메뉴 건너뛰기




Volumn 22, Issue 17, 2003, Pages 4534-4543

Endonucleolytic processing of CCA-less tRNA precursors by RNase Z in Bacillus subtilis

Author keywords

3 tRNase; CCA; Endonuclease; RNase Z; tRNA

Indexed keywords

EXORIBONUCLEASE; RIBONUCLEASE; RIBONUCLEASE Z; RNA PRECURSOR; TRANSFER RNA; UNCLASSIFIED DRUG;

EID: 0043239333     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdg435     Document Type: Article
Times cited : (116)

References (44)
  • 1
    • 0344298926 scopus 로고    scopus 로고
    • The ribonuclease P database
    • Brown, J.W. (1999) The ribonuclease P database. Nucleic Acids Res., 27, 314.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 314
    • Brown, J.W.1
  • 2
    • 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)
    • Castano, 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
    • Castano, J.G.1    Tobian, J.A.2    Zasloff, M.3
  • 3
    • 0037115876 scopus 로고    scopus 로고
    • The phylogenetic distribution of bacterial ribonucleases
    • Condon, C. and Putzer, H. (2002) The phylogenetic distribution of bacterial ribonucleases. Nucleic Acids Res., 30, 5339-5346.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 5339-5346
    • Condon, C.1    Putzer, H.2
  • 4
    • 0002807705 scopus 로고
    • tRNA processing nucleases
    • Söll, D. and RajBhandary, U.L. (eds). American Society for Microbiology, Washington, DC
    • Deutscher, M.P. (1995) tRNA processing nucleases. In Söll, D. and RajBhandary, U.L. (eds), tRNA: Structure, Biosynthesis and Function. American Society for Microbiology, Washington, DC, pp. 51-65.
    • (1995) tRNA: Structure, Biosynthesis and Function , pp. 51-65
    • Deutscher, M.P.1
  • 5
    • 0017610231 scopus 로고
    • Transfer RNA metabolism in Escherichia coli cells deficient in tRNA nucleotidyltransferase
    • Deutscher, M.P., Lin, J.J. and Evans, J.A. (1977) Transfer RNA metabolism in Escherichia coli cells deficient in tRNA nucleotidyltransferase. J. Mol. Biol., 117, 1081-1094.
    • (1977) J. Mol. Biol. , vol.117 , pp. 1081-1094
    • Deutscher, M.P.1    Lin, J.J.2    Evans, J.A.3
  • 6
    • 0021894203 scopus 로고
    • Nucleolytic processing of a tRNAArg-tRNAAsp dimeric precursor by a homologous component from Saccharomyces cerevisiae
    • Engelke, D.R., Gegenheimer, P. and Abelson, J. (1985) Nucleolytic processing of a tRNAArg-tRNAAsp dimeric precursor by a homologous component from Saccharomyces cerevisiae. J. Biol. Chem., 260, 1271-1279.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1271-1279
    • Engelke, D.R.1    Gegenheimer, P.2    Abelson, J.3
  • 7
    • 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
  • 8
    • 0018416467 scopus 로고
    • In vitro processing of B. mori transfer RNA precursor molecules
    • Garber, R.L. and Altman, S. (1979) In vitro processing of B. mori transfer RNA precursor molecules. Cell, 17, 389-397.
    • (1979) Cell , vol.17 , pp. 389-397
    • Garber, R.L.1    Altman, S.2
  • 9
    • 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
  • 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
    • 0018637808 scopus 로고
    • The primary transcription product of a silkworm alanine tRNA gene: Identification of in vitro sites of initiation, termination and processing
    • Hagenbuchle, 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
    • Hagenbuchle, O.1    Larson, D.2    Hall, G.I.3    Sprague, K.U.4
  • 12
    • 0036231352 scopus 로고    scopus 로고
    • Archaeal RNase P has multiple protein subunits homologous to eukaryotic nuclear RNase P proteins
    • Hall, T.A. and Brown, J.W. (2002) Archaeal RNase P has multiple protein subunits homologous to eukaryotic nuclear RNase P proteins. RNA. 8, 296-306.
    • (2002) RNA , vol.8 , pp. 296-306
    • Hall, T.A.1    Brown, J.W.2
  • 13
    • 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
  • 14
    • 0345668475 scopus 로고    scopus 로고
    • Essential Bacillus subtilis genes
    • Kobayashi, K. et al. (2003) Essential Bacillus subtilis genes. Proc. Natl Acad. Sci. USA, 100, 4678-4683.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4678-4683
