Biochemistry (Moscow)

, Volume 77, Issue 8, pp 857–863 | Cite as

Role of EctR as transcriptional regulator of ectoine biosynthesis genes in Methylophaga thalassica

  • I. I. Mustakhimov
  • A. S. Reshetnikov
  • D. N. Fedorov
  • V. N. KhmeleninaEmail author
  • Y. A. Trotsenko


In the halophilic aerobic methylotrophic bacterium Methylophaga thalassica, the genes encoding the enzymes for biosynthesis of the osmoprotectant ectoine were shown to be located in operon ectABC-ask. Transcription of the ect-operon was started from the two promoters homologous to the σ70-dependent promoter of Escherichia coli and regulated by protein EctR, whose encoding gene, ectR, is transcribed from three promoters. Genes homologous to ectR of methylotrophs were found in clusters of ectoine biosynthesis genes in some non-methylotrophic halophilic bacteria. EctR proteins of methylotrophic and heterotrophic halophiles belong to the MarR-family of transcriptional regulators but form a separate branch on the phylogenetic tree of the MarR proteins.

Key words

methylotrophic bacterium, osmoprotectant, ectoine genes, transcriptional regulation 



diamino butyric acid


isopropyl β-D-1-thiogalactopyranoside


Luria-Bertani medium


open reading frame


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Doronina, N. V., Sakharovski, V. G., Drachuk, S. V., and Trotsenko, Y. A. (1998) Microbiology (Moscow), 67, 378–382.Google Scholar
  2. 2.
    Khmelenina, V. N., Kalyuzhnaya, M., Sakharovski, V. G., Suzina, N. E., Trotsenko, Y. A., and Gottschalk, G. (1999) Arch. Microbiol., 172, 321–329.PubMedCrossRefGoogle Scholar
  3. 3.
    Peters, P., Galinski, E. A., and Truper, H. G. (1990) FEMS Microbiol. Lett., 71, 157–162.CrossRefGoogle Scholar
  4. 4.
    Khmelenina, V. N., Mustakhimov, I. I., Reshetnikov, A. S., Kalyuzhnaya, M., and Trotsenko, Y. A. (2010) Am. J. Agric. Biol. Sci., 5, 446–458.CrossRefGoogle Scholar
  5. 5.
    Reshetnikov, A. S., Khmelenina, V. N., Mustakhimov, I. I., Kalyuzhnaya, M., Lidstrom, M., and Trotsenko, Y. A. (2011) Extremophiles, 15, 653–663.PubMedCrossRefGoogle Scholar
  6. 6.
    Mustakhimov, I. I., Reshetnikov, A. S., Khmelenina, V. N., and Trotsenko, Y. A. (2010) Microbiology (Moscow), 79, 585–593.CrossRefGoogle Scholar
  7. 7.
    Mustakhimov, I. I., Reshetnikov, A. S., Khmelenina, V. N., and Trotsenko, Y. A. (2009) Dokl. Biochem. Biophys., 429, 305–308.PubMedCrossRefGoogle Scholar
  8. 8.
    Mustakhimov, I. I., Reshetnikov, A. S., Glukhov, A. S., Khmelenina, V. N., Kalyuzhnaya, M. G., and Trotsenko, Y. A. (2010) J. Bacteriol., 192, 410–417.PubMedCrossRefGoogle Scholar
  9. 9.
    Kalyuzhnaya, M., Khmelenina, V. N., Kotelnikova, S., Holmquist, L., Pedersen, K., and Trotsenko, Y. A. (1999) Syst. Appl. Microbiol., 22, 565–572.PubMedCrossRefGoogle Scholar
  10. 10.
