메뉴 건너뛰기




Volumn 14, Issue 5, 2008, Pages 928-937

Maturation of the 5S rRNA 5′ end is catalyzed in vitro by the endonuclease tRNase Z in the archaeon H. volcanii

Author keywords

Archaea; Haloferax volcanii; RNase Z; rRNA processing; tRNA processing; tRNase Z

Indexed keywords

ENDONUCLEASE; POTASSIUM CHLORIDE; PROTEIN TRNASE Z; RIBOSOME RNA; SODIUM CHLORIDE; TRANSFER RNA; UNCLASSIFIED DRUG; ARCHAEAL RNA; PRE RIBOSOMAL RNA ENDORIBONUCLEASE; PRE-RIBOSOMAL RNA ENDORIBONUCLEASE; RECOMBINANT PROTEIN; RIBONUCLEASE; RNA 5S; RNA PRECURSOR;

EID: 42449149147     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.933208     Document Type: Article
Times cited : (33)

References (40)
  • 1
    • 2342625231 scopus 로고    scopus 로고
    • Development of additional selectable markers for the halophilic archaeon Haloferax volcanii based on the leuB and trpA genes
    • Allers, T., Ngo, H.P., Mevarech, M., and Lloyd, R.G. 2004. Development of additional selectable markers for the halophilic archaeon Haloferax volcanii based on the leuB and trpA genes. Appl. Environ. Microbiol. 70: 943-953 .
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 943-953
    • Allers, T.1    Ngo, H.P.2    Mevarech, M.3    Lloyd, R.G.4
  • 2
    • 0037309062 scopus 로고    scopus 로고
    • Development of a gene knockout system for the halophilic archaeon Haloferax volcanii by use of the pyrE gene
    • Bitan-Banin, G., Ortenberg, R., and Mevarech, M. 2003. Development of a gene knockout system for the halophilic archaeon Haloferax volcanii by use of the pyrE gene. J. Bacteriol. 185: 772-778.
    • (2003) J. Bacteriol , vol.185 , pp. 772-778
    • Bitan-Banin, G.1    Ortenberg, R.2    Mevarech, M.3
  • 3
    • 35648943743 scopus 로고    scopus 로고
    • Regulated polyploidy in halophilic archaea
    • doi: 10.1371/journal.pone.0000092
    • Breuert, S., Allers, T., Spohn, G., and Soppa, J. 2006. Regulated polyploidy in halophilic archaea. PLoS ONE 1: e92. doi: 10.1371/journal.pone.0000092.
    • (2006) PLoS ONE , vol.1
    • Breuert, S.1    Allers, T.2    Spohn, G.3    Soppa, J.4
  • 4
    • 0005961647 scopus 로고
    • Archaebacteria: Transcription and processing of ribosomal RNA sequences in Halobacterium cutirubrum
    • Chant, J. and Dennis, P. 1986. Archaebacteria: Transcription and processing of ribosomal RNA sequences in Halobacterium cutirubrum. EMBO J. 5: 1091-1097.
    • (1986) EMBO J , vol.5 , pp. 1091-1097
    • Chant, J.1    Dennis, P.2
  • 5
    • 26444483970 scopus 로고    scopus 로고
    • Characterization of TRZ1, a yeast homolog of the human candidate prostate cancer susceptibility gene ELAC2
    • Chen, Y., Beck, A., Davenport, C., Chen, Y., Shattuck, D., and Tavtigian, S.T. 2005. Characterization of TRZ1, a yeast homolog of the human candidate prostate cancer susceptibility gene ELAC2. BMC Mol. Biol. 6: 12.
    • (2005) BMC Mol. Biol , vol.6 , pp. 12
    • Chen, Y.1    Beck, A.2    Davenport, C.3    Chen, Y.4    Shattuck, D.5    Tavtigian, S.T.6
  • 6
    • 0037115876 scopus 로고    scopus 로고
    • The phylogenetic distribution of bacterial ribonucleases
    • doi: 10.1093/nar/gkf691
    • Condon, C. and Putzer, H. 2002. The phylogenetic distribution of bacterial ribonucleases. Nucleic Acids Res. 30: 5339-5346. doi: 10.1093/nar/gkf691.
    • (2002) Nucleic Acids Res , vol.30 , pp. 5339-5346
    • Condon, C.1    Putzer, H.2
  • 8
    • 0031659282 scopus 로고    scopus 로고
    • Transcription analysis of two disparate rRNA operons in the halophilic archaeon Haloarcula marismortui
    • Dennis, P.P., Ziesche, S., and Mylvaganam, S. 1998. Transcription analysis of two disparate rRNA operons in the halophilic archaeon Haloarcula marismortui. J. Bacteriol. 180: 4804-4813.
    • (1998) J. Bacteriol , vol.180 , pp. 4804-4813
    • Dennis, P.P.1    Ziesche, S.2    Mylvaganam, S.3
  • 9
