메뉴 건너뛰기




Volumn 186, Issue 20, 2004, Pages 6956-6969

Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis

(31)  Hendrickson, E L b   Kaul, R a,b   Zhou, Y b   Bovee, D b   Chapman, P b   Chung, J b   De Macario, E Conway e   Dodsworth, J A b   Gillett, W b   Graham, D E f   Hackett, M c   Haydock, A K b   Kang, A b   Land, M L g   Levy, R b   Lie, T J b   Major, T A h   Moore, B C b   Porat, I h   Palmeiri, A b   more..


Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ALANINE DEHYDROGENASE; ALANINE RACEMASE; CELL CYCLE PROTEIN 6; CYSTEINE; GENE PRODUCT; HYDROGENASE; IRON SULFUR PROTEIN; NITROGEN; PEPTIDE DERIVATIVE; RIBONUCLEASE H; RNASE HII; SELENOCYSTEINE; UNCLASSIFIED DRUG;

EID: 4944254822     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.20.6956-6969.2004     Document Type: Article
Times cited : (179)

References (128)
  • 1
    • 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
  • 2
    • 0031437603 scopus 로고    scopus 로고
    • Bacterial chemotaxis: Rhodobacter sphaeroides and Sinorhizobium meliloti - Variations on a theme?
    • Armitage, J. P., and R. Schmitt. 1997. Bacterial chemotaxis: Rhodobacter sphaeroides and Sinorhizobium meliloti - variations on a theme? Microbiology 143:3671-3682.
    • (1997) Microbiology , vol.143 , pp. 3671-3682
    • Armitage, J.P.1    Schmitt, R.2
  • 4
    • 0021245679 scopus 로고
    • Lysine biosynthesis in Methanobacterium thermoautotrophicum is by the diaminopimelic acid pathway
    • Bakhiet, N., F. W. Forney, D. P. Stahly, and L. Daniels. 1984. Lysine biosynthesis in Methanobacterium thermoautotrophicum is by the diaminopimelic acid pathway. Curr. Microbiol. 10:195-198.
    • (1984) Curr. Microbiol. , vol.10 , pp. 195-198
    • Bakhiet, N.1    Forney, F.W.2    Stahly, D.P.3    Daniels, L.4
  • 5
    • 0032102006 scopus 로고    scopus 로고
    • Transcription and translation in Archaea: A mosaic of eukaryal and bacterial features
    • Bell, S. D., and S. P. Jackson. 1998. Transcription and translation in Archaea: a mosaic of eukaryal and bacterial features. Trends Microbiol. 6:222-228.
    • (1998) Trends Microbiol. , vol.6 , pp. 222-228
    • Bell, S.D.1    Jackson, S.P.2
  • 6
    • 0028198145 scopus 로고
    • Selenium is involved in the negative regulation of the expression of selenium-free [NiFe] hydrogenases in Methanococcus voltae
    • Berghofer, Y., K. Agha-Amiri, and A. Klein. 1994. Selenium is involved in the negative regulation of the expression of selenium-free [NiFe] hydrogenases in Methanococcus voltae. Mol. Gen. Genet. 242:369-373.
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 369-373
    • Berghofer, Y.1    Agha-Amiri, K.2    Klein, A.3
  • 7
    • 0031844818 scopus 로고    scopus 로고
    • Archaea and the cell cycle
    • Bernander, R. 1998. Archaea and the cell cycle. Mol. Microbiol. 29:955-961.
    • (1998) Mol. Microbiol. , vol.29 , pp. 955-961
    • Bernander, R.1
  • 8
    • 0038687976 scopus 로고    scopus 로고
    • The archaeal cell cycle: Current issues
    • Bernander, R. 2003. The archaeal cell cycle: current issues. Mol. Microbiol. 48:599-604.
    • (2003) Mol. Microbiol. , vol.48 , pp. 599-604
    • Bernander, R.1
  • 9
    • 0034212268 scopus 로고    scopus 로고
    • Chromosome replication, nucleoid segregation and cell division in archaea
    • Bernander, R. 2000. Chromosome replication, nucleoid segregation and cell division in archaea. Trends Microbiol. 8:278-283.
    • (2000) Trends Microbiol. , vol.8 , pp. 278-283
    • Bernander, R.1
  • 10
    • 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., R. Ortenberg, and M. Mevarech. 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
  • 11
    • 0035916786 scopus 로고    scopus 로고
    • Archaeal primase: Bridging the gap between RNA and DNA polymerases
    • Bocquier, A. A., L. Liu, I. K. Cann, K. Komori, D. Kohda, and Y. Ishino. 2001. Archaeal primase: bridging the gap between RNA and DNA polymerases. Curr. Biol. 11:452-456.
    • (2001) Curr. Biol. , vol.11 , pp. 452-456
    • Bocquier, A.A.1    Liu, L.2    Cann, I.K.3    Komori, K.4    Kohda, D.5    Ishino, Y.6
  • 14
    • 0035235980 scopus 로고    scopus 로고
    • The emerging periplasm-localized subclass of AroQ chorismate mutases, exemplified by those from Salmonella typhimurium and Pseudomonas aeruginosa
    • RESEARCH0030.1-30.16
    • Calhoun, D. H., C. A. Bonner, W. Gu, G. Xie, and R. A. Jensen. 2001. The emerging periplasm-localized subclass of AroQ chorismate mutases, exemplified by those from Salmonella typhimurium and Pseudomonas aeruginosa. Genome Biol. 2:RESEARCH0030.1-30.16.
    • (2001) Genome Biol. , vol.2
    • Calhoun, D.H.1    Bonner, C.A.2    Gu, W.3    Xie, G.4    Jensen, R.A.5
  • 15
    • 0032899732 scopus 로고    scopus 로고
    • Function and regulation of glnA in the methanogenic archaeon Methanococcus maripaludis
    • Cohen-Kupiec, R., C. J. Marx, and J. A. Leigh. 1999. Function and regulation of glnA in the methanogenic archaeon Methanococcus maripaludis. J. Bacteriol. 181:256-261.
    • (1999) J. Bacteriol. , vol.181 , pp. 256-261
    • Cohen-Kupiec, R.1    Marx, C.J.2    Leigh, J.A.3
  • 16
    • 0025296152 scopus 로고
    • Characterization of a gene involved in histidine biosynthesis in Halobacterium (Haloferax) volcanii: Isolation and rapid mapping by transformation of an auxotroph with cosmid DNA
    • Conover, R. K., and W. F. Doolittle. 1990. Characterization of a gene involved in histidine biosynthesis in Halobacterium (Haloferax) volcanii: isolation and rapid mapping by transformation of an auxotroph with cosmid DNA. J. Bacteriol. 172:3244-3249.
    • (1990) J. Bacteriol. , vol.172 , pp. 3244-3249
    • Conover, R.K.1    Doolittle, W.F.2
  • 17
    • 0035180870 scopus 로고    scopus 로고
    • Archaeal shikimate kinase, a new member of the GHMP-kinase family
    • Daugherty, M., V. Vonstein, R. Overbeek, and A. Osterman. 2001. Archaeal shikimate kinase, a new member of the GHMP-kinase family. J. Bacteriol. 183:292-300.
    • (2001) J. Bacteriol. , vol.183 , pp. 292-300
    • Daugherty, M.1    Vonstein, V.2    Overbeek, R.3    Osterman, A.4
  • 20
    • 0012017744 scopus 로고
    • Biosynthesis of isoleucine in methanogenic bacteria: A 13C NMR study
    • Ekiel, I., I. C. P. Smith, and G. D. Sprott. 1984. Biosynthesis of isoleucine in methanogenic bacteria: a 13C NMR study. Biochemistry 23:1683-1687.
