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Volumn 185, Issue 18, 2003, Pages 5483-5490

Influence of temperature on tRNA modification in archaea: Methanococcoides burtonii (optimum growth temperature [Topt], 23°C) and Stetteria hydrogenophila (Topt, 95°C)

Author keywords

[No Author keywords available]

Indexed keywords

TRANSFER RNA;

EID: 0042337212     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.18.5483-5490.2003     Document Type: Article
Times cited : (96)

References (52)
  • 2
    • 0015541340 scopus 로고
    • The effect of growth temperature on the in vivo ribose methylation of Bacillus stearothermophilus
    • Agris, P. F., P. Koh, and D. Söll. 1973. The effect of growth temperature on the in vivo ribose methylation of Bacillus stearothermophilus. Arch. Biochem. Biophys. 154:277-282.
    • (1973) Arch. Biochem. Biophys. , vol.154 , pp. 277-282
    • Agris, P.F.1    Koh, P.2    Söll, D.3
  • 3
    • 0024415902 scopus 로고
    • Codon recognition patterns as deduced from sequences of the complete set of transfer RNA species in Mycoplasma capricolum
    • Andachi, Y., F. Yamao, A. Muto, and S. Osawa. 1989. Codon recognition patterns as deduced from sequences of the complete set of transfer RNA species in Mycoplasma capricolum. J. Mol. Biol. 209:37-54.
    • (1989) J. Mol. Biol. , vol.209 , pp. 37-54
    • Andachi, Y.1    Yamao, F.2    Muto, A.3    Osawa, S.4
  • 4
    • 0001918945 scopus 로고    scopus 로고
    • Location and distribution of modified nucleotides in tRNA
    • H. Grosjean and R. Benne (ed.), ASM Press, Washington, D.C.
    • Auffinger, P., and E. Westhof. 1998. Location and distribution of modified nucleotides in tRNA, p. 569-576. In H. Grosjean and R. Benne (ed.), Modification and editing of RNA. ASM Press, Washington, D.C.
    • (1998) Modification and Editing of RNA , pp. 569-576
    • Auffinger, P.1    Westhof, E.2
  • 5
    • 0021103441 scopus 로고
    • Complete analysis of tRNA-modified nucleosides by high performance liquid chromatography: The 29 modified nucleosides of Salmonella typhimurium and Escherichia coli tRNA
    • Buck, M., M. Connick, and B. N. Ames. 1983. Complete analysis of tRNA-modified nucleosides by high performance liquid chromatography: the 29 modified nucleosides of Salmonella typhimurium and Escherichia coli tRNA. Anal. Biochem. 129:1-13.
    • (1983) Anal. Biochem. , vol.129 , pp. 1-13
    • Buck, M.1    Connick, M.2    Ames, B.N.3
  • 7
    • 0042704187 scopus 로고    scopus 로고
    • Detection and structure analysis of modified nucleosides in RNA by mass spectrometry
    • H. Grosjean and R. Benne (ed.), ASM Press, Washington, D.C.
    • Crain, P. F. 1998. Detection and structure analysis of modified nucleosides in RNA by mass spectrometry, p. 47-57. In H. Grosjean and R. Benne (ed.), Modification and editing of RNA. ASM Press, Washington, D.C.
    • (1998) Modification and Editing of RNA , pp. 47-57
    • Crain, P.F.1
  • 8
    • 0025683270 scopus 로고
    • Preparation and enzymatic hydrolysis of RNA and DNA for mass spectrometry
    • Crain, P. F. 1990. Preparation and enzymatic hydrolysis of RNA and DNA for mass spectrometry. Methods Enzymol. 193:782-790.
