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Original Articles

Phylogenetic and Disruption Analyses of Aspartate Kinase of Deinococcus radiodurans

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Pages 1015-1020 | Received 28 Nov 2006, Accepted 14 Jan 2007, Published online: 22 May 2014

  • 1) Griffiths, E., and Gupta, R. S., Distinctive protein signatures provide molecular markers and evidence for the monophyletic nature of the Deinococcus-Thermus phylum. J. Bacteriol., 186, 3097–3107 (2004).
  • 2) Omelchenko, M. V., Wolf, Y. I., Gaidamakova, E. K., Matrosova, V. Y., Vasilenko, A., Zhai, M., Daly, M. J., Koonin, E. V., and Makarova, K. S., Comparative genomics of Thermus thermophilus and Deinococcus radiodurans: divergent routes of adaptation to thermophily and radiation resistance. BMC Evol. Biol., 5, 57 (2005).
  • 3) Kosuge, T., and Hoshino, T., Lysine is synthesized through the α-aminoadipate pathway in Thermus thermophilus. FEMS Microbiol. Lett., 169, 361–367 (1998).
  • 4) Kobashi, N., Nishiyama, M., and Tanokura, M., Aspartate kinase-independent lysine synthesis in an extremely thermophilic bacterium, Thermus thermophilus: lysine is synthesized via α-aminoadipic acid not via diaminopimelic acid. J. Bacteriol., 181, 1713–1718 (1999).
  • 5) Nishida, H., Nishiyama, M., Kobashi, N., Kosuge, T., Hoshino, T., and Yamane, H., A prokaryotic gene cluster involved in synthesis of lysine through the amino adipate pathway: a key to the evolution of amino acid biosynthesis. Genome Res., 9, 1175–1183 (1999).
  • 6) Nishida, H., Distribution of genes for lysine biosynthesis through the aminoadipate pathway among prokaryotic genomes. Bioinformatics, 17, 189–191 (2001).
  • 7) Nishida, H., and Narumi, I., Disruption analysis of DR1420 and/or DR1758 in the extremely radioresistant bacterium Deinococcus radiodurans. Microbiology, 148, 2911–2914 (2002).
  • 8) White, O., Eisen, J. A., Heidelberg, J. F., Hickey, E. K., Peterson, J. D., Dodson, R. J., Haft, D. H., Gwinn, M. L., Nelson, W. C., Richardson, D. L., Moffat, K. S., Qin, H., Jiang, L., Pamphile, W., Crosby, M., Shen, M., Vamathevan, J. J., Lam, P., McDonald, L., Utterback, T., Zalewski, C., Makarova, K. S., Aravind, L., Daly, M. J., Minton, K. W., Fleischmann, R. D., Ketchum, K. A., Nelson, K. E., Salzberg, S., Smith, H. O., Venter, J. C., and Fraser, C. M., Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1. Science, 286, 1571–1577 (1999).
  • 9) Henne, A., Bruggemann, H., Raasch, C., Wiezer, A., Hartsch, T., Liesegang, H., Johann, A., Lienard, T., Gohl, O., Martinez-Arias, R., Jacobi, C., Starkuviene, V., Schlenczeck, S., Dencker, S., Huber, R., Klenk, H. P., Kramer, W., Merkl, R., Gottschalk, G., and Fritz, H. J., The genome sequence of the extreme thermophile Thermus thermophilus. Nat. Biotechnol., 22, 547–553 (2004).
  • 10) Ferrara, P., Duchange, N., Zakin, M. M., and Cohen, G. N., Internal homologies in the two aspartokinase–homoserine dehydrogenases of Escherichia coli K-12. Proc. Natl. Acad. Sci. USA, 81, 3019–3023 (1984).
  • 11) Parsot, C., and Cohen, G. N., Cloning and nucleotide sequence of the Bacillus subtilis hom gene coding for homoserine dehydrogenase. J. Biol. Chem., 263, 14654–14660 (1988).
  • 12) Truffa-Bachi, P., Guiso, N., Cohen, G. N., Theze, J., and Burr, B., Evolution of biosynthetic pathways: immunological approach. Proc. Natl. Acad. Sci. USA, 72, 1268–1271 (1975).
  • 13) Kanehisa, M., Goto, S., Hattori, M., Aoki-Kinoshita, K. F., Itoh, M., Kawashima, S., Katayama, T., Araki, M., and Hirakawa, M., From genomics to chemical genomics: new developments in KEGG. Nucleic Acids Res., 34, D354–D357 (2006).
  • 14) Altschul, S. F., Gish, W., Miller, W., Myers, E. W., and Lipman, D. J., Basic local alignment search tool. J. Mol. Biol., 215, 403–410 (1990).
  • 15) Thompson, J. D., Higgins, D. G., and Gibson, T. J., CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res., 22, 4673–4680 (1994).
  • 16) Kumar, S., Tamura, K., and Nei, M., MEGA 3: integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief. Bioinformatics, 5, 150–163 (2004).
  • 17) Venkateswaran, A., McFarlan, S. C., Ghosal, D., Minton, K. W., Vasilenko, A., Makarova, K., Wackett, L. P., and Daly, M. J., Physiologic determinants of radiation resistance in Deinococcus radiodurans. Appl. Environ. Microbiol., 66, 2620–2626 (2000).
  • 18) Kato, C., Kurihara, T., Kobashi, N., Yamane, H., and Nishiyama, M., Conversion of feedback regulation in aspartate kinase by domain exchange. Biochem. Biophys. Res. Commun., 316, 802–808 (2004).
  • 19) Moir, D., and Paulus, H., Properties and subunit structure of aspartokinase II from Bacillus subtilis VB217. J. Biol. Chem., 252, 4648–4654 (1977).
  • 20) Marco-Marín, C., Ramón-Maiques, S., Tavárez, S., and Rubio, V., Site-directed mutagenesis of Escherichia coli acetylglutamate kinase and aspartokinase III probes the catalytic and substrate-binding mechanisms of these amino acid kinase family enzymes and allows three-dimensional modeling of aspartokinase. J. Mol. Biol., 334, 459–476 (2003).
  • 21) Kobashi, N., Nishiyama, M., and Yamane, H., Characterization of aspartate kinase III of Bacillus subtilis. Biosci. Biotechnol. Biochem., 65, 1391–1394 (2001).
  • 22) Chassagnole, C., Raïs, B., Quentin, E., Fell, D. A., and Mazat, J.-P., An integrated study of threonine-pathway enzyme kinetics in Escherichia coli. Biochem. J., 356, 415–423 (2001).

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