    • (1984) Biochemistry , vol.23 , pp. 1683-1687
    • Ekiel, I.1    Smith, I.C.P.2    Sprott, G.D.3
  • 21
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectra of peptides with amino acid sequences in a protein database
    • Eng, J. K., A. L. McCormack, and J. R. Yates. 1994. An approach to correlate tandem mass spectra of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 5:976-989.
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.3
  • 22
    • 0031978181 scopus 로고    scopus 로고
    • Base-calling of automated sequencer traces using phred. II. Error probabilities
    • Ewing, B., and P. Green. 1998. Base-calling of automated sequencer traces using phred. II. Error probabilities. Genome Res. 8:186-194.
    • (1998) Genome Res. , vol.8 , pp. 186-194
    • Ewing, B.1    Green, P.2
  • 23
    • 0029117343 scopus 로고
    • glmS of Thermus thermophilus HB8: An essential gene for cell-wall synthesis identified immediately upstream of the S-layer gene
    • Fernandez-Herrero, L. A., M. A. Badet-Denisot, B. Badet, and J. Berenguer. 1995. glmS of Thermus thermophilus HB8: an essential gene for cell-wall synthesis identified immediately upstream of the S-layer gene. Mol. Microbiol. 17:1-12.
    • (1995) Mol. Microbiol. , vol.17 , pp. 1-12
    • Fernandez-Herrero, L.A.1    Badet-Denisot, M.A.2    Badet, B.3    Berenguer, J.4
  • 25
    • 0038643328 scopus 로고    scopus 로고
    • Synthesis of catalytically active form III ribulose 1,5-bisphosphate carboxylase/oxygenase in archaea
    • Finn, M. W., and F. R. Tabita. 2003. Synthesis of catalytically active form III ribulose 1,5-bisphosphate carboxylase/oxygenase in archaea. J. Bacteriol. 185:3049-3059.
    • (2003) J. Bacteriol. , vol.185 , pp. 3049-3059
    • Finn, M.W.1    Tabita, F.R.2
  • 27
    • 0036715039 scopus 로고    scopus 로고
    • Evolutionary conservation of reactions in translation
    • Ganoza, M. C., M. C. Kiel, and H. Aoki. 2002. Evolutionary conservation of reactions in translation. Microbiol. Mol. Biol. Rev. 66:460-485.
    • (2002) Microbiol. Mol. Biol. Rev. , vol.66 , pp. 460-485
    • Ganoza, M.C.1    Kiel, M.C.2    Aoki, H.3
  • 28
    • 0344855596 scopus 로고    scopus 로고
    • Expression vectors for Methanococcus maripaludis: Overexpression of acetohydroxyacid synthase and beta-galactosidase
    • Gardner, W. L., and W. B. Whitman. 1999. Expression vectors for Methanococcus maripaludis: overexpression of acetohydroxyacid synthase and beta-galactosidase. Genetics 152:1439-1447.
    • (1999) Genetics , vol.152 , pp. 1439-1447
    • Gardner, W.L.1    Whitman, W.B.2
  • 29
    • 0036192533 scopus 로고    scopus 로고
    • The parAB gene products of Pseudomonas putida exhibit partition activity in both P. putida and Escherichia coli
    • Godfrin-Estevenon, A. M., F. Pasta, and D. Lane. 2002. The parAB gene products of Pseudomonas putida exhibit partition activity in both P. putida and Escherichia coli. Mol. Microbiol. 43:39-49.
    • (2002) Mol. Microbiol. , vol.43 , pp. 39-49
    • Godfrin-Estevenon, A.M.1    Pasta, F.2    Lane, D.3
  • 30
    • 0035054380 scopus 로고    scopus 로고
    • Automated finishing with autofinish
    • Gordon, D., C. Desmarais, and P. Green. 2001. Automated finishing with autofinish. Genome Res. 11:614-625.
    • (2001) Genome Res. , vol.11 , pp. 614-625
    • Gordon, D.1    Desmarais, C.2    Green, P.3
  • 32
    • 0036005602 scopus 로고    scopus 로고
    • Elucidation of methanogenic coenzyme biosyntheses: From spectroscopy to genomics
    • Graham, D. E., and R. H. White. 2002. Elucidation of methanogenic coenzyme biosyntheses: from spectroscopy to genomics. Nat. Prod. Rep. 19:133-147.
    • (2002) Nat. Prod. Rep. , vol.19 , pp. 133-147
    • Graham, D.E.1    White, R.H.2
  • 33
    • 0037165614 scopus 로고    scopus 로고
    • A divergent archaeal member of the alkaline phosphatase binuclear metalloenzyme superfamily has phosphoglycerate mutase activity
    • Graham, D. E., H. Xu, and R. H. White. 2002. A divergent archaeal member of the alkaline phosphatase binuclear metalloenzyme superfamily has phosphoglycerate mutase activity. FEBS Lett. 517:190-194.
    • (2002) FEBS Lett. , vol.517 , pp. 190-194
    • Graham, D.E.1    Xu, H.2    White, R.H.3
  • 34
    • 0034891038 scopus 로고    scopus 로고
    • Methanococcus jannaschii generates L-proline by cyclization of L-ornithine
    • Graupner, M., and R. H. White. 2001. Methanococcus jannaschii generates L-proline by cyclization of L-ornithine. J. Bacteriol. 183:5203-5205.
    • (2001) J. Bacteriol. , vol.183 , pp. 5203-5205
    • Graupner, M.1    White, R.H.2
  • 35
    • 0036177599 scopus 로고    scopus 로고
    • New class of IMP cyclohydrolases in Methanococcus jannaschii
    • Graupner, M., H. Xu, and R. H. White. 2002. New class of IMP cyclohydrolases in Methanococcus jannaschii. J. Bacteriol. 184:1471-1473.
    • (2002) J. Bacteriol. , vol.184 , pp. 1471-1473
    • Graupner, M.1    Xu, H.2    White, R.H.3
  • 36
    • 0033616712 scopus 로고    scopus 로고
    • Thermal adaptation analyzed by comparison of protein sequences from mesophilic and extremely thermophilic Methanococcus species
    • Haney, P. J., J. H. Badger, G. L. Buldak, C. I. Reich, C. R. Woese, and G. J. Olsen. 1999. Thermal adaptation analyzed by comparison of protein sequences from mesophilic and extremely thermophilic Methanococcus species. Proc. Natl. Acad. Sci. USA 96:3578-3583.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3578-3583
    • Haney, P.J.1    Badger, J.H.2    Buldak, G.L.3    Reich, C.I.4    Woese, C.R.5    Olsen, G.J.6
  • 37
    • 4444244015 scopus 로고    scopus 로고
    • Continuous culture of Methanococcus maripaludis under defined nutrient conditions
    • a. Haydock, A. K., I. Porat, W. B. Whitman, and J. A. Leigh. 2004. Continuous culture of Methanococcus maripaludis under defined nutrient conditions. FEMS Microbiol. Lett. 238:85-91.