    • (1990) Methods Enzymol. , vol.193 , pp. 782-790
    • Crain, P.F.1
  • 9
    • 0029077840 scopus 로고
    • Characterization of fully 2′-modified oligoribonucleotide hetero- and homoduplex hybridization and nuclease sensitivity
    • Cummins, L. L., S. R. Owens, L. M. Risen, E. A. Lesnik, S. M. Freier, D. McGee, C. J. Guinosso, and P. D. Cook. 1995. Characterization of fully 2′-modified oligoribonucleotide hetero- and homoduplex hybridization and nuclease sensitivity. Nucleic Acids Res. 23:2019-2024.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 2019-2024
    • Cummins, L.L.1    Owens, S.R.2    Risen, L.M.3    Lesnik, E.A.4    Freier, S.M.5    McGee, D.6    Guinosso, C.J.7    Cook, P.D.8
  • 11
    • 0029736427 scopus 로고    scopus 로고
    • Quantitative measurement of dihyrouridine in RNA using isotope dilution chromatography-mass spectrometry (LC/MS)
    • Dalluge, J. J., T. Hashizume, and J. A. McCloskey. 1996. Quantitative measurement of dihyrouridine in RNA using isotope dilution chromatography-mass spectrometry (LC/MS). Nucleic Acids Res. 24:3242-3245.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3242-3245
    • Dalluge, J.J.1    Hashizume, T.2    McCloskey, J.A.3
  • 13
    • 0018462013 scopus 로고
    • Role of ribothymidine in the thermal stability of transfer RNA as monitored by proton magnetic resonance
    • Davanloo, P., M. Sprinzl, K. Watanabe, M. Albani, and H. Kersten. 1979. Role of ribothymidine in the thermal stability of transfer RNA as monitored by proton magnetic resonance. Nucleic Acids Res. 6:1571-1581.
    • (1979) Nucleic Acids Res. , vol.6 , pp. 1571-1581
    • Davanloo, P.1    Sprinzl, M.2    Watanabe, K.3    Albani, M.4    Kersten, H.5
  • 14
    • 0002841715 scopus 로고    scopus 로고
    • Biophysical and conformational properties of modified nucleosides in RNA (nuclear magnetic resonance studies)
    • H. Grosjean and R. Benne (ed.), ASM Press, Washington, D.C.
    • Davis, D. R. 1998. Biophysical and conformational properties of modified nucleosides in RNA (nuclear magnetic resonance studies), p. 85-102. In H. Grosjean and R. Benne (ed.), Modification and editing of RNA. ASM Press, Washington, D.C.
    • (1998) Modification and Editing of RNA , pp. 85-102
    • Davis, D.R.1
  • 15
    • 0034999985 scopus 로고    scopus 로고
    • A guided tour: Small RNA function in Archaea
    • Dennis, P. P., A. Omer, and T. Lowe. 2001. A guided tour: small RNA function in Archaea. Mol. Microbiol. 40:509-519.
    • (2001) Mol. Microbiol. , vol.40 , pp. 509-519
    • Dennis, P.P.1    Omer, A.2    Lowe, T.3
  • 16
    • 0027370662 scopus 로고
    • Probing structural differences between native and in vitro transcribed Escherichia coli valine transfer RNA: Evidence for stable base modification-dependent conformers
    • Derrick, W. B., and J. Horowitz. 1993. Probing structural differences between native and in vitro transcribed Escherichia coli valine transfer RNA: evidence for stable base modification-dependent conformers. Nucleic Acids Res. 21:4948-4953.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 4948-4953
    • Derrick, W.B.1    Horowitz, J.2
  • 18
    • 0024289115 scopus 로고
    • Thermospray liquid chromatography/mass spectrometry in deuterium oxide
    • Edmonds, C. G., S. C. Pomerantz, F. F. Hsu, and J. A. McCloskey. 1988. Thermospray liquid chromatography/mass spectrometry in deuterium oxide. Anal. Chem. 60:2314-2317.
    • (1988) Anal. Chem. , vol.60 , pp. 2314-2317
    • Edmonds, C.G.1    Pomerantz, S.C.2    Hsu, F.F.3    McCloskey, J.A.4
  • 19
    • 0032101712 scopus 로고    scopus 로고
    • Presence and location of modified nucleotides in E. coli tmRNA: Structural mimicry with tRNA acceptor branches
    • Felden, B., K. Hanawa, J. F. Atkins, H. Himeno, A. Muto, R. F. Gesteland, J. A. McCloskey, and P. F. Crain. 1998. Presence and location of modified nucleotides in E. coli tmRNA: structural mimicry with tRNA acceptor branches. EMBO J. 17:3188-3196.
    • (1998) EMBO J. , vol.17 , pp. 3188-3196
    • Felden, B.1    Hanawa, K.2    Atkins, J.F.3    Himeno, H.4    Muto, A.5    Gesteland, R.F.6    McCloskey, J.A.7    Crain, P.F.8
  • 21
    • 85012734147 scopus 로고
    • Ribonucleoside analysis by reversed-phase high performance liquid chromatography
    • C. W. Gehrke and K. C. Kuo (ed.), A. Elsevier, New York, N.Y.
