Numata, T., Tanaka, I., and Kimura, M. (2005) Crystal structure of a ribonuclease P protein Ph1601p from Pyrococcus horikoshii OT3: an archaeal homolog of human nuclear ribonuclease P protein Rpp21. Biochemistry 44, 12086-12093
    • (2005) Biochemistry , vol.44 , pp. 12086-12093
    • Kakuta, Y.1    Ishimatsu, I.2    Numata, T.3    Tanaka, I.4    Kimura, M.5
  • 12
    • 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
    • Numata, T., Ishimatsu, I., Kakuta, Y., Tanaka, I., and Kimura, M. (2004) Crystal structure of archaeal ribonuclease P protein Ph1771p from Pyrococcus horikoshii OT3: an archaeal homolog of eukaryotic ribonuclease P protein Rpp29. RNA 10, 1423-1432
    • (2004) RNA , vol.10 , pp. 1423-1432
    • Numata, T.1    Ishimatsu, I.2    Kakuta, Y.3    Tanaka, I.4    Kimura, M.5
  • 13
    • 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
  • 14
    • 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
    • Kawano, S., Nakashima, T., Kakuta, Y., Tanaka, I., and Kimura, M. (2006) 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, 583-591
    • (2006) J. Mol. Biol. , vol.357 , pp. 583-591
    • Kawano, S.1    Nakashima, T.2    Kakuta, Y.3    Tanaka, I.4    Kimura, M.5
  • 15
    • 22444431914 scopus 로고    scopus 로고
    • Protein-protein interactions in the subunits of ribonuclease P in hyperthermophilic archaeon Pyrococcus horikoshii OT3
    • Kifusa, M., Fukuhara, H., Hayashi, T., and Kimura, M. (2005) Protein-protein interactions in the subunits of ribonuclease P in hyperthermophilic archaeon Pyrococcus horikoshii OT3. Biosci. Biotechnol. Biochem. 69, 1209-1212
    • (2005) Biosci. Biotechnol. Biochem. , vol.69 , pp. 1209-1212
    • Kifusa, M.1    Fukuhara, H.2    Hayashi, T.3    Kimura, M.4
  • 16
    • 0029286551 scopus 로고
    • Identification of phosphates involved in catalysis by the ribozyme RNase P RNA
    • Harris, M.E. and Pace, N.R. (1995) Identification of phosphates involved in catalysis by the ribozyme RNase P RNA. RNA 1, 210-218
    • (1995) RNA , vol.1 , pp. 210-218
    • Harris, M.E.1    Pace, N.R.2
  • 17
    • 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. (1998) Identification by modification-interference of purine N-7 and ribose 2′-OH groups critical for catalysis by bacterial ribonuclease P. RNA 4, 937-947
    • (1998) RNA , vol.4 , pp. 937-947
    • Kazantsev, A.V.1    Pace, N.R.2
  • 18
    • 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. (2000) Helix P4 is a divalent metal ion briding site in the conserved core of the ribonuclease P ribozyme. RNA 6, 511-519
    • (2000) RNA , vol.6 , pp. 511-519
    • Christian, E.1    Kaye, N.M.2    Harris, M.E.3
  • 19
    • 0036071392 scopus 로고    scopus 로고
    • Specific phosphorothioate substitutions probe the active site of Bacillus subtilis ribobuclease P
    • Crary, S.M., Curz, J.C., and Fierke, C.A. (2002) Specific phosphorothioate substitutions probe the active site of Bacillus subtilis ribobuclease P. RNA 8, 933-947
    • (2002) RNA , vol.8 , pp. 933-947
    • Crary, S.M.1    Curz, J.C.2    Fierke, C.A.3
  • 20
    • 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. (2003) Recognition of the 5′ leader of pre-tRNA substrates by the active site of ribonuclease P. RNA 9, 734-745
    • (2003) RNA , vol.9 , pp. 734-745
    • Zahler, N.H.1    Christian, E.L.2    Harris, M.E.3
  • 21
    • 25644433566 scopus 로고    scopus 로고
    • Crystal structure of the RNA component of bacterial ribonuclease P
    • Torres-Larios, A., Swinger, K., Krasilnikov, A.S., Pan, T., and Mondragon, A. (2005) Crystal structure of the RNA component of bacterial ribonuclease P. Nature 437, 584-587
    • (2005) Nature , vol.437 , pp. 584-587
    • Torres-Larios, A.1    Swinger, K.2    Krasilnikov, A.S.3    Pan, T.4    Mondragon, A.5
  • 23
    • 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
  • 24
    • 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
  • 27
    • 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. (2005) Protein activation of a ribozyme: the role of bacterial RNase P protein. EMBO J. 24, 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
  • 28
    • 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. (2003) 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, 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
  • 29
    • 25144500661 scopus 로고    scopus 로고
    • RNase P: Role of distinct protein cofactors in tRNA substrate recognition and RNA-based catalysis
    • Sharin, E., Schein, A., Mann, H., Ben-Asouli, Y., and Jarrous, N. (2005) RNase P: role of distinct protein cofactors in tRNA substrate recognition and RNA-based catalysis. Nucleic Acids Res., 33, 5120-5132
    • (2005) Nucleic Acids Res. , vol.33 , pp. 5120-5132
    • Sharin, E.1    Schein, A.2    Mann, H.3    Ben-Asouli, Y.4    Jarrous, N.5
  • 30
    • 0030669671 scopus 로고    scopus 로고
    • Intermediates and kinetic traps in the folding of a large ribozyme revealed by circular dichroism and UV absorbance spectroscopies and catalytic activity
    • Pan, T. and Sosnick, T.R. (1997) Intermediates and kinetic traps in the folding of a large ribozyme revealed by circular dichroism and UV absorbance spectroscopies and catalytic activity. Nat. Struct. Biol. 4, 931-938
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 931-938
    • Pan, T.1    Sosnick, T.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.