    • Kobayashi, K.1
  • 15
    • 0037415721 scopus 로고    scopus 로고
    • Plant dicistronic tRNA-snoRNA genes: A new mode of expression of the small nucleolar RNAs processed by RNase Z
    • Kruszka, K., Barneche, F., Guyot, R., Ailhas, J., Meneau, I., Schiffer, S., Marchfelder, A. and Echeverria, M. (2003) Plant dicistronic tRNA-snoRNA genes: a new mode of expression of the small nucleolar RNAs processed by RNase Z. EMBO J., 22, 621-632.
    • (2003) EMBO J. , vol.22 , pp. 621-632
    • Kruszka, K.1    Barneche, F.2    Guyot, R.3    Ailhas, J.4    Meneau, I.5    Schiffer, S.6    Marchfelder, A.7    Echeverria, M.8
  • 16
    • 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
  • 17
    • 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
  • 18
    • 0030576503 scopus 로고    scopus 로고
    • Maturation pathways for E. coli tRNA precursors: A random multienzyme process in vivo
    • Li, Z. and Deutscher, M.P. (1996) Maturation pathways for E. coli tRNA precursors: a random multienzyme process in vivo. Cell, 86, 503-512.
    • (1996) Cell , vol.86 , pp. 503-512
    • Li, Z.1    Deutscher, M.P.2
  • 19
    • 0036210631 scopus 로고    scopus 로고
    • RNase E plays an essential role in the maturation of Escherichia coli tRNA precursors
    • Li, Z. and Deutscher, M.P. (2002) RNase E plays an essential role in the maturation of Escherichia coli tRNA precursors. RNA, 8, 97-109.
    • (2002) RNA , vol.8 , pp. 97-109
    • Li, Z.1    Deutscher, M.P.2
  • 22
    • 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
  • 23
    • 0024814177 scopus 로고
    • Conformational alterations in the ermC transcript in vivo during induction
    • Mayford, M. and Weisblum, B. (1989) Conformational alterations in the ermC transcript in vivo during induction. EMBO J., 8, 4307-4314.
    • (1989) EMBO J. , vol.8 , pp. 4307-4314
    • Mayford, M.1    Weisblum, B.2
  • 24
    • 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
  • 25
    • 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
  • 26
    • 0032103908 scopus 로고    scopus 로고
    • RNA heptamers that direct RNA cleavage by mammalian tRNA 3′ processing endoribonuclease
    • Nashimoto, M., Geary, S., Tamura, M. and Kaspar, R. (1998) RNA heptamers that direct RNA cleavage by mammalian tRNA 3′ processing endoribonuclease. Nucleic Acids Res., 26, 2565-2572.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 2565-2572
    • Nashimoto, M.1    Geary, S.2    Tamura, M.3    Kaspar, R.4
  • 27
    • 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
  • 28
    • 0033168104 scopus 로고    scopus 로고
    • Long 5′ leaders inhibit removal of a 3′ trailer from a precursor tRNA by mammalian tRNA 3′ processing endoribonuclease
    • Nashimoto, M., Wesemann, D.R., Geary, S., Tamura, M. and Kaspar, R.L. (1999b) Long 5′ leaders inhibit removal of a 3′ trailer from a precursor tRNA by mammalian tRNA 3′ processing endoribonuclease. Nucleic Acids Res., 27, 2770-2776.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 2770-2776
    • Nashimoto, M.1    Wesemann, D.R.2    Geary, S.3    Tamura, M.4    Kaspar, R.L.5
  • 29
    • 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
  • 30
    • 0036571060 scopus 로고    scopus 로고
    • Initiation of tRNA maturation by RNase E is essential for cell viability in E. coli
    • Ow, M.C. and Kushner, S.R. (2002) Initiation of tRNA maturation by RNase E is essential for cell viability in E. coli. Genes Dev., 16, 1102-1115.
    • (2002) Genes Dev. , vol.16 , pp. 1102-1115
    • Ow, M.C.1    Kushner, S.R.2
  • 31
    • 0030436198 scopus 로고    scopus 로고
    • Pre-tRNA 3′-processing in Saccharomyces cerevisiae. Purification and characterization of exo- and endoribonucleases
    • Papadimitriou, A. and Gross, H.J. (1996) Pre-tRNA 3′-processing in Saccharomyces cerevisiae. Purification and characterization of exo- and endoribonucleases. Eur. J. Biochem., 242, 747-759.
    • (1996) Eur. J. Biochem. , vol.242 , pp. 747-759
    • Papadimitriou, A.1    Gross, H.J.2
  • 32
    • 0031854048 scopus 로고    scopus 로고
