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Volumn 51, Issue 12, 2012, Pages 2378-2389

Linking energy production and protein synthesis in hydrogenotrophic methanogens

Author keywords

[No Author keywords available]

Indexed keywords

BINDING AFFINITIES; BINDING DETERMINANT; BIOCHEMICAL DATA; CELLULAR RESPONSE; ENERGY PRODUCTIONS; ENVIRONMENTAL CONDITIONS; HYDROGENOTROPHIC METHANOGENS; PARALOGS; PROTEIN SYNTHESIS; PROTEIN TRANSLATION; SYNTHETASES; TERNARY COMPLEX;

EID: 84859205976     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300106p     Document Type: Article
Times cited : (7)

References (49)
  • 1
    • 0036357283 scopus 로고    scopus 로고
    • The unique biochemistry of methanogenesis
    • Deppenmeier, U. (2002) The unique biochemistry of methanogenesis Prog. Nucleic Acid Mol. Biol. 71, 222-283
    • (2002) Prog. Nucleic Acid Mol. Biol. , vol.71 , pp. 222-283
    • Deppenmeier, U.1
  • 2
  • 3
    • 44449149379 scopus 로고    scopus 로고
    • Life close to the thermodynamic limit: How methanogenic archaea conserve energy
    • Deppenmeier, U. and Müller, V. (2008) Life close to the thermodynamic limit: how methanogenic archaea conserve energy Results Probl Cell Differ. 45, 123-152
    • (2008) Results Probl Cell Differ. , vol.45 , pp. 123-152
    • Deppenmeier, U.1    Müller, V.2
  • 4
    • 0001203042 scopus 로고
    • Bioenergetics of methanogenesis
    • (Ferry, J. G. Ed.) pp, Chapman and Hall, New York.
    • Muller, V., Blaut, M., and Gottschalk, G. (1993) Bioenergetics of methanogenesis, in Methanogenesis (Ferry, J. G., Ed.) pp 360-406, Chapman and Hall, New York.
    • (1993) Methanogenesis , pp. 360-406
    • Muller, V.1    Blaut, M.2    Gottschalk, G.3
  • 5
    • 33947380915 scopus 로고    scopus 로고
    • Adaptations to energy stress dictate the ecology and evolution of the Archaea
    • Valentine, D. L. (2007) Adaptations to energy stress dictate the ecology and evolution of the Archaea Nat. Rev. Microbiol. 5, 316-323
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 316-323
    • Valentine, D.L.1
  • 6
    • 0031016808 scopus 로고    scopus 로고
    • Hydrogen regulation of growth, growth yields, and methane gene transcription in Methanobacterium thermoautotrophicum Δh
    • Morgan, R. M., Pihl, T. D., Nölling, J., and Reeve, J. N. (1997) Hydrogen regulation of growth, growth yields, and methane gene transcription in Methanobacterium thermoautotrophicum ΔH J. Bacteriol. 179, 889-898
    • (1997) J. Bacteriol. , vol.179 , pp. 889-898
    • Morgan, R.M.1    Pihl, T.D.2    Nölling, J.3    Reeve, J.N.4
  • 7
    • 0033626511 scopus 로고    scopus 로고
    • 2-forming methylenetetrahydromethanopterin dehydrogenase (Hmd) and of HmdII and HmdIII in Methanothermobacter marburgensis
    • 2-forming methylenetetrahydromethanopterin dehydrogenase (Hmd) and of HmdII and HmdIII in Methanothermobacter marburgensis Arch. Microbiol. 174, 225-232
    • (2000) Arch. Microbiol. , vol.174 , pp. 225-232
    • Afting, C.1    Kremmer, E.2    Brucker, C.3    Hochheimer, A.4    Thauer, R.K.5
  • 8
    • 1842329756 scopus 로고    scopus 로고
    • Methanogenesis: Genes, genomes, and who's on first?