    • Gehrke, C. W., and K.-C. Kuo. 1990. Ribonucleoside analysis by reversed-phase high performance liquid chromatography, p. A3-A64. In C. W. Gehrke and K. C. Kuo (ed.), Chromatography and identification of nucleosides, part A. Journal of chromatography library, vol. 45A. Elsevier, New York, N.Y.
    • (1990) Chromatography and Identification of Nucleosides, Part A. Journal of Chromatography Library , vol.45
    • Gehrke, C.W.1    Kuo, K.-C.2
  • 23
    • 0035928817 scopus 로고    scopus 로고
    • Specific binding of 8-oxoguanine-containing RNA to polynucleotide phosphorylase protein
    • Hayakawa, H., M. Kuwano, and M. Sekiguchi. 2001. Specific binding of 8-oxoguanine-containing RNA to polynucleotide phosphorylase protein. Biochemistry 40:9977-9982.
    • (2001) Biochemistry , vol.40 , pp. 9977-9982
    • Hayakawa, H.1    Kuwano, M.2    Sekiguchi, M.3
  • 24
    • 0022273096 scopus 로고
    • Two tRNA Ile species from an extreme thermophile, Thermus thermophilus HB8: Effect of 2-thiolation of ribothymidine on the thermostability of tRNA
    • Horie, N., M. Hara-Yokoyama, S. Yokoyama, K. Watanabe, Y. Kuchino, S. Nishimura, and T. Miyazawa. 1985. Two tRNA Ile species from an extreme thermophile, Thermus thermophilus HB8: effect of 2-thiolation of ribothymidine on the thermostability of tRNA. Biochemistry 24:5711-5715.
    • (1985) Biochemistry , vol.24 , pp. 5711-5715
    • Horie, N.1    Hara-Yokoyama, M.2    Yokoyama, S.3    Watanabe, K.4    Kuchino, Y.5    Nishimura, S.6    Miyazawa, T.7
  • 25
    • 0031129435 scopus 로고    scopus 로고
    • Stetteria hydrogenophila, gen. nov. and sp. nov., a novel mixotrophic sulfur-dependent crenarchaeote isolated from Milos, Greece
    • Jochimsen, B., S. Peinemann-Simon, H. Völker, D. Stüben, R. Botz, P. Stoffers, P. R. Dando, and M. Thomm. 1997. Stetteria hydrogenophila, gen. nov. and sp. nov., a novel mixotrophic sulfur-dependent crenarchaeote isolated from Milos, Greece. Extremophiles 1:67-73.
    • (1997) Extremophiles , vol.1 , pp. 67-73
    • Jochimsen, B.1    Peinemann-Simon, S.2    Völker, H.3    Stüben, D.4    Botz, R.5    Stoffers, P.6    Dando, P.R.7    Thomm, M.8
  • 26
  • 27
    • 0028272470 scopus 로고
    • Role of posttranscriptional modification in stabilization of transfer RNA from hyperthermophiles
    • Kowalak, J. A., J. J. Dalluge, J. A. McCloskey, and K. O. Stetter. 1994. Role of posttranscriptional modification in stabilization of transfer RNA from hyperthermophiles. Biochemistry 33:7869-7876.
    • (1994) Biochemistry , vol.33 , pp. 7869-7876
    • Kowalak, J.A.1    Dalluge, J.J.2    McCloskey, J.A.3    Stetter, K.O.4
  • 28
    • 0018832937 scopus 로고
    • Thermally induced biosynthesis of 2′-O-methylguanosine in tRNA from an extreme thermophile, Thermus thermophilus HB27
    • Kumagi, I., K. Watanabe, and T. Oshima. 1980. Thermally induced biosynthesis of 2′-O-methylguanosine in tRNA from an extreme thermophile, Thermus thermophilus HB27. Proc. Natl. Acad. Sci. USA 77:1922-1926.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 1922-1926
    • Kumagi, I.1    Watanabe, K.2    Oshima, T.3
  • 30
    • 0043205324 scopus 로고    scopus 로고
    • Appendix: Modified nucleosides from RNA
    • D. Söll, S. Nishimura, and P. B. Moore (ed.), Elsevier, Amsterdam, The Netherlands
    • McCloskey, J. A. 2001. Appendix: modified nucleosides from RNA, p. 309-316. In D. Söll, S. Nishimura, and P. B. Moore (ed.), RNA. Elsevier, Amsterdam, The Netherlands.