    • PcrA is an essential DNA helicase of Bacillus subtilis fulfilling functions both in repair and rolling-circle replication
    • Petit, M.-A., Dervyn, E., Rose, M., Entian, K.-D., McGovern, S., Ehrlich, D.S. and Bruand, C. (1998) PcrA is an essential DNA helicase of Bacillus subtilis fulfilling functions both in repair and rolling-circle replication. Mol. Microbiol., 29, 261-273.
    • (1998) Mol. Microbiol. , vol.29 , pp. 261-273
    • Petit, M.-A.1    Dervyn, E.2    Rose, M.3    Entian, K.-D.4    McGovern, S.5    Ehrlich, D.S.6    Bruand, C.7
  • 33
    • 0036018264 scopus 로고    scopus 로고
    • tRNA 3′ end maturation in archaea has eukaryotic features: The RNase Z from Haloferax volcanii
    • Schierling, K., Rosch, 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    Rosch, S.2    Rupprecht, R.3    Schiffer, S.4    Marchfelder, A.5
  • 35
    • 0037013852 scopus 로고    scopus 로고
    • Assigning a function to a conserved group of proteins: The tRNA 3′-processing enzymes
    • Schiffer, S., Rosch, 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    Rosch, S.2    Marchfelder, A.3
  • 36
    • 0038743281 scopus 로고    scopus 로고
    • Recombinant RNase Z does not recognize CCA as part of the tRNA and its cleavage efficiency is influenced by acceptor stem length
    • Schiffer, S., Rosch, S. and Marchfelder, A. (2003) Recombinant RNase Z does not recognize CCA as part of the tRNA and its cleavage efficiency is influenced by acceptor stem length. Biol. Chem., 384, 333-342.
    • (2003) Biol. Chem. , vol.384 , pp. 333-342
    • Schiffer, S.1    Rosch, S.2    Marchfelder, A.3
  • 37
    • 0021056480 scopus 로고
    • Identification of multiple RNases in Xenopus laevis oocytes and their possible role in tRNA processing
    • Solari, A. and Deutscher, M.P. (1983) Identification of multiple RNases in Xenopus laevis oocytes and their possible role in tRNA processing. Mol. Cell. Biol., 3, 1711-1717.
    • (1983) Mol. Cell. Biol. , vol.3 , pp. 1711-1717
    • Solari, A.1    Deutscher, M.P.2
  • 38
    • 0023403272 scopus 로고
    • A cell-free plant extract for accurate pre-tRNA processing, splicing and modification
    • Stange, N. and Beier, H. (1987) A cell-free plant extract for accurate pre-tRNA processing, splicing and modification. EMBO J., 6, 2811-2818.
    • (1987) EMBO J. , vol.6 , pp. 2811-2818
    • Stange, N.1    Beier, H.2
  • 39
    • 0023853759 scopus 로고
    • Processing of a sporulation σ factor in Bacillus subtilis: How morphological structure could control gene expression
    • Stragier, P., Bonamy, C. and Karmazyn-Campelli, C. (1988) Processing of a sporulation σ factor in Bacillus subtilis: how morphological structure could control gene expression. Cell, 52, 697-704.
    • (1988) Cell , vol.52 , pp. 697-704
    • Stragier, P.1    Bonamy, C.2    Karmazyn-Campelli, C.3
  • 40
    • 0038750928 scopus 로고    scopus 로고
    • A candidate prostate cancer susceptibilty gene encodes tRNA 3′ processing endoribonuclease
    • Takaku, H., Minagawa, A., Takagi, M. and Nashimoto, M. (2003) A candidate prostate cancer susceptibilty gene encodes tRNA 3′ processing endoribonuclease. Nucleic Acids Res., 31, 2272-2278.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 2272-2278
    • Takaku, H.1    Minagawa, A.2    Takagi, M.3    Nashimoto, M.4
  • 41
    • 0035135523 scopus 로고    scopus 로고
    • A candidate prostate cancer susceptibility gene at chromosome 17p
    • Tavtigian, S.V. et al.: (2001) A candidate prostate cancer susceptibility gene at chromosome 17p. Nat. Genet., 27, 172-180.
    • (2001) Nat. Genet. , vol.27 , pp. 172-180
    • Tavtigian, S.V.1
  • 42
    • 0031737309 scopus 로고    scopus 로고
    • A vector for systematic gene inactivation in Bacillus subtilis
    • Vagner, V., Dervyn, E. and Ehrlich, S.D. (1998) A vector for systematic gene inactivation in Bacillus subtilis. Microbiology, 144, 3097-3104.
    • (1998) Microbiology , vol.144 , pp. 3097-3104
    • Vagner, V.1    Dervyn, E.2    Ehrlich, S.D.3
  • 44


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.