    • Reeve, J. N., Nölling, J., Morgan, R. M., and Smith, D. R. (1997) Methanogenesis: genes, genomes, and who's on first? J. Bacteriol. 179, 5975-5986
    • (1997) J. Bacteriol. , vol.179 , pp. 5975-5986
    • Reeve, J.N.1    Nölling, J.2    Morgan, R.M.3    Smith, D.R.4
  • 9
    • 34547405862 scopus 로고    scopus 로고
    • Functionally distinct genes regulated by hydrogen limitation and growth rate in methanogenic Archaea
    • Hendrickson, E. L., Haydock, A. K., Moore, B. C., Whitman, W. B., and Leigh, J. A. (2007) Functionally distinct genes regulated by hydrogen limitation and growth rate in methanogenic Archaea Proc. Natl. Acad. Sci. U. S. A. 104, 8930-8934
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 8930-8934
    • Hendrickson, E.L.1    Haydock, A.K.2    Moore, B.C.3    Whitman, W.B.4    Leigh, J.A.5
  • 11
    • 0025877458 scopus 로고
    • Activities of formylmethanofuran dehydrogenase, methylenetetrahydromethanopterin dehydrogenase, methylenetetrahydromethanopterin reductase, and heterodisulfide reductase in methanogenic bacteria
    • Schworer, B. and Thauer, R. K. (1991) Activities of formylmethanofuran dehydrogenase, methylenetetrahydromethanopterin dehydrogenase, methylenetetrahydromethanopterin reductase, and heterodisulfide reductase in methanogenic bacteria Arch. Microbiol. 155, 459-465
    • (1991) Arch. Microbiol. , vol.155 , pp. 459-465
    • Schworer, B.1    Thauer, R.K.2
  • 12
    • 0026338480 scopus 로고
    • 420-reducing methylene tetrahydromethanopterin dehydrogenases are genetically distinct enzymes in Methanobacterium thermautotrophicum (Marburg)
    • 420-reducing methylene tetrahydromethanopterin dehydrogenases are genetically distinct enzymes in Methanobacterium thermautotrophicum (Marburg) Eur. J. Biochem. 202, 1205-1208
    • (1991) Eur. J. Biochem. , vol.202 , pp. 1205-1208
    • Von Bunau, R.1    Zirngibl, C.2    Thauer, R.K.3    Klein, A.4
  • 13
    • 0028833512 scopus 로고
    • 420-dependent methylene-5,6,7,8-tetrahydromethanopterin dehydrogenase gene from Methanobacterium thermautotrophicum strain Marburg and functional expression in Escherichia coli
    • 420-dependent methylene-5,6,7,8-tetrahydromethanopterin dehydrogenase gene from Methanobacterium thermautotrophicum strain Marburg and functional expression in Escherichia coli J. Biol. Chem. 270, 2827-2832
    • (1995) J. Biol. Chem. , vol.270 , pp. 2827-2832
    • Mukhopadhyay, B.1    Purwantini, E.2    Pihl, T.D.3    Reeve, J.N.4    Daniels, L.5
  • 14
    • 0031908850 scopus 로고    scopus 로고
    • 420-reducing hydrogenases in Methanosarcina barkeri
    • 420-reducing hydrogenases in Methanosarcina barkeri Arch. Microbiol. 169, 201-205
    • (1998) Arch. Microbiol. , vol.169 , pp. 201-205
    • Vaupel, M.1    Thauer, R.K.2
  • 15
    • 0025014263 scopus 로고
    • 10-methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermautotrophicum has hydrogenase activity
    • 10-methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermautotrophicum has hydrogenase activity FEBS Lett. 261, 112-116
