메뉴 건너뛰기




Volumn 384, Issue 3, 2003, Pages 333-342

Recombinant RNase Z does not recognize CCA as part of the tRNA and its cleavage efficieny is influenced by acceptor stem lenght

Author keywords

3 end maturation; Acceptor stem; CCA; Endonuclease; RNase Z; tRNA

Indexed keywords

PLANT EXTRACT; RECOMBINANT ENZYME; RIBONUCLEASE Z; RNA POLYMERASE; TRANSFER RNA; TRINUCLEOTIDE; UNCLASSIFIED DRUG;

EID: 0038743281     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2003.039     Document Type: Review
Times cited : (23)

References (24)
  • 1
    • 0021837835 scopus 로고
    • Purification and characterization of an endonuclease from Xenopus laevis ovaries which accurately processes the 3′ terminus of human pre-tRNA-Met(i) (3′ pre-tRNase)
    • Castaño, J.G., Tobian, J.A. and Zasloff, M. (1985). Purification and characterization of an endonuclease from Xenopus laevis ovaries which accurately processes the 3′ terminus of human pre-tRNA-Met(i) (3′ pre-tRNase). J. Biol. Chem., 260, 9002-9008.
    • (1985) J. Biol. Chem. , vol.260 , pp. 9002-9008
    • Castaño, J.G.1    Tobian, J.A.2    Zasloff, M.3
  • 2
    • 0002807705 scopus 로고
    • tRNA processing nucleases
    • D. Söll and U. Raj-Bhandary eds. (Washington, DC, USA: ASM Press)
    • Deutscher, M.P. (1995). tRNA processing nucleases. In: tRNA: Structure, Biosynthesis, and Function, D. Söll and U. Raj-Bhandary, eds. (Washington, DC, USA: ASM Press), pp. 51-65.
    • (1995) TRNA: Structure, Biosynthesis, and Function , pp. 51-65
    • Deutscher, M.P.1
  • 3
    • 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
  • 4
    • 0029278892 scopus 로고
    • Characterization and partial purification of two pre-tRNA 5′-processing activities from Daucus carrota (carrot) suspension cells
    • Franklin, S.E., Zwick, M.G. and Johnson, J.D. (1995). Characterization and partial purification of two pre-tRNA 5′-processing activities from Daucus carrota (carrot) suspension cells. Plant J. 7, 553-563.
    • (1995) Plant J. , vol.7 , pp. 553-563
    • Franklin, S.E.1    Zwick, M.G.2    Johnson, J.D.3
  • 5
    • 0018702460 scopus 로고
    • Transcription of a cloned Bombyx mori tRNA2Ala gene: Nucleotide sequence of the tRNA precursor and its processing in vitro
    • Garber, R.L. and Gage, L.P. (1979). Transcription of a cloned Bombyx mori tRNA2Ala gene: nucleotide sequence of the tRNA precursor and its processing in vitro. Cell 18, 817-828.
    • (1979) Cell , vol.18 , pp. 817-828
    • Garber, R.L.1    Gage, L.P.2
  • 6
    • 0018637808 scopus 로고
    • The primary transcription product of a silkworm alanine tRNA gene: Identification of in vitro sites of initiation, termination and processing
    • Hagenbüchle, O., Larson, D., Hall, G.I. and Sprague, K.U. (1979). The primary transcription product of a silkworm alanine tRNA gene: identification of in vitro sites of initiation, termination and processing. Cell 18, 1217-1229.
    • (1979) Cell , vol.18 , pp. 1217-1229
    • Hagenbüchle, O.1    Larson, D.2    Hall, G.I.3    Sprague, K.U.4
  • 7
    • 0031575911 scopus 로고    scopus 로고
    • Purification and characterization of the precursor tRNA 3′-end processing nuclease from Aspergillus nidulans
    • Han, S.J. and Kang, H.S. (1997). Purification and characterization of the precursor tRNA 3′-end processing nuclease from Aspergillus nidulans. Biochem. Biophys. Res. Commun. 233, 354-358.