    Sambrook, J., and Russell, D. W. (2001) Molecular Cloning: a Laboratory Manual, 3rd Edn., Cold Spring Harbor Laboratory, N.-Y.Google Scholar
  11. 11.
    Laemmli, U. K. (1970) Nature, 227, 680–685.PubMedCrossRefGoogle Scholar
  12. 12.
    Shacterle, G. R., and Pollack, R. L. (1973) Anal. Biochem., 51, 654–657.CrossRefGoogle Scholar
  13. 13.
    Reshetnikov, A. S., Khmelenina, V. N., and Trotsenko, Y. A. (2006) Arch. Microbiol., 184, 286–297.PubMedCrossRefGoogle Scholar
  14. 14.
    Thomson, J. D., Gibson, T. J., Plewniak, F., Jeanmougin, F., and Higgins, D. G. (1997) Nucleic Acids Res., 24, 4876–4882.CrossRefGoogle Scholar
  15. 15.
    Tamura, K., Dudley, J., Nei, M., and Kumar, S. (2007) Molecular Biology and Evolution 10.1093/molbev/msm092.Google Scholar
  16. 16.
    Wosten, M. M. S. M. (1998) FEMS Microbiol. Rev., 22, 127–150.PubMedCrossRefGoogle Scholar
  17. 17.
    Ross, W., Gosink, K. K., Salomon, J., Igarashi, K., Zou, C., Ishihama, A., Severinov, K., and Gourse, R. L. (1993) Science, 262, 1407–1412.PubMedCrossRefGoogle Scholar
  18. 18.
    Alekshun, M. N., Levy, S. B., Mealy, T. R., Seaton, B. A., and Head, J. F. (2001) Nature Struct. Biol., 8, 710–714.PubMedCrossRefGoogle Scholar
  19. 19.
    Hong, M., Fuangthong, M., Helmann, J. D., and Brennan, R. G. (2005) Mol. Cell, 20, 131–141.PubMedCrossRefGoogle Scholar
  20. 20.
    Egland, P. G., and Harwood, C. S. (1999) J. Bacteriol., 181, 2102–2109.PubMedGoogle Scholar
  21. 21.
    Park, H. S., and Kim, H. S. (2001) J. Bacteriol., 183, 5074–5081.PubMedCrossRefGoogle Scholar
  22. 22.
    Providenti, M. A., and Wyndham, R. C. (2001) Appl. Environ. Microbiol., 67, 3530–3541.PubMedCrossRefGoogle Scholar
  23. 23.
    Tropel, D., and van der Meer, J. R. (2004) Microbiol. Mol. Biol. Rev., 68, 474–500.PubMedCrossRefGoogle Scholar
  24. 24.
    Wilkinson, S. P., and Grove, A. (2004) J. Biol. Chem., 279, 51442–51450.PubMedCrossRefGoogle Scholar
  25. 25.
    Calderon, M. I., Vargas, C., Rojo, F., Iglesias-Guerra, F., Csonka, L. N., Ventosa, A., and Nieto, J. J. (2004) Microbiology (UK), 150, 3051–3063.PubMedCrossRefGoogle Scholar
  26. 26.
    Bestvater, T., and Galinski, E. A. (2002) Extremophiles, 6, 15–20.PubMedCrossRefGoogle Scholar
  27. 27.
    Kuhlmann, A. U., and Bremer, E. (2002) Appl. Environ. Microbiol., 68, 772–783.PubMedCrossRefGoogle Scholar
  28. 28.
    Bursy, J., Pierik, A. J., Pica, N., and Bremer, E. (2007) J. Biol. Chem., 282, 31147–31155.PubMedCrossRefGoogle Scholar

Copyright information

© Pleiades Publishing, Ltd. 2012

Authors and Affiliations

  • I. I. Mustakhimov
    • 1
  • A. S. Reshetnikov
    • 1
  • D. N. Fedorov
    • 1
  • V. N. Khmelenina
    • 1
    Email author
  • Y. A. Trotsenko
    • 1
  1. 1.Skryabin Institute of Biochemistry and Physiology of MicroorganismsRussian Academy of SciencesPushchino, Moscow RegionRussia

Personalised recommendations