    • (2004) FEMS Microbiol. Lett. , vol.238 , pp. 85-91
    • Haydock, A.K.1    Porat, I.2    Whitman, W.B.3    Leigh, J.A.4
  • 38
    • 0028136101 scopus 로고
    • The heterodisulfide reductase from Methanobacterium thermoautotrophicum contains sequence motifs characteristic of pyridine-nucleotide-dependent thioredoxin reductases
    • Hedderich, R., J. Koch, D. Linder, and R. K. Thauer. 1994. The heterodisulfide reductase from Methanobacterium thermoautotrophicum contains sequence motifs characteristic of pyridine-nucleotide-dependent thioredoxin reductases. Eur. J. Biochem. 225:253-261.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 253-261
    • Hedderich, R.1    Koch, J.2    Linder, D.3    Thauer, R.K.4
  • 39
    • 0036048625 scopus 로고    scopus 로고
    • Transcription in the archaea: Basal factors, regulation, and stress-gene expression
    • Hickey, A. J., E. Conway de Macario, and A. J. L. Macario. 2002. Transcription in the archaea: basal factors, regulation, and stress-gene expression. Crit. Rev. Biochem. Mol. Biol. 37:537-599.
    • (2002) Crit. Rev. Biochem. Mol. Biol. , vol.37 , pp. 537-599
    • Hickey, A.J.1    Conway De Macario, E.2    Macario, A.J.L.3
  • 40
    • 2942597013 scopus 로고    scopus 로고
    • Comparison of pathways for amino acid biosynthesis in archaebacteria using their genomic DNA sequences
    • Higuchi, S., T. Kawashima, and M. Suzuki. 1999. Comparison of pathways for amino acid biosynthesis in archaebacteria using their genomic DNA sequences. Proc. Jpn. Acad. 75:241-245.
    • (1999) Proc. Jpn. Acad. , vol.75 , pp. 241-245
    • Higuchi, S.1    Kawashima, T.2    Suzuki, M.3
  • 41
    • 0031664705 scopus 로고    scopus 로고
    • The formylmethanofuran dehydrogenase isoenzymes in Methanobacterium wolfei and Methanobacterium thermoautotrophicum: Induction of the molybdenum isoenzyme by molybdate and constitutive synthesis of the tungsten isoenzyme
    • Hochheimer, A., R. Hedderich, and R. K. Thauer. 1998. The formylmethanofuran dehydrogenase isoenzymes in Methanobacterium wolfei and Methanobacterium thermoautotrophicum: induction of the molybdenum isoenzyme by molybdate and constitutive synthesis of the tungsten isoenzyme. Arch. Microbiol. 170:389-393.
    • (1998) Arch. Microbiol. , vol.170 , pp. 389-393
    • Hochheimer, A.1    Hedderich, R.2    Thauer, R.K.3
  • 42
    • 0029989411 scopus 로고    scopus 로고
    • The molybdenum formylmethanofuran dehydrogenase operon and the tungsten formylmethanofuran dehydrogenase operon from Methanobacterium thermoautotrophicum. Structures and transcriptional regulation
    • Hochheimer, A., D. Linder, R. K. Thauer, and R. Hedderich. 1996. The molybdenum formylmethanofuran dehydrogenase operon and the tungsten formylmethanofuran dehydrogenase operon from Methanobacterium thermoautotrophicum. Structures and transcriptional regulation. Eur. J. Biochem. 242:156-162.
    • (1996) Eur. J. Biochem. , vol.242 , pp. 156-162
    • Hochheimer, A.1    Linder, D.2    Thauer, R.K.3    Hedderich, R.4
  • 43
    • 0032516466 scopus 로고    scopus 로고
    • Alpha-keto acid chain elongation reactions involved in the biosynthesis of coenzyme B (7-mercaptoheptanoyl threonine phosphate) in methanogenic archaea
    • Howell, D. M., K. Harich, H. Xu, and R. H. White. 1998. Alpha-keto acid chain elongation reactions involved in the biosynthesis of coenzyme B (7-mercaptoheptanoyl threonine phosphate) in methanogenic archaea. Biochemistry 37:10108-10117.
    • (1998) Biochemistry , vol.37 , pp. 10108-10117
    • Howell, D.M.1    Harich, K.2    Xu, H.3    White, R.H.4
  • 44
    • 0032924783 scopus 로고    scopus 로고
    • (R)-Citramalate synthase in methanogenic archaea
    • Howell, D. M., H. Xu, and R. H. White. 1999. (R)-Citramalate synthase in methanogenic archaea. J. Bacteriol. 181:331-333.
    • (1999) J. Bacteriol. , vol.181 , pp. 331-333
    • Howell, D.M.1    Xu, H.2    White, R.H.3
  • 45
    • 0037076380 scopus 로고    scopus 로고
    • Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE
    • Hu, Z., E. P. Gogol, and J. Lutkenhaus. 2002. Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE. Proc. Natl. Acad. Sci. USA 99:6761-6766.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6761-6766
    • Hu, Z.1    Gogol, E.P.2    Lutkenhaus, J.3
  • 46
    • 0032415809 scopus 로고    scopus 로고
    • The euryarchaeotes, a subdomain of Archaea, survive on a single DNA polymerase: Fact or farce?
    • Ishino, Y., and I. K. Cann. 1998. The euryarchaeotes, a subdomain of Archaea, survive on a single DNA polymerase: fact or farce? Genes Genet. Syst. 73:323-336.
    • (1998) Genes Genet. Syst. , vol.73 , pp. 323-336
    • Ishino, Y.1    Cann, I.K.2
  • 47
    • 0035914323 scopus 로고    scopus 로고
    • Purification and characterization of membrane-associated CooC protein and its functional role in the insertion of nickel into carbon monoxide dehydrogenase from Rhodospirillum rubrum
    • Jeon, W. B., J. Cheng, and P. W. Ludden. 2001. Purification and characterization of membrane-associated CooC protein and its functional role in the insertion of nickel into carbon monoxide dehydrogenase from Rhodospirillum rubrum. J. Biol. Chem. 276:38602-38609.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38602-38609
    • Jeon, W.B.1    Cheng, J.2    Ludden, P.W.3
  • 48
    • 0019497185 scopus 로고
    • Selenium-dependent and selenium-independent formate dehydrogenases of Methanococcus vannielii. Separation of the two forms and characterization of the purified selenium-independent form
    • Jones, J. B., and T. C. Stadtman. 1981. Selenium-dependent and selenium-independent formate dehydrogenases of Methanococcus vannielii. Separation of the two forms and characterization of the purified selenium-independent form. J. Biol. Chem. 256:656-663.
    • (1981) J. Biol. Chem. , vol.256 , pp. 656-663
    • Jones, J.B.1    Stadtman, T.C.2
  • 49
    • 0002620715 scopus 로고
    • Characterization of Methanococcus maripaludis sp. nov., a new methanogen isolated from salt marsh sediment
    • Jones, W. J., M. J. B. Paynter, and R. Gupta. 1983. Characterization of Methanococcus maripaludis sp. nov., a new methanogen isolated from salt marsh sediment. Arch. Microbiol. 135:91-97.
    • (1983) Arch. Microbiol. , vol.135 , pp. 91-97
    • Jones, W.J.1    Paynter, M.J.B.2    Gupta, R.3
  • 51
    • 0025833831 scopus 로고
    • Cloning and sequencing of a multigene family encoding the flagellins of Methanococcus voltae
    • Kalmokoff, M. L., and K. F. Jarrell. 1991. Cloning and sequencing of a multigene family encoding the flagellins of Methanococcus voltae. J. Bacteriol. 173:7113-7125.