    • (1997) Biochem. Biophys. Res. Commun. , vol.233 , pp. 354-358
    • Han, S.J.1    Kang, H.S.2
  • 8
    • 0031889777 scopus 로고    scopus 로고
    • 5′ end maturation and RNA editing have to precede tRNA 3′ processing in plant mitochondria
    • Kunzmann, A., Brennicke, A. and Marchfelder, A. (1998). 5′ end maturation and RNA editing have to precede tRNA 3′ processing in plant mitochondria. Proc. Natl. Acad. Sci. USA 95, 108-113.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 108-113
    • Kunzmann, A.1    Brennicke, A.2    Marchfelder, A.3
  • 9
    • 0031974633 scopus 로고    scopus 로고
    • Matrices of paired substitutions show the effects of tRNA D/T loop sequence on Drosophila RNase P and 3′-tRNase processing
    • Levinger, L., Bourne, R., Kolla, S., Cylin, E., Russell, K., Wang, X. and Mohan, A. (1998). Matrices of paired substitutions show the effects of tRNA D/T loop sequence on Drosophila RNase P and 3′-tRNase processing. J. Biol. Chem. 273, 1015-1025.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1015-1025
    • Levinger, L.1    Bourne, R.2    Kolla, S.3    Cylin, E.4    Russell, K.5    Wang, X.6    Mohan, A.7
  • 10
    • 0023664627 scopus 로고
    • Separation and characterization of 5′- and 3′-tRNA processing nucleases from rat liver mitochondria
    • Manam, S. and Van Tuyle, G.C. (1987). Separation and characterization of 5′- and 3′-tRNA processing nucleases from rat liver mitochondria. J. Biol. Chem. 262, 10272-10279.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10272-10279
    • Manam, S.1    Van Tuyle, G.C.2
  • 11
    • 0028484051 scopus 로고
    • Characterization and partial purification of tRNA processing activities from potato mitochondria
    • Marchfelder, A. and Brennicke, A. (1994). Characterization and partial purification of tRNA processing activities from potato mitochondria. Plant Physiol. 105, 1247-1254.
    • (1994) Plant Physiol. , vol.105 , pp. 1247-1254
    • Marchfelder, A.1    Brennicke, A.2
  • 12
    • 0034728385 scopus 로고    scopus 로고
    • tRNA 3′ processing in plants: Nuclear and mitochondrial activities differ
    • Mayer, M., Schiffer, S. and Marchfelder, A. (2000). tRNA 3′ processing in plants: nuclear and mitochondrial activities differ. Biochemistry 39, 2096-2105.
    • (2000) Biochemistry , vol.39 , pp. 2096-2105
    • Mayer, M.1    Schiffer, S.2    Marchfelder, A.3
  • 13
    • 0033057704 scopus 로고    scopus 로고
    • The 3′ end CCA of mature tRNA is an antideterminant for eukaryotic 3′-tRNase
    • Mohan, A., Whyte, S., Wang, X., Nashimoto, M. and Levinger, L. (1999). The 3′ end CCA of mature tRNA is an antideterminant for eukaryotic 3′-tRNase. RNA 5, 245-256.
    • (1999) RNA , vol.5 , pp. 245-256
    • Mohan, A.1    Whyte, S.2    Wang, X.3    Nashimoto, M.4    Levinger, L.5
  • 14
    • 0035094698 scopus 로고    scopus 로고
    • The final cut. The importance of tRNA 3′-processing
    • Mörl, M. and Marchfelder, A. (2001). The final cut. The importance of tRNA 3′-processing. EMBO Rep. 2, 17-20.
    • (2001) EMBO Rep. , vol.2 , pp. 17-20
    • Mörl, M.1    Marchfelder, A.2
  • 15
    • 0030754921 scopus 로고    scopus 로고
    • Distribution of both lengths and 5′ terminal nucleotides of mammalian pre-tRNA 3′ trailers reflects properties of 3′ processing endoribonuclease