    • (1990) FEBS Lett. , vol.261 , pp. 112-116
    • Zirngibl, C.1    Hedderich, R.2    Thauer, R.K.3
  • 17
    • 47249144402 scopus 로고    scopus 로고
    • 420 and production of hydrogen during methanogenesis
    • 420 and production of hydrogen during methanogenesis J. Bacteriol. 190, 4818-4821
    • (2008) J. Bacteriol. , vol.190 , pp. 4818-4821
    • Hendrickson, E.L.1    Leigh, J.A.2
  • 19
    • 33750086029 scopus 로고    scopus 로고
    • The iron-sulfur cluster-free hydrogenase (Hmd) is a metalloenzyme with a novel iron binding motif
    • Korbas, M., Vogt, S., Meyer-Klaucke, W., Bill, E., Lyon, E. J., and Thauer, R. K. (2006) The iron-sulfur cluster-free hydrogenase (Hmd) is a metalloenzyme with a novel iron binding motif J. Biol. Chem. 281, 30804-30813
    • (2006) J. Biol. Chem. , vol.281 , pp. 30804-30813
    • Korbas, M.1    Vogt, S.2    Meyer-Klaucke, W.3    Bill, E.4    Lyon, E.J.5    Thauer, R.K.6
  • 22
    • 15644383855 scopus 로고    scopus 로고
    • Complete genome sequence of Methanobacterium thermoautotrophicum Δh: Functional analysis and comparatiye genomics
    • Smith, D. R., Doucette-Stamm, L. A., Deloughery, C., Lee, H., Dubois, J., and Aldredge, T. 1997, Complete genome sequence of Methanobacterium thermoautotrophicum ΔH: functional analysis and comparatiye genomics J. Bacteriol. 179, 7135-7155
    • (1997) J. Bacteriol. , vol.179 , pp. 7135-7155
    • Smith, D.R.1    Doucette-Stamm, L.A.2    Deloughery, C.3    Lee, H.4    Dubois, J.5    Aldredge, T.6
  • 23
  • 24
    • 70349322995 scopus 로고    scopus 로고
    • Comprehensive computational analysis of Hmd enzymes and paralogs in methanogenic Archaea
    • Goldman, A. D., Leigh, J. A., and Samudrala, R. (2009) Comprehensive computational analysis of Hmd enzymes and paralogs in methanogenic Archaea BMC Evol. Biol. 9, 199
    • (2009) BMC Evol. Biol. , vol.9 , pp. 199
    • Goldman, A.D.1    Leigh, J.A.2    Samudrala, R.3
  • 25
    • 0034604238 scopus 로고    scopus 로고
    • Synthesis of cysteinyl-tRNA(Cys) by a genome that lacks the normal cysteine-tRNA synthetase
    • Lipman, R. S., Sowers, K. R., and Hou, Y. M. (2000) Synthesis of cysteinyl-tRNA(Cys) by a genome that lacks the normal cysteine-tRNA synthetase Biochemistry 39, 7792-7798
    • (2000) Biochemistry , vol.39 , pp. 7792-7798
    • Lipman, R.S.1    Sowers, K.R.2    Hou, Y.M.3
  • 26
    • 0038408635 scopus 로고    scopus 로고
    • Association of an aminoacyl-tRNA synthetase with a putative metabolic protein in archaea
    • Lipman, R. S. A., Chen, J., Evilia, C., Vitseva, O., and Hou, Y.-M. (2003) Association of an aminoacyl-tRNA synthetase with a putative metabolic protein in archaea Biochemistry 42, 7487-7496
    • (2003) Biochemistry , vol.42 , pp. 7487-7496
    • Lipman, R.S.A.1    Chen, J.2    Evilia, C.3    Vitseva, O.4    Hou, Y.-M.5
  • 27
    • 44749086081 scopus 로고    scopus 로고
    • Structural and functional mapping of the archaeal multi-aminoacyl-tRNA synthetase complex
    • Hausmann, C. D. and Ibba, M. (2008) Structural and functional mapping of the archaeal multi-aminoacyl-tRNA synthetase complex FEBS Lett. 582, 2178-2182