    • (1991) J. Bacteriol. , vol.173 , pp. 7113-7125
    • Kalmokoff, M.L.1    Jarrell, K.F.2
  • 52
    • 0031895257 scopus 로고    scopus 로고
    • The nif gene operon of the methanogenic archaeon Methanococcus maripaludis
    • Kessler, P. S., C. Blank, and J. A. Leigh. 1998. The nif gene operon of the methanogenic archaeon Methanococcus maripaludis. J. Bacteriol. 180:1504-1511.
    • (1998) J. Bacteriol. , vol.180 , pp. 1504-1511
    • Kessler, P.S.1    Blank, C.2    Leigh, J.A.3
  • 54
    • 0344289523 scopus 로고    scopus 로고
    • Genetics of nitrogen regulation in Methanococcus maripaludis
    • Kessler, P. S., and J. A. Leigh. 1999. Genetics of nitrogen regulation in Methanococcus maripaludis. Genetics 152:1343-1351.
    • (1999) Genetics , vol.152 , pp. 1343-1351
    • Kessler, P.S.1    Leigh, J.A.2
  • 55
    • 0032560551 scopus 로고    scopus 로고
    • The thermosome: Archetype of group II chaperonins
    • Klumpp, M., and W. Baumeister. 1998. The thermosome: archetype of group II chaperonins. FEBS Lett. 430:73-77.
    • (1998) FEBS Lett. , vol.430 , pp. 73-77
    • Klumpp, M.1    Baumeister, W.2
  • 56
    • 22844456742 scopus 로고    scopus 로고
    • Enzymes identified using genomic DNA sequences suggest some typical characteristics of de novo biosynthesis of purines in archaebacteria
    • Koike, H., T. Kawashima, and M. Suzuki. 1999. Enzymes identified using genomic DNA sequences suggest some typical characteristics of de novo biosynthesis of purines in archaebacteria. Proc. Jpn. Acad. 75:263-268.
    • (1999) Proc. Jpn. Acad. , vol.75 , pp. 263-268
    • Koike, H.1    Kawashima, T.2    Suzuki, M.3
  • 57
    • 0035854709 scopus 로고    scopus 로고
    • Replication protein A in Pyrococcus furiosus is involved in homologous DNA recombination
    • Komori, K., and Y. Ishino. 2001. Replication protein A in Pyrococcus furiosus is involved in homologous DNA recombination. J. Biol. Chem. 276:25654-25660.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25654-25660
    • Komori, K.1    Ishino, Y.2
  • 58
    • 0033529916 scopus 로고    scopus 로고
    • A Holliday junction resolvase from Pyrococcus furiosus: Functional similarity to Escherichia coli RuvC provides evidence for conserved mechanism of homologous recombination in Bacteria, Eukarya, and Archaea
    • Komori, K., S. Sakae, H. Shinagawa, K. Morikawa, and Y. Ishino. 1999. A Holliday junction resolvase from Pyrococcus furiosus: functional similarity to Escherichia coli RuvC provides evidence for conserved mechanism of homologous recombination in Bacteria, Eukarya, and Archaea. Proc. Natl. Acad. Sci. USA 96:8873-8878.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8873-8878
    • Komori, K.1    Sakae, S.2    Shinagawa, H.3    Morikawa, K.4    Ishino, Y.5
  • 59
    • 0034662744 scopus 로고    scopus 로고
    • Crystal structure of archaeal RNase HII: A homologue of human major RNase H
    • Lai, L., H. Yokota, L. W. Hung, R. Kim, and S. H. Kim. 2000. Crystal structure of archaeal RNase HII: a homologue of human major RNase H. Struct. Fold Des. 8:897-904.
    • (2000) Struct. Fold Des. , vol.8 , pp. 897-904
    • Lai, L.1    Yokota, H.2    Hung, L.W.3    Kim, R.4    Kim, S.H.5
  • 60
    • 0033534161 scopus 로고    scopus 로고
    • Three-dimensional structure of Escherichia coli asparagine synthetase B: A short journey from substrate to product
    • Larsen, T. M., S. K. Boehlein, S. M. Schuster, N. G. Richards, J. B. Thoden, H. M. Holden, and I. Rayment. 1999. Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product. Biochemistry 38:16146-16157.
    • (1999) Biochemistry , vol.38 , pp. 16146-16157
    • Larsen, T.M.1    Boehlein, S.K.2    Schuster, S.M.3    Richards, N.G.4    Thoden, J.B.5    Holden, H.M.6    Rayment, I.7
  • 61
    • 0029122698 scopus 로고
    • Membrane fusion and the cell cycle: Cdc48p participates in the fusion of ER membranes
    • Latterich, M., K. U. Frohlich, and R. Schekman. 1995. Membrane fusion and the cell cycle: Cdc48p participates in the fusion of ER membranes. Cell 82:885-893.
    • (1995) Cell , vol.82 , pp. 885-893
    • Latterich, M.1    Frohlich, K.U.2    Schekman, R.3
  • 62
    • 0242440314 scopus 로고    scopus 로고
    • Gene organization: Selection, selfishness, and serendipity
    • Lawrence, J. G. 2003. Gene organization: selection, selfishness, and serendipity. Annu. Rev. Microbiol. 57:419-440.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 419-440
    • Lawrence, J.G.1
  • 63
    • 0035012849 scopus 로고    scopus 로고
    • Initiating DNA synthesis: From recruiting to activating the MCM complex
    • Lei, M., and B. K. Tye. 2001. Initiating DNA synthesis: from recruiting to activating the MCM complex. J. Cell Sci. 114:1447-1454.
    • (2001) J. Cell Sci. , vol.114 , pp. 1447-1454
    • Lei, M.1    Tye, B.K.2
  • 65
    • 0037837811 scopus 로고    scopus 로고
    • The Methanococcus jannaschii dCTP deaminase is a bifunctional deaminase and diphosphatase
    • Li, H., H. Xu, D. E. Graham, and R. H. White. 2003. The Methanococcus jannaschii dCTP deaminase is a bifunctional deaminase and diphosphatase. J. Biol. Chem. 278:11100-11106.
    • (2003) J. Biol. Chem. , vol.278 , pp. 11100-11106
    • Li, H.1    Xu, H.2    Graham, D.E.3    White, R.H.4
  • 66
    • 0037221867 scopus 로고    scopus 로고
    • A novel repressor of nif and glnA expression in the methanogenic archaeon Methanococcus maripaludis
    • Lie, T. J., and J. A. Leigh. 2003. A novel repressor of nif and glnA expression in the methanogenic archaeon Methanococcus maripaludis. Mol. Microbiol. 47:235-246.
    • (2003) Mol. Microbiol. , vol.47 , pp. 235-246
    • Lie, T.J.1    Leigh, J.A.2
  • 67
    • 0742269406 scopus 로고    scopus 로고
    • The importance of porE and porF in the anabolic pyruvate oxidoreductase of Methanococcus maripaludis
    • Lin, W., and W. B. Whitman. 2004. The importance of porE and porF in the anabolic pyruvate oxidoreductase of Methanococcus maripaludis. Arch. Microbiol. 181:68-73.
    • (2004) Arch. Microbiol. , vol.181 , pp. 68-73
    • Lin, W.1    Whitman, W.B.2
  • 68
    • 0037861912 scopus 로고    scopus 로고
    • The anabolic pyruvate oxidoreductase from Methanococcus maripaludis
    • Lin, W. C., Y. L. Yang, and W. B. Whitman. 2003. The anabolic pyruvate oxidoreductase from Methanococcus maripaludis. Arch. Microbiol. 179:444-456.