    • (2001) RNA , pp. 309-316
    • McCloskey, J.A.1
  • 32
    • 0035890653 scopus 로고    scopus 로고
    • Post-transcriptional modification in archaeal tRNAs: Identities and phylogenetic relations of nucleotides from mesophilic and hyperthermophilic Methanococcales
    • McCloskey, J. A., D. E. Graham, S. Zhou, P. F. Crain, M. Ibba, J. Konisky, D. Söll, and G. J. Olsen. 2001. Post-transcriptional modification in archaeal tRNAs: identities and phylogenetic relations of nucleotides from mesophilic and hyperthermophilic Methanococcales. Nucleic Acids Res. 29:4699-4706.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 4699-4706
    • McCloskey, J.A.1    Graham, D.E.2    Zhou, S.3    Crain, P.F.4    Ibba, M.5    Konisky, J.6    Söll, D.7    Olsen, G.J.8
  • 34
    • 0001494356 scopus 로고    scopus 로고
    • Appendix 1: Chemical structures and classification of posttranscriptionally modified nucleosides in RNA
    • H. Grosjean and R. Benne (ed.), ASM Press, Washington, D.C.
    • Motorin, Y., and H. Grosjean. 1998. Appendix 1: chemical structures and classification of posttranscriptionally modified nucleosides in RNA, p. 543-549. In H. Grosjean and R. Benne (ed.), Modification and editing of RNA. ASM Press, Washington, D.C.
    • (1998) Modification and Editing of RNA , pp. 543-549
    • Motorin, Y.1    Grosjean, H.2
  • 35
    • 0001266227 scopus 로고
    • Effect of growth rate and starvation-survival on the viability and stability of a psychrophilic marine bacterium
    • Moyer, C. L., and R. Y. Morita. 1989. Effect of growth rate and starvation-survival on the viability and stability of a psychrophilic marine bacterium. Appl. Environ. Microbiol. 55:1122-1127.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 1122-1127
    • Moyer, C.L.1    Morita, R.Y.2
  • 36
    • 0029902203 scopus 로고    scopus 로고
    • A computer-simulated restriction fragment length polymorphism analysis of bacteria small-subunit rRNA genes: Efficiency of selected tetrameric restriction enzymes for studies of microbial diversity in nature
    • Moyer, C. L., J. M. Tiedje, F. C. Dobbs, and D. M. Karl. 1996. A computer-simulated restriction fragment length polymorphism analysis of bacteria small-subunit rRNA genes: efficiency of selected tetrameric restriction enzymes for studies of microbial diversity in nature. Appl. Environ. Microbiol. 62:2501-2507.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2501-2507
    • Moyer, C.L.1    Tiedje, J.M.2    Dobbs, F.C.3    Karl, D.M.4
  • 37
    • 0032455220 scopus 로고    scopus 로고
    • Posttranscriptional modifications in 16S and 23S rRNAs of the archaeal hyperthermophile Sulfolobus solfataricus
    • Noon, K. R., E. Bruenger, and J. A. McCloskey. 1998. Posttranscriptional modifications in 16S and 23S rRNAs of the archaeal hyperthermophile Sulfolobus solfataricus. J. Bacteriol. 180:2883-2888.
    • (1998) J. Bacteriol. , vol.180 , pp. 2883-2888
    • Noon, K.R.1    Bruenger, E.2    McCloskey, J.A.3
  • 39
    • 0025612935 scopus 로고
    • Analysis of RNA hydrolyzates by LC/MS
    • Pomerantz, S. C., and J. A. McCloskey. 1990. Analysis of RNA hydrolyzates by LC/MS. Methods Enzymol. 193:796-824.