    • (2008) FEBS Lett. , vol.582 , pp. 2178-2182
    • Hausmann, C.D.1    Ibba, M.2
  • 28
    • 35548983465 scopus 로고    scopus 로고
    • An aminoacyl-tRNA synthetase:elongation factor complex for substrate channeling in archaeal translation
    • Praetorius-Ibba, M., Hausmann, C. D., Paras, M., Rogers, T. E., and Ibba, M. (2007) An aminoacyl-tRNA synthetase:elongation factor complex for substrate channeling in archaeal translation Nucleic Acids Res. 35, 6094-6102
    • (2007) Nucleic Acids Res. , vol.35 , pp. 6094-6102
    • Praetorius-Ibba, M.1    Hausmann, C.D.2    Paras, M.3    Rogers, T.E.4    Ibba, M.5
  • 29
    • 77956095201 scopus 로고    scopus 로고
    • New functions of aminoacyl-tRNA synthetases beyond translation
    • Guo, M., Yang, X.-L., and Schimmel, P. (2010) New functions of aminoacyl-tRNA synthetases beyond translation Nat. Rev. Mol. Cell Biol. 11, 668-674
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 668-674
    • Guo, M.1    Yang, X.-L.2    Schimmel, P.3
  • 34
    • 79956133928 scopus 로고    scopus 로고
    • The design involved in PapI and Lrp regulation of the pap operon
    • Kawamura, T., Vartanian, A. S., Zhou, H., and Dahlquist, F. W. (2011) The design involved in PapI and Lrp regulation of the pap operon J. Mol. Biol. 409, 311-332
    • (2011) J. Mol. Biol. , vol.409 , pp. 311-332
    • Kawamura, T.1    Vartanian, A.S.2    Zhou, H.3    Dahlquist, F.W.4
  • 35
    • 0028817155 scopus 로고
    • Validity of nucleic acid purities monitored by 260nm/280nm absorbance ratios
    • Glasel, J. A. (1995) Validity of nucleic acid purities monitored by 260nm/280nm absorbance ratios BioTechniques 18, 62-63
    • (1995) BioTechniques , vol.18 , pp. 62-63
    • Glasel, J.A.1
  • 36
    • 34547585449 scopus 로고    scopus 로고
    • Determination of refractive index increment ratios for protein-nucleic acid complexes by surface plasmon resonance
    • Di Primo, C. and Lebars, I. (2007) Determination of refractive index increment ratios for protein-nucleic acid complexes by surface plasmon resonance Anal. Biochem. 368, 148-155
    • (2007) Anal. Biochem. , vol.368 , pp. 148-155
    • Di Primo, C.1    Lebars, I.2
  • 37
    • 77955235194 scopus 로고    scopus 로고
    • Synthesis of Glu-tRNA(Gln) by engineered and natural aminoacyl-tRNA synthetases
    • Rodríguez-Hernández, A., Bhaskaran, H., Hadd, A., and Perona, J. J. (2010) Synthesis of Glu-tRNA(Gln) by engineered and natural aminoacyl-tRNA synthetases Biochemistry 49, 6727-6736
    • (2010) Biochemistry , vol.49 , pp. 6727-6736
    • Rodríguez-Hernández, A.1    Bhaskaran, H.2    Hadd, A.3    Perona, J.J.4
  • 38
    • 39549086795 scopus 로고    scopus 로고
    • Mobility shift DNA-binding assay using gel electrophoresis
    • (Ausubel, F. M. Eds.) Chapter 12, Unit 12.2.
    • Buratowski, S. and Chodosh, L. A. (2001) Mobility shift DNA-binding assay using gel electrophoresis, in Current Protocols in Molecular Biology (Ausubel, F. M., Eds.) Chapter 12, Unit 12.2.