    • (2003) Arch. Microbiol. , vol.179 , pp. 444-456
    • Lin, W.C.1    Yang, Y.L.2    Whitman, W.B.3
  • 69
    • 0035976978 scopus 로고    scopus 로고
    • The archaeal DNA primase: Biochemical characterization of the p41-p46 complex from Pyrococcus furiosus
    • Liu, L., K. Komori, S. Ishino, A. A. Bocquier, I. K. Cann, D. Kohda, and Y. Ishino. 2001. The archaeal DNA primase: biochemical characterization of the p41-p46 complex from Pyrococcus furiosus. J. Biol. Chem. 276:45484-45490.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45484-45490
    • Liu, L.1    Komori, K.2    Ishino, S.3    Bocquier, A.A.4    Cann, I.K.5    Kohda, D.6    Ishino, Y.7
  • 70
    • 2442718034 scopus 로고    scopus 로고
    • Evolution of assisted protein folding: The distribution of the main chaperoning systems within the phylogenetic domain archaea
    • Macario, A. J., M. Malz, and E. Conway de Macario. 2004. Evolution of assisted protein folding: the distribution of the main chaperoning systems within the phylogenetic domain archaea. Front. Biosci. 9:1318-1332.
    • (2004) Front. Biosci. , vol.9 , pp. 1318-1332
    • Macario, A.J.1    Malz, M.2    Conway De Macario, E.3
  • 71
    • 0032516484 scopus 로고    scopus 로고
    • A small, thermostable, and monofunctional chorismate mutase from the archaeon Methanococcus jannaschii
    • MacBeath, G., P. Kast, and D. Hilvert. 1998. A small, thermostable, and monofunctional chorismate mutase from the archaeon Methanococcus jannaschii. Biochemistry 37:10062-10073.
    • (1998) Biochemistry , vol.37 , pp. 10062-10073
    • MacBeath, G.1    Kast, P.2    Hilvert, D.3
  • 72
    • 0034612226 scopus 로고    scopus 로고
    • Zinc-bundle structure of the essential RNA polymerase subunit RPB10 from Methanobacterium thermoautotrophicum
    • Mackereth, C. D., C. H. Arrowsmith, A. M. Edwards, and L. P. McIntosh. 2000. Zinc-bundle structure of the essential RNA polymerase subunit RPB10 from Methanobacterium thermoautotrophicum. Proc. Natl. Acad. Sci. USA 97:6316-6321.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6316-6321
    • Mackereth, C.D.1    Arrowsmith, C.H.2    Edwards, A.M.3    McIntosh, L.P.4
  • 73
    • 0345363243 scopus 로고    scopus 로고
    • Nucleoid structure and partition in Methanococcus jannaschii: An archaeon with multiple copies of the chromosome
    • Malandrin, L., H. Huber, and R. Bernander. 1999. Nucleoid structure and partition in Methanococcus jannaschii: an archaeon with multiple copies of the chromosome. Genetics 152:1315-1323.
    • (1999) Genetics , vol.152 , pp. 1315-1323
    • Malandrin, L.1    Huber, H.2    Bernander, R.3
  • 74
    • 0033878942 scopus 로고    scopus 로고
    • Characterization and kinetic mechanism of mono- and bifunctional ornithine acetyltransferases from thermophilic microorganisms
    • Marc, F., P. Weigel, C. Legrain, Y. Almeras, M. Santrot, N. Glansdorff, and V. Sakanyan. 2000. Characterization and kinetic mechanism of mono- and bifunctional ornithine acetyltransferases from thermophilic microorganisms. Eur. J. Biochem. 267:5217-5226.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5217-5226
    • Marc, F.1    Weigel, P.2    Legrain, C.3    Almeras, Y.4    Santrot, M.5    Glansdorff, N.6    Sakanyan, V.7
  • 75
    • 0028298029 scopus 로고
    • Cloning and characterization of a new purine biosynthetic enzyme: A non-folate glycinamide ribonucleotide transformylase from E. coli
    • Marolewski, A., J. M. Smith, and S. J. Benkovic. 1994. Cloning and characterization of a new purine biosynthetic enzyme: a non-folate glycinamide ribonucleotide transformylase from E. coli. Biochemistry 33:2531-2537.
    • (1994) Biochemistry , vol.33 , pp. 2531-2537
    • Marolewski, A.1    Smith, J.M.2    Benkovic, S.J.3
  • 76
    • 0035949506 scopus 로고    scopus 로고
    • In vivo interactions of archaeal Cdc6/Orc1 and minichromosome maintenance proteins with the replication origin
    • Matsunaga, F., P. Forterre, Y. Ishino, and H. Myllykallio. 2001. In vivo interactions of archaeal Cdc6/Orc1 and minichromosome maintenance proteins with the replication origin. Proc. Natl. Acad. Sci. USA 98:11152-11157.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11152-11157
    • Matsunaga, F.1    Forterre, P.2    Ishino, Y.3    Myllykallio, H.4
  • 77
    • 0029832099 scopus 로고    scopus 로고
    • Analysis of the CO dehydrogenase/acetyl-coenzyme A synthase operon of Methanosarcina thermophila
    • Maupin-Furlow, J. A., and J. G. Ferry. 1996. Analysis of the CO dehydrogenase/acetyl-coenzyme A synthase operon of Methanosarcina thermophila. J. Bacteriol. 178:6849-6856.
    • (1996) J. Bacteriol. , vol.178 , pp. 6849-6856
    • Maupin-Furlow, J.A.1    Ferry, J.G.2
  • 78
    • 0027297771 scopus 로고
    • Aminotransferases: Demonstration of homology and division into evolutionary subgroups
    • Mehta, P. K., T. I. Hale, and P. Christen. 1993. Aminotransferases: demonstration of homology and division into evolutionary subgroups. Eur. J. Biochem. 214:549-561.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 549-561
    • Mehta, P.K.1    Hale, T.I.2    Christen, P.3
  • 79
    • 0021607711 scopus 로고
    • Enzymes of arginine biosynthesis in methanogenic bacteria
    • Meile, L., and T. Leisinger. 1984. Enzymes of arginine biosynthesis in methanogenic bacteria. Experientia 40:899-900.
    • (1984) Experientia , vol.40 , pp. 899-900
    • Meile, L.1    Leisinger, T.2
  • 80
    • 0037022651 scopus 로고    scopus 로고
    • Transfer RNA-dependent amino acid biosynthesis: An essential route to asparagine formation
    • Min, B., J. T. Pelaschier, D. E. Graham, D. Tumbula-Hansen, and D. Soll. 2002. Transfer RNA-dependent amino acid biosynthesis: an essential route to asparagine formation. Proc. Natl. Acad. Sci. USA 99:2678-2683.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2678-2683
    • Min, B.1    Pelaschier, J.T.2    Graham, D.E.3    Tumbula-Hansen, D.4    Soll, D.5
  • 81
    • 0034546359 scopus 로고    scopus 로고
    • A stable archaeal pyruvate carboxylase from the hyperthermophile Methanococcus jannaschii
    • Mukhopadhyay, B., V. J. Patel, and R. S. Wolfe. 2000. A stable archaeal pyruvate carboxylase from the hyperthermophile Methanococcus jannaschii. Arch. Microbiol. 174:406-414.