    • (1990) Methods Enzymol. , vol.193 , pp. 796-824
    • Pomerantz, S.C.1    McCloskey, J.A.2
  • 40
    • 0026437551 scopus 로고
    • Structure determination of two new amino acid-containing derivatives of adenosine from tRNA of thermophilic bacteria and archaea
    • Reddy, D. M., P. F. Crain, C. G. Edmonds, R. Gupta, T. Hashizume, K. O. Stetter, F. Widdel, and J. A. McCloskey. 1992. Structure determination of two new amino acid-containing derivatives of adenosine from tRNA of thermophilic bacteria and archaea. Nucleic Acids Res. 20:5607-5614.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 5607-5614
    • Reddy, D.M.1    Crain, P.F.2    Edmonds, C.G.3    Gupta, R.4    Hashizume, T.5    Stetter, K.O.6    Widdel, F.7    McCloskey, J.A.8
  • 43
    • 0023953676 scopus 로고
    • Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro
    • Sampson, J. R., and O. C. Uhlenbeck. 1988. Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro. Proc. Natl. Acad. Sci. USA 85:1033-1037.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1033-1037
    • Sampson, J.R.1    Uhlenbeck, O.C.2
  • 47
    • 0035108129 scopus 로고    scopus 로고
    • Effects of ribosomes and intracellular solutes on activities and stabilities of elongation factor 2 proteins from psychrotolerant and thermophilic methanogens
    • Thomas, T., N. Kumar, and R. Cavicchioli. 2001. Effects of ribosomes and intracellular solutes on activities and stabilities of elongation factor 2 proteins from psychrotolerant and thermophilic methanogens. J. Bacteriol. 183:1974-1982.
    • (2001) J. Bacteriol. , vol.183 , pp. 1974-1982
    • Thomas, T.1    Kumar, N.2    Cavicchioli, R.3
  • 48
    • 0000400795 scopus 로고
    • 6-dimethyladenosine in 16S ribosomal RNA
    • B. Hardesty and G. Kramer (ed.), Springer-Verlag, New York, N.Y.
    • 6-dimethyladenosine in 16S ribosomal RNA, p. 412-424. In B. Hardesty and G. Kramer (ed.), Structure, function, and genetics of ribosomes. Springer-Verlag, New York, N.Y.
    • (1985) Structure, Function, and Genetics of Ribosomes , pp. 412-424
    • Van Knippenberg, P.H.1
  • 49
    • 0021771170 scopus 로고
    • Phylogeny of the conserved 3′ terminal structure of the RNA of small ribosomal subunits
    • van Knippenberg, P. H., J. M. Van Kimmenade, and H. A. Heus. 1984. Phylogeny of the conserved 3′ terminal structure of the RNA of small ribosomal subunits. Nucleic Acids Res. 12:2595-2604.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 2595-2604
    • Van Knippenberg, P.H.1    Van Kimmenade, J.M.2    Heus, H.A.3
  • 50
    • 0018834013 scopus 로고
    • Purification and thermal stability of several amino acid-specific tRNAs from an extreme thermophile, Thermus thermophilus HB8
    • Watanabe, K., T. Oshima, K. Iijima, Z. Yamaizumi, and S. Nishimura. 1980. Purification and thermal stability of several amino acid-specific tRNAs from an extreme thermophile, Thermus thermophilus HB8. J. Biochem. (Tokyo) 87:1-13.
    • (1980) J. Biochem. (Tokyo) , vol.87 , pp. 1-13
    • Watanabe, K.1    Oshima, T.2    Iijima, K.3    Yamaizumi, Z.4    Nishimura, S.5
  • 51
    • 0017173794 scopus 로고
    • Heat-induced stability of tRNA from an extreme thermophile, Thermus thermophilus
    • Watanabe, K., M. Shinma, and T. Oshima. 1976. Heat-induced stability of tRNA from an extreme thermophile, Thermus thermophilus. Biochem. Biophys. Res. Commun. 72:1137-1144.
    • (1976) Biochem. Biophys. Res. Commun. , vol.72 , pp. 1137-1144
    • Watanabe, K.1    Shinma, M.2    Oshima, T.3
  • 52
    • 0026772501 scopus 로고
    • Redox ribonucleosides. Isolation and characterization of 5-hydroxyuridine, 8-hydroxyguanosine and 8-hydroxyadenosine from Torula yeast RNA
    • Yanagawa, H., Y. Ogawa, and M. Ueno. 1992. Redox ribonucleosides. Isolation and characterization of 5-hydroxyuridine, 8-hydroxyguanosine and 8-hydroxyadenosine from Torula yeast RNA. J. Biol. Chem. 267:13320-13326.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13320-13326
    • Yanagawa, H.1    Ogawa, Y.2    Ueno, M.3


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