    • (2001) Current Protocols in Molecular Biology
    • Buratowski, S.1    Chodosh, L.A.2
  • 39
    • 0028934572 scopus 로고
    • Fluorescence anisotropy applied to biomolecular interactions
    • Jameson, D. M. and Sawyer, W. H. (1995) Fluorescence anisotropy applied to biomolecular interactions Methods Enzymol. 246, 283-300
    • (1995) Methods Enzymol. , vol.246 , pp. 283-300
    • Jameson, D.M.1    Sawyer, W.H.2
  • 40
    • 0033582291 scopus 로고    scopus 로고
    • Intra-tRNA distance measurements for nucleocapsid protein-dependent tRNA unwinding during priming of HIV reverse transcription
    • Chan, B., Weidemaier, K., Yip, W. T., Barbara, P. F., and Musier-Forsyth, K. (1999) Intra-tRNA distance measurements for nucleocapsid protein-dependent tRNA unwinding during priming of HIV reverse transcription Proc. Natl. Acad. Sci. U. S. A. 96, 459-464
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 459-464
    • Chan, B.1    Weidemaier, K.2    Yip, W.T.3    Barbara, P.F.4    Musier-Forsyth, K.5
  • 41
    • 39049099984 scopus 로고    scopus 로고
    • Methods for the study of strictly anaerobic microorganisms
    • (Oren, F. A. R. a. A. Ed.) Vol. Elsevier/Academic Press, Oxford.
    • Sowers, K. R. and Watts, J. E. M. (2006) Methods for the study of strictly anaerobic microorganisms, in Methods in Microbiology (Oren, F. A. R. a. A., Ed.) Vol. 35, Elsevier/Academic Press, Oxford.
    • (2006) Methods in Microbiology , vol.35
    • Sowers, K.R.1    Watts, J.E.M.2
  • 42
    • 0032731169 scopus 로고    scopus 로고
    • Reactor-scale cultivation of the hyperthermophilic methanarchaeon Methanococcus jannaschii to high cell densities
    • Mukhopadhyay, B., Johnson, E. F., and Wolfe, R. S. (1999) Reactor-scale cultivation of the hyperthermophilic methanarchaeon Methanococcus jannaschii to high cell densities Appl. Environ. Microbiol. 65, 5059-5065
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 5059-5065
    • Mukhopadhyay, B.1    Johnson, E.F.2    Wolfe, R.S.3
  • 43
    • 77951276163 scopus 로고    scopus 로고
    • Optimization of the hybridization-based method for purification of thermostable tRNAs in the presence of tetraalkylammonium salts
    • Yokogawa, T., Kitamura, Y., Nakamura, D., Ohno, S., and Nishikawa, K. (2010) Optimization of the hybridization-based method for purification of thermostable tRNAs in the presence of tetraalkylammonium salts Nucleic Acids Res. 38, e89
    • (2010) Nucleic Acids Res. , vol.38 , pp. 89
    • Yokogawa, T.1    Kitamura, Y.2    Nakamura, D.3    Ohno, S.4    Nishikawa, K.5
  • 44
    • 38649136232 scopus 로고    scopus 로고
    • Methods for kinetic and thermodynamic analysis of aminoacyl-tRNA synthetases
    • Francklyn, C. S., First, E. A., Perona, J. J., and Hou, Y.-M. (2008) Methods for kinetic and thermodynamic analysis of aminoacyl-tRNA synthetases Methods 44, 100-118
    • (2008) Methods , vol.44 , pp. 100-118
    • Francklyn, C.S.1    First, E.A.2    Perona, J.J.3    Hou, Y.-M.4
  • 47
    • 0004040064 scopus 로고    scopus 로고
    • 2 nd ed. pp, Kluwer Academic/Plenum Publishers, New York.
    • Lakowicz, J. R. (1999) Principles of Fluorescence Spectroscopy, 2 nd ed., pp 291-319, Kluwer Academic/Plenum Publishers, New York.
    • (1999) Principles of Fluorescence Spectroscopy , pp. 291-319
    • Lakowicz, J.R.1


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