    • (2000) Arch. Microbiol. , vol.174 , pp. 406-414
    • Mukhopadhyay, B.1    Patel, V.J.2    Wolfe, R.S.3
  • 82
    • 0036169401 scopus 로고    scopus 로고
    • Novel type of ADP-forming acetyl coenzyme A synthetase in hyperthermophilic archaea: Heterologous expression and characterization of isoenzymes from the sulfate reducer Archaeoglobus fulgidus and the methanogen Methanococcus jannaschii
    • Musfeldt, M., and P. Schonheit. 2002. Novel type of ADP-forming acetyl coenzyme A synthetase in hyperthermophilic archaea: heterologous expression and characterization of isoenzymes from the sulfate reducer Archaeoglobus fulgidus and the methanogen Methanococcus jannaschii. J. Bacteriol. 184:636-644.
    • (2002) J. Bacteriol. , vol.184 , pp. 636-644
    • Musfeldt, M.1    Schonheit, P.2
  • 83
  • 84
    • 0029987549 scopus 로고    scopus 로고
    • Glutamate-1-semialdehyde aminotransferase from Sulfolobus solfataricus
    • Palmieri, G., M. Di Palo, A. Scaloni, S. Orru, G. Marino, and G. Sannia. 1996. Glutamate-1-semialdehyde aminotransferase from Sulfolobus solfataricus. Biochem. J. 320:541-545.
    • (1996) Biochem. J. , vol.320 , pp. 541-545
    • Palmieri, G.1    Di Palo, M.2    Scaloni, A.3    Orru, S.4    Marino, G.5    Sannia, G.6
  • 85
    • 0036084146 scopus 로고    scopus 로고
    • InBase: The Intein Database
    • Perler, F. B. 2002. InBase: the Intein Database. Nucleic Acids Res. 30:383-384.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 383-384
    • Perler, F.B.1
  • 86
    • 0027993193 scopus 로고
    • Growth-phase-dependent transcription of the genes that encode the two methyl coenzyme M reductase isoenzymes and N5-methyltetrahydromethanopterin: coenzyme M methyltransferase in Methanobacterium thermoautotrophicum delta H
    • Pihl, T. D., S. Sharma, and J. N. Reeve. 1994. Growth-phase-dependent transcription of the genes that encode the two methyl coenzyme M reductase isoenzymes and N5-methyltetrahydromethanopterin:coenzyme M methyltransferase in Methanobacterium thermoautotrophicum delta H. J. Bacteriol. 176:6384-6391.
    • (1994) J. Bacteriol. , vol.176 , pp. 6384-6391
    • Pihl, T.D.1    Sharma, S.2    Reeve, J.N.3
  • 87
    • 0034616957 scopus 로고    scopus 로고
    • A TOPRIM domain in the crystal structure of the catalytic core of Escherichia coli primase confirms a structural link to DNA topoisomerases
    • Podobnik, M., P. McInerney, M. O'Donnell, and J. Kuriyan. 2000. A TOPRIM domain in the crystal structure of the catalytic core of Escherichia coli primase confirms a structural link to DNA topoisomerases. J. Mol. Biol. 300:353-362.
    • (2000) J. Mol. Biol. , vol.300 , pp. 353-362
    • Podobnik, M.1    McInerney, P.2    O'Donnell, M.3    Kuriyan, J.4
  • 88
    • 3242793348 scopus 로고    scopus 로고
    • Two biosynthetic pathways for the aromatic amino acids in the archaeon Methanooccus maripaludis
    • Porat, I., B. W. Waters, Q. Teng, and W. B. Whitman. 2004. Two biosynthetic pathways for the aromatic amino acids in the archaeon Methanooccus maripaludis. J. Bacteriol. 186:4940-4950.
    • (2004) J. Bacteriol. , vol.186 , pp. 4940-4950
    • Porat, I.1    Waters, B.W.2    Teng, Q.3    Whitman, W.B.4
  • 89
    • 1642364959 scopus 로고    scopus 로고
    • Development of a markerless genetic exchange method for Methanosarcina acetivorans C2A and its use in construction of new genetic tools for methanogenic archaea
    • Pritchett, M. A., J. K. Zhang, and W. W. Metcalf. 2004. Development of a markerless genetic exchange method for Methanosarcina acetivorans C2A and its use in construction of new genetic tools for methanogenic archaea. Appl. Environ. Microbiol. 70:1425-1433.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 1425-1433
    • Pritchett, M.A.1    Zhang, J.K.2    Metcalf, W.W.3
  • 90
    • 0031690990 scopus 로고    scopus 로고
    • Methanococcus jannaschii flap endonuclease: Expression, purification, and substrate requirements
    • Rao, H. G., A. Rosenfeld, and J. G. Wetmur. 1998. Methanococcus jannaschii flap endonuclease: expression, purification, and substrate requirements. J. Bacteriol. 180:5406-5412.
    • (1998) J. Bacteriol. , vol.180 , pp. 5406-5412
    • Rao, H.G.1    Rosenfeld, A.2    Wetmur, J.G.3
  • 91
    • 0025683248 scopus 로고
    • Two genetically distinct methyl-coenzyme M reductases in Methanobacterium thermoautotrophicum strain Marburg and delta H
    • Rospert, S., D. Linder, J. Ellermann, and R. K. Thauer. 1990. Two genetically distinct methyl-coenzyme M reductases in Methanobacterium thermoautotrophicum strain Marburg and delta H. Eur. J. Biochem. 194:871-877.
    • (1990) Eur. J. Biochem. , vol.194 , pp. 871-877
    • Rospert, S.1    Linder, D.2    Ellermann, J.3    Thauer, R.K.4
  • 92
    • 0037214551 scopus 로고    scopus 로고
    • Inactivation of the selB gene in Methanococcus maripaludis: Effect on synthesis of selenoproteins and their sulfur-containing homologs
    • Rother, M., I. Mathes, F. Lottspeich, and A. Bock. 2003. Inactivation of the selB gene in Methanococcus maripaludis: effect on synthesis of selenoproteins and their sulfur-containing homologs. J. Bacteriol. 185:107-114.
    • (2003) J. Bacteriol. , vol.185 , pp. 107-114
    • Rother, M.1    Mathes, I.2    Lottspeich, F.3    Bock, A.4
  • 93
    • 0035015556 scopus 로고    scopus 로고
    • Heterologous expression of archaeal selenoprotein genes directed by the SECIS element located in the 3′ non-translated region
    • Rother, M., A. Resch, W. L. Gardner, W. B. Whitman, and A. Bock. 2001. Heterologous expression of archaeal selenoprotein genes directed by the SECIS element located in the 3′ non-translated region. Mol. Microbiol. 40:900-908.
    • (2001) Mol. Microbiol. , vol.40 , pp. 900-908
    • Rother, M.1    Resch, A.2    Gardner, W.L.3    Whitman, W.B.4    Bock, A.5
  • 95
    • 0038191051 scopus 로고    scopus 로고
    • Concentration and assembly of the division ring proteins FtsZ, FtsA, and ZipA during the Escherichia coli cell cycle
    • Rueda, S., M. Vicente, and J. Mingorance. 2003. Concentration and assembly of the division ring proteins FtsZ, FtsA, and ZipA during the Escherichia coli cell cycle. J. Bacteriol. 185:3344-3351.