    • 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
  • 11
    • 0019787261 scopus 로고
    • Processing of procaryotic ribonucleic acid
    • Gegenheimer, P. and Apirion, D. 1981. Processing of procaryotic ribonucleic acid. Microbiol. Rev. 45: 502-541.
    • (1981) Microbiol. Rev , vol.45 , pp. 502-541
    • Gegenheimer, P.1    Apirion, D.2
  • 13
    • 0027982167 scopus 로고
    • High-pressure freezing of cell suspensions in cellulose capillary tubes
    • Hohenberg, H., Mannweiler, K., and Muller, M. 1994. High-pressure freezing of cell suspensions in cellulose capillary tubes. J. Microsc. 175: 34-43.
    • (1994) J. Microsc , vol.175 , pp. 34-43
    • Hohenberg, H.1    Mannweiler, K.2    Muller, M.3
  • 14
    • 0030730242 scopus 로고    scopus 로고
    • Properties of H. volcanii tRNA intron endonuclease reveal a relationship between the archaeal and eucaryal tRNA intron processing systems
    • Kleman-Leyer, K., Armbruster, D.W., and Daniels, C.J. 1997. Properties of H. volcanii tRNA intron endonuclease reveal a relationship between the archaeal and eucaryal tRNA intron processing systems. Cell 89: 839-847.
    • (1997) Cell , vol.89 , pp. 839-847
    • Kleman-Leyer, K.1    Armbruster, D.W.2    Daniels, C.J.3
  • 16
    • 0031889777 scopus 로고    scopus 로고
    • 5′ end maturation and RNA editing have to precede tRNA 39 processing in plant mitochondria
    • Kunzmann, A., Brennicke, A., and Marchfelder, A. 1998. 5′ end maturation and RNA editing have to precede tRNA 39 processing in plant mitochondria. Proc. Natl. Acad. Sci. 95: 108-113.
    • (1998) Proc. Natl. Acad. Sci , vol.95 , pp. 108-113
    • Kunzmann, A.1    Brennicke, A.2    Marchfelder, A.3
  • 17
    • 0016139829 scopus 로고
    • Salt-dependent properties of proteins from extremely halophilic bacteria
    • Lanyi, J.K. 1974. Salt-dependent properties of proteins from extremely halophilic bacteria. Bacteriol. Rev. 38: 272-290.
    • (1974) Bacteriol. Rev , vol.38 , pp. 272-290
    • Lanyi, J.K.1
  • 18
  • 19
    • 0029151159 scopus 로고
    • The tRNA processing enzyme RNase T is essential for maturation of 5S RNA
    • Li, Z. and Deutscher, M.P. 1995. The tRNA processing enzyme RNase T is essential for maturation of 5S RNA. Proc. Natl. Acad. Sci. 92: 6883-6886.
    • (1995) Proc. Natl. Acad. Sci , vol.92 , pp. 6883-6886
    • Li, Z.1    Deutscher, M.P.2
  • 20
    • 0025344837 scopus 로고
    • In vitro processing of mitochondrial and plastid derived tRNA precursors in a plant mitochondrial extract
    • Marchfelder, A., Schuster, W., and Brennicke, A. 1990. In vitro processing of mitochondrial and plastid derived tRNA precursors in a plant mitochondrial extract. Nucleic Acids Res. 18: 1401-1406.
    • (1990) Nucleic Acids Res , vol.18 , pp. 1401-1406
    • Marchfelder, A.1    Schuster, W.2    Brennicke, A.3
  • 21
    • 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
  • 22
    • 34250398425 scopus 로고
    • Halobacterium volcanii spec. nov., a Dead Sea halobacterium with a moderate salt requirement
    • Mullakhanbhai, M.F. and Larsen, H. 1975. Halobacterium volcanii spec. nov., a Dead Sea halobacterium with a moderate salt requirement. Arch. Microbiol. 104: 207-214.
    • (1975) Arch. Microbiol , vol.104 , pp. 207-214
    • Mullakhanbhai, M.F.1    Larsen, H.2
  • 23
    • 0033554375 scopus 로고    scopus 로고
    • Minimum requirements for substrates of mammalian tRNA 3′ processing endoribonuclease
    • Nashimoto, M., Tamura, M., and Kaspar, R.L. 1999. 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
  • 24
    • 34249714815 scopus 로고    scopus 로고
    • Norais, C., Hawkins, M., Hartman, A.L., Eisen, J.A., Myllykallio, H., and Allers, T. 2007. Genetic and physical mapping of DNA replication origins in Haloferax volcanii. PLoS Genet. 3: e77. doi: 10.1371/journal.pgen. 0030077.