    • Nashimoto, M. (1997). Distribution of both lengths and 5′ terminal nucleotides of mammalian pre-tRNA 3′ trailers reflects properties of 3′ processing endoribonuclease. Nucleic Acids Res. 25, 1148-1154.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1148-1154
    • Nashimoto, M.1
  • 16
    • 0033554375 scopus 로고    scopus 로고
    • Minimum requirements for substrates of mammalian tRNA 3′ processing endoribonuclease
    • Nashimoto, M., Tamura, M. and Kaspar, R.L. (1999a). Minimum requirements for substrates of mammalian tRNA 3′ processing endoribonuclease. Biochemistry 38, 12089-12096.
    • (1999) Biochemistry , vol.38 , pp. 12089-12096
    • Nashimoto, M.1    Tamura, M.2    Kaspar, R.L.3
  • 17
    • 0033537798 scopus 로고    scopus 로고
    • Selection of cleavage site by mammalian tRNA 3′ processing endoribonuclease
    • Nashimoto, M., Tamura, M. and Kaspar, R.L. (1999b). Selection of cleavage site by mammalian tRNA 3′ processing endoribonuclease. J. Mol. Biol. 287, 727-740.
    • (1999) J. Mol. Biol. , vol.287 , pp. 727-740
    • Nashimoto, M.1    Tamura, M.2    Kaspar, R.L.3
  • 18
    • 0026570259 scopus 로고
    • Cleavage specificity of chloroplast and nuclear tRNA 3′-processing nucleases
    • Oommen, A., Li, X.Q. and Gegenheimer, P. (1992). Cleavage specificity of chloroplast and nuclear tRNA 3′-processing nucleases. Mol. Cell. Biol. 12, 865-875.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 865-875
    • Oommen, A.1    Li, X.Q.2    Gegenheimer, P.3
  • 19
    • 0036018264 scopus 로고    scopus 로고
    • tRNA 3′ end maturation in archaea has eukaryotic features: The RNase Z from Haloferax volcanii
    • Schierling, K., Rösch, S., Rupprecht, R., Schiffer, S. and Marchfelder, A. (2002). tRNA 3′ end maturation in archaea has eukaryotic features: the RNase Z from Haloferax volcanii. J. Mol. Biol. 316, 895-902.
    • (2002) J. Mol. Biol. , vol.316 , pp. 895-902
    • Schierling, K.1    Rösch, S.2    Rupprecht, R.3    Schiffer, S.4    Marchfelder, A.5
  • 21
    • 0037013852 scopus 로고    scopus 로고
    • Assigning a function to a conserved group of proteins: The tRNA 3′-processing enzymes
    • Schiffer, S., Rösch, S. and Marchfelder, A. (2002). Assigning a function to a conserved group of proteins: the tRNA 3′-processing enzymes. EMBO J. 21, 2769-2777.
    • (2002) EMBO J. , vol.21 , pp. 2769-2777
    • Schiffer, S.1    Rösch, S.2    Marchfelder, A.3
  • 23
    • 0026165754 scopus 로고
    • Expression of nuclear tRNA(Tyr) genes from Arabidopsis thaliana in HeLa cell and wheat germ extracts
    • Stange, N., Beier, D. and Beier, H. (1991). Expression of nuclear tRNA(Tyr) genes from Arabidopsis thaliana in HeLa cell and wheat germ extracts. Plant Mol. Biol. 16, 865-875.
    • (1991) Plant Mol. Biol. , vol.16 , pp. 865-875
    • Stange, N.1    Beier, D.2    Beier, H.3
  • 24
    • 0025182710 scopus 로고
    • A potato mitochondrial isoleucine tRNA is coded for by a mitochondrial gene possesing a methionine anticodon
    • Weber, F. Dietrich, A., Weil, J.-H. and Maréchal-Drouard, L. (1990). A potato mitochondrial isoleucine tRNA is coded for by a mitochondrial gene possesing a methionine anticodon. Nucleic Acids Res. 18, 5027-5030.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 5027-5030
    • Weber, F.1    Dietrich, A.2    Weil, J.-H.3    Maréchal-Drouard, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.