    • (2003) J. Bacteriol. , vol.185 , pp. 3344-3351
    • Rueda, S.1    Vicente, M.2    Mingorance, J.3
  • 96
    • 0037066774 scopus 로고    scopus 로고
    • ADP-dependent glucokinase/phosphofructokinase, a novel bifunctional enzyme from the hyperthermophilic archaeon Methanococcus jannaschii
    • Sakuraba, H., I. Yoshioka, S. Koga, M. Takahashi, Y. Kitahama, T. Satomura, R. Kawakami, and T. Ohshima. 2002. ADP-dependent glucokinase/ phosphofructokinase, a novel bifunctional enzyme from the hyperthermophilic archaeon Methanococcus jannaschii. J. Biol. Chem. 277:12495-12498.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12495-12498
    • Sakuraba, H.1    Yoshioka, I.2    Koga, S.3    Takahashi, M.4    Kitahama, Y.5    Satomura, T.6    Kawakami, R.7    Ohshima, T.8
  • 97
    • 0033056683 scopus 로고    scopus 로고
    • Expression of the Methanobacterium thermoautotrophicum hpt gene, encoding hypoxanthine (guanine) phosphoribosyltransferase, in Escherichia coli
    • Sauer, J., and P. Nygaard. 1999. Expression of the Methanobacterium thermoautotrophicum hpt gene, encoding hypoxanthine (guanine) phosphoribosyltransferase, in Escherichia coli. J. Bacteriol. 181:1958-1962.
    • (1999) J. Bacteriol. , vol.181 , pp. 1958-1962
    • Sauer, J.1    Nygaard, P.2
  • 99
    • 0034038010 scopus 로고    scopus 로고
    • The yexA gene product is required for phosphoribosylformylglycinamidine synthetase activity in Bacillus subtilis
    • Saxild, H. H., and P. Nygaard. 2000. The yexA gene product is required for phosphoribosylformylglycinamidine synthetase activity in Bacillus subtilis. Microbiology 146:807-814.
    • (2000) Microbiology , vol.146 , pp. 807-814
    • Saxild, H.H.1    Nygaard, P.2
  • 100
    • 0343488601 scopus 로고    scopus 로고
    • A reconstruction of the metabolism of Methanococcus jannaschii from sequence data
    • Selkov, E., N. Maltsev, G. J. Olsen, R. Overbeek, and W. B. Whitman. 1997. A reconstruction of the metabolism of Methanococcus jannaschii from sequence data. Gene 197:GC11-GC26.
    • (1997) Gene , vol.197
    • Selkov, E.1    Maltsev, N.2    Olsen, G.J.3    Overbeek, R.4    Whitman, W.B.5
  • 101
    • 0034686021 scopus 로고    scopus 로고
    • The intrinsic DNA helicase activity of Methanobacterium thermoautotrophicum delta H minichromosome maintenance protein
    • Shechter, D. F., C. Y. Ying, and J. Gautier. 2000. The intrinsic DNA helicase activity of Methanobacterium thermoautotrophicum delta H minichromosome maintenance protein. J. Biol. Chem. 275:15049-15059.
    • (2000) J. Biol. Chem. , vol.275 , pp. 15049-15059
    • Shechter, D.F.1    Ying, C.Y.2    Gautier, J.3
  • 102
    • 0032516868 scopus 로고    scopus 로고
    • Identification and characterization of the Nudix hydrolase from the archaeon, Methanococcus jannaschii, as a highly specific ADP-ribose pyrophosphatase
    • Sheikh, S., S. F. O'Handley, C. A. Dunn, and M. J. Bessman. 1998. Identification and characterization of the Nudix hydrolase from the archaeon, Methanococcus jannaschii, as a highly specific ADP-ribose pyrophosphatase. J. Biol. Chem. 273:20924-20928.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20924-20928
    • Sheikh, S.1    O'Handley, S.F.2    Dunn, C.A.3    Bessman, M.J.4
  • 103
    • 0023447129 scopus 로고
    • Pathway of acetate assimilation in autotrophic and heterotrophic methanococci
    • Shieh, J. S., and W. B. Whitman. 1987. Pathway of acetate assimilation in autotrophic and heterotrophic methanococci. J. Bacteriol. 169:5327-5329.
    • (1987) J. Bacteriol. , vol.169 , pp. 5327-5329
    • Shieh, J.S.1    Whitman, W.B.2
  • 104
    • 0035800865 scopus 로고    scopus 로고
    • Archaeal fructose-1,6-bisphosphate aldolases constitute a new family of archaeal type class I aldolase
    • Siebers, B., H. Brinkmann, C. Dorr, B. Tjaden, H. Lilie, J. van der Oost, and C. H. Verhees. 2001. Archaeal fructose-1,6-bisphosphate aldolases constitute a new family of archaeal type class I aldolase. J. Biol. Chem. 276:28710-28718.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28710-28718
    • Siebers, B.1    Brinkmann, H.2    Dorr, C.3    Tjaden, B.4    Lilie, H.5    Van Der Oost, J.6    Verhees, C.H.7
  • 107
    • 0343907310 scopus 로고    scopus 로고
    • Identification and sequence analysis of Sulfolobus solfataricus purE and purK genes
    • Sorensen, I. S., and G. Dandanell. 1997. Identification and sequence analysis of Sulfolobus solfataricus purE and purK genes. FEMS Microbiol. Lett. 154:173-180.
    • (1997) FEMS Microbiol. Lett. , vol.154 , pp. 173-180
    • Sorensen, I.S.1    Dandanell, G.2
  • 108
    • 0027534777 scopus 로고
    • Metabolic pathways in Methanococcus jannaschii and other methanogenic bacteria
    • Sprott, G. D., I. Ekiel, and G. B. Patel. 1993. Metabolic pathways in Methanococcus jannaschii and other methanogenic bacteria. Appl. Environ. Microbiol. 59:1092-1098.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 1092-1098
    • Sprott, G.D.1    Ekiel, I.2    Patel, G.B.3
  • 110
    • 0036393898 scopus 로고    scopus 로고
    • DTASelect and Contrast: Tools for assembling and comparing protein identifications from shotgun proteomics
    • Tabb, D. L., W. H. McDonald, and J. R. Yates III. 2002. DTASelect and Contrast: tools for assembling and comparing protein identifications from shotgun proteomics. J. Proteome Res. 1:21-26.
    • (2002) J. Proteome Res. , vol.1 , pp. 21-26
    • Tabb, D.L.1    McDonald, W.H.2    Yates III, J.R.3
  • 111
    • 0028029014 scopus 로고
    • Aspartate aminotransferase from a thermophilic formate-utilizing methanogen, Methanobacterium thermoformicicum strain SF-4: Relation to serine and phosphoserine aminotransferases, but not to the aspartate aminotransferase family
    • Tanaka, T., S. Yamamoto, T. Moriya, M. Taniguchi, H. Hayashi, H. Kagamiyama, and S. Oi. 1994. Aspartate aminotransferase from a thermophilic formate-utilizing methanogen, Methanobacterium thermoformicicum strain SF-4: relation to serine and phosphoserine aminotransferases, but not to the aspartate aminotransferase family. J. Biochem. (Tokyo) 115:309-317.
    • (1994) J. Biochem. (Tokyo) , vol.115 , pp. 309-317
    • Tanaka, T.1    Yamamoto, S.2    Moriya, T.3    Taniguchi, M.4    Hayashi, H.5    Kagamiyama, H.6    Oi, S.7
  • 112
    • 0033568398 scopus 로고    scopus 로고
    • Methanobacterium thermoautotrophicum encodes two multisubunit membrane-bound [NiFe] hydrogenases. Transcription of the operons and sequence analysis of the deduced proteins
    • Tersteegen, A., and R. Hedderich. 1999. Methanobacterium thermoautotrophicum encodes two multisubunit membrane-bound [NiFe] hydrogenases. Transcription of the operons and sequence analysis of the deduced proteins. Eur. J. Biochem. 264:930-943.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 930-943
    • Tersteegen, A.1    Hedderich, R.2
  • 113
    • 0030986445 scopus 로고    scopus 로고
    • Ribose biosynthesis and evidence for an alternative first step in the common aromatic amino acid pathway in Methanococcus maripaludis
    • Tumbula, D. L., Q. Teng, M. G. Bartlett, and W. B. Whitman. 1997. Ribose biosynthesis and evidence for an alternative first step in the common aromatic amino acid pathway in Methanococcus maripaludis. J. Bacteriol. 179:6010-6013.