    • Norais, C., Hawkins, M., Hartman, A.L., Eisen, J.A., Myllykallio, H., and Allers, T. 2007. Genetic and physical mapping of DNA replication origins in Haloferax volcanii. PLoS Genet. 3: e77. doi: 10.1371/journal.pgen. 0030077.
  • 25
    • 0033022073 scopus 로고    scopus 로고
    • Bioenergetic aspects of halophilism
    • Oren, A. 1999. Bioenergetic aspects of halophilism. Microbiol. Mol. Biol. Rev. 63: 334-348.
    • (1999) Microbiol. Mol. Biol. Rev , vol.63 , pp. 334-348
    • Oren, A.1
  • 26
    • 0034021158 scopus 로고    scopus 로고
    • The extremely halophilic archaeon Haloferax volcanii has two very different dihydrofolate reductases
    • Ortenberg, R., Rozenblatt-Rosen, O., and Mevarech, M. 2000. The extremely halophilic archaeon Haloferax volcanii has two very different dihydrofolate reductases. Mol. Microbiol. 35: 1493-1505.
    • (2000) Mol. Microbiol , vol.35 , pp. 1493-1505
    • Ortenberg, R.1    Rozenblatt-Rosen, O.2    Mevarech, M.3
  • 28
    • 33645826534 scopus 로고    scopus 로고
    • RNase Z in Escherichia coli plays a significant role in mRNA decay
    • Perwez, T. and Kushner, S.R. 2006. RNase Z in Escherichia coli plays a significant role in mRNA decay. Mol. Microbiol. 60: 723-737.
    • (2006) Mol. Microbiol , vol.60 , pp. 723-737
    • Perwez, T.1    Kushner, S.R.2
  • 29
    • 42449161350 scopus 로고    scopus 로고
    • Rösch, S. 2004. Isolation and characterisation of the tRNase Z from Archaea. Biology II, p. 130-University of Ulm, Ulm .
    • Rösch, S. 2004. Isolation and characterisation of the tRNase Z from Archaea. Biology II, p. 130-University of Ulm, Ulm .
  • 31
    • 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
  • 33
    • 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
  • 36
    • 0021093623 scopus 로고
    • Precursor nucleotides at the 5′ end are not required for processing by RNase E at the 3′ end of 5-S rRNA
    • Szeberenyi, J., Roy, M.K., and Apirion, D. 1983. Precursor nucleotides at the 5′ end are not required for processing by RNase E at the 3′ end of 5-S rRNA. Eur. J. Biochem. 136: 321-326.
    • (1983) Eur. J. Biochem , vol.136 , pp. 321-326
    • Szeberenyi, J.1    Roy, M.K.2    Apirion, D.3
  • 37
    • 0033367325 scopus 로고    scopus 로고
    • Ribosome synthesis in Saccharomyces cerevisiae
    • Venema, J. and Tollervey, D. 1999. Ribosome synthesis in Saccharomyces cerevisiae. Annu. Rev. Genet. 33: 261-311.
    • (1999) Annu. Rev. Genet , vol.33 , pp. 261-311
    • Venema, J.1    Tollervey, D.2
  • 38
    • 29044449835 scopus 로고    scopus 로고
    • The tRNase Z family of proteins. Physiological functions, substrate specificity, and structural properties
    • Vogel, A., Schilling, O., Späth, B., and Marchfelder, A. 2005. The tRNase Z family of proteins. Physiological functions, substrate specificity, and structural properties. Biol. Chem. 386: 1253-1264.
    • (2005) Biol. Chem , vol.386 , pp. 1253-1264
    • Vogel, A.1    Schilling, O.2    Späth, B.3    Marchfelder, A.4
  • 39
    • 0036440834 scopus 로고    scopus 로고
    • Freeze substitution of high-pressure frozen samples: The visibility of biological membranes is improved when the substitution medium contains water
    • Walther, P. and Ziegler, A. 2002. Freeze substitution of high-pressure frozen samples: The visibility of biological membranes is improved when the substitution medium contains water. J. Microsc. 208: 3-10.
    • (2002) J. Microsc , vol.208 , pp. 3-10
    • Walther, P.1    Ziegler, A.2
  • 40
    • 0035041676 scopus 로고    scopus 로고
    • Conformational analysis of DNA-trinucleotide-hairpin- loop structures using a continuum solvent model
    • Zacharias, M. 2001. Conformational analysis of DNA-trinucleotide-hairpin- loop structures using a continuum solvent model. Biophys. J. 80: 2350-2363.
    • (2001) Biophys. J , vol.80 , pp. 2350-2363
    • Zacharias, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.