    • (1997) J. Bacteriol. , vol.179 , pp. 6010-6013
    • Tumbula, D.L.1    Teng, Q.2    Bartlett, M.G.3    Whitman, W.B.4
  • 114
    • 0032970932 scopus 로고    scopus 로고
    • Genetics of Methanococcus: Possibilities for functional genomics in Archaea
    • Tumbula, D. L., and W. B. Whitman. 1999. Genetics of Methanococcus: possibilities for functional genomics in Archaea. Mol. Microbiol. 33:1-7.
    • (1999) Mol. Microbiol. , vol.33 , pp. 1-7
    • Tumbula, D.L.1    Whitman, W.B.2
  • 115
    • 0041828241 scopus 로고    scopus 로고
    • Scaling laws in the functional content of genomes
    • van Nimwegen, E. 2003. Scaling laws in the functional content of genomes. Trends Genet. 19:479-484.
    • (2003) Trends Genet. , vol.19 , pp. 479-484
    • Van Nimwegen, E.1
  • 116
    • 0029671286 scopus 로고    scopus 로고
    • Coenzyme F390 synthetase from Methanobacterium thermoautotrophicum Marburg belongs to the superfamily of adenylate-forming enzymes
    • Vermeij, P., R. J. van der Steen, J. T. Keltjens, G. D. Vogels, and T. Leisinger. 1996. Coenzyme F390 synthetase from Methanobacterium thermoautotrophicum Marburg belongs to the superfamily of adenylate-forming enzymes. J. Bacteriol. 178:505-510.
    • (1996) J. Bacteriol. , vol.178 , pp. 505-510
    • Vermeij, P.1    Van Der Steen, R.J.2    Keltjens, J.T.3    Vogels, G.D.4    Leisinger, T.5
  • 117
    • 0030014783 scopus 로고    scopus 로고
    • DNA topoisomerases
    • Wang, J. C. 1996. DNA topoisomerases. Annu. Rev. Biochem. 65:635-692.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 635-692
    • Wang, J.C.1
  • 118
    • 0036855274 scopus 로고    scopus 로고
    • Reconstructed protein arrays from 3D HPLC/tandem mass spectrometry and 2D gels: Complementary approaches to Porphyromonas gingivalis protein expression
    • Wang, T., Y. Zhang, W. Chen, Y. Park, R. J. Lamont, and M. Hackett. 2002. Reconstructed protein arrays from 3D HPLC/tandem mass spectrometry and 2D gels: complementary approaches to Porphyromonas gingivalis protein expression. Analyst 127:1450-1456.
    • (2002) Analyst , vol.127 , pp. 1450-1456
    • Wang, T.1    Zhang, Y.2    Chen, W.3    Park, Y.4    Lamont, R.J.5    Hackett, M.6
  • 119
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn, M. P., D. Wolters, and J. R. Yates III. 2001. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotechnol. 19:242-247.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates III, J.R.3
  • 120
    • 0009865535 scopus 로고    scopus 로고
    • Methanococcaceae
    • D. R. Boone, R. W. Castenholz, and G. M. Garrity (ed.). Springer-Verlag, New York, N.Y.
    • Whitman, W. B., D. R. Boone, and Y. Koga. 2001. Methanococcaceae, p. 236-240. In D. R. Boone, R. W. Castenholz, and G. M. Garrity (ed.), Bergey's manual of systematic bacteriology, 2nd ed., vol. 1. Springer-Verlag, New York, N.Y.
    • (2001) Bergey's Manual of Systematic Bacteriology, 2nd Ed. , vol.1 , pp. 236-240
    • Whitman, W.B.1    Boone, D.R.2    Koga, Y.3
  • 122
    • 0001476847 scopus 로고
    • Role of amino acids and vitamins in nutrition of mesophilic Methanococcus spp
    • Whitman, W. B., S. Sohn, S. Kuk, and R. Xing. 1987. Role of amino acids and vitamins in nutrition of mesophilic Methanococcus spp. Appl. Environ. Microbiol. 53:2373-2378.
    • (1987) Appl. Environ. Microbiol. , vol.53 , pp. 2373-2378
    • Whitman, W.B.1    Sohn, S.2    Kuk, S.3    Xing, R.4
  • 123
    • 0037386409 scopus 로고    scopus 로고
    • Function and regulation of the formate dehydrogenase genes of the methanogenic archaeon Methanococcus maripaludis
    • Wood, G. E., A. K. Haydock, and J. A. Leigh. 2003. Function and regulation of the formate dehydrogenase genes of the methanogenic archaeon Methanococcus maripaludis. J. Bacteriol. 185:2548-2554.
    • (2003) J. Bacteriol. , vol.185 , pp. 2548-2554
    • Wood, G.E.1    Haydock, A.K.2    Leigh, J.A.3
  • 124
    • 0026501143 scopus 로고
    • Characterization of amino acid aminotransferases of Methanococcus aeolicus
    • Xing, R. Y., and W. B. Whitman. 1992. Characterization of amino acid aminotransferases of Methanococcus aeolicus. J. Bacteriol. 174:541-548.
    • (1992) J. Bacteriol. , vol.174 , pp. 541-548
    • Xing, R.Y.1    Whitman, W.B.2
  • 125
    • 0026032524 scopus 로고
    • Characterization of enzymes of the branched-chain amino acid biosynthetic pathway in Methanococcus spp
    • Xing, R. Y., and W. B. Whitman. 1991. Characterization of enzymes of the branched-chain amino acid biosynthetic pathway in Methanococcus spp. J. Bacteriol. 173:2086-2092.
    • (1991) J. Bacteriol. , vol.173 , pp. 2086-2092
    • Xing, R.Y.1    Whitman, W.B.2
  • 126
    • 0032775448 scopus 로고    scopus 로고
    • Identifying two ancient enzymes in Archaea using predicted secondary structure alignment
    • Xu, H., R. Aurora, G. D. Rose, and R. H. White. 1999. Identifying two ancient enzymes in Archaea using predicted secondary structure alignment. Nat. Struct. Biol. 6:750-754.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 750-754
    • Xu, H.1    Aurora, R.2    Rose, G.D.3    White, R.H.4
  • 127
    • 0028123664 scopus 로고
    • Pathway of glycogen metabolism in Methanococcus madpaludis
    • Yu, J. P., J. Ladapo, and W. B. Whitman. 1994. Pathway of glycogen metabolism in Methanococcus madpaludis. J. Bacteriol. 176:325-332.
    • (1994) J. Bacteriol. , vol.176 , pp. 325-332
    • Yu, J.P.1    Ladapo, J.2    Whitman, W.B.3
  • 128
    • 0000253782 scopus 로고
    • Physiological ecology of methanogens
    • J. G. Ferry (ed.). Chapman and Hall, London, United Kingdom
    • Zinder, S. H. 1993. Physiological ecology of methanogens, p. 128-206. In J. G. Ferry (ed.), Methanogenesis. Chapman and Hall, London, United Kingdom.
    • (1993) Methanogenesis , pp. 128-206
    • Zinder, S.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.