Abstract
Thermophilic and thermoresistant strains of bacilli were screened on a medium containing Chrome Azurol S for the producers of siderophores. It was found that the Bacillus licheniformis VK21 strain dramatically increases secretion of the metabolite, a chelator of Fe3+, in response to addition of manganese(II) salts. The growth of the producer on a minimal medium containing MnSO4 under the conditions of iron deficiency is accompanied by the accumulation of a catecholic product, the content of which reaches maximum at the beginning of the stationary growth phase of culture. In the presence of FeCl3, the amount of the catecholic product in the medium considerably decreases. The siderophore, called SVK21, was isolated from the cultural medium and purified by reversed phase HPLC, and its siderophore function was confirmed by the test for the restoration of growth of producer cells in a medium containing EDTA. The UV spectrum of the siderophore has absorption maxima at 248 and 315 nm. According to the amino acid analysis and NMR spectrometry, the metabolite SVK21 is 2,3-dihydroxybenzoyl-glycyl-threonine.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Neilands, J.B., Structure and Bonding, 1984, vol. 58, pp. 1–24.
Neilands, J.B., J. Biol. Chem., 1995, vol. 270, pp. 26723–26726.
Hider, R.C., Structure and Bonding, 1984, vol. 58, pp. 25–87.
Maksimova, N.P., Blazhevich, O.V., Lysak, V.V., and Fomichev, Yu.K., Mikrobiologiya, 1994, vol. 63, pp. 1038–1044.
Drechsel, H. and Jung, G., J. Pept. Sci., 1998, vol. 4, pp. 147–181.
Marahiel, M.A., Stachelchaus, T., and Mootz, H.D., Chem. Rev., 1997, vol. 97, pp. 2651–2673.
Konz, D. and Marahiel, M.A., Chem. Biol., 1999, vol. 6, pp. 39–48.
Meyer, J.-M., Arch. Microbiol., 2000, vol. 174, pp. 135–142.
Bultreys, A., Gheysen, I., Maraite, H., and De Hoffmann, E., Appl. Env., Microbiol., 2001, vol. 67, pp. 1718–1727.
O'Brian, I.G. and Gibson, F., Biochim. Biophys. Acta, 1970, vol. 215, pp. 393–402.
Pollack, J.R. and Neilands, J.B., Biochem. Biophys. Res. Commun., 1970, vol. 38, pp. 989–992.
Ong, S.A., Peterson, T., and Neilands, J.B., J. Biol. Chem., 1979, vol. 254, pp. 1860–1865.
Page, W.J. and von Tigerstrom, M., J. Gen. Microbiol., 1988, vol. 134, pp. 453–460.
Haag, H., Hantke, K., Drechsel, H., Stojiljkovic, I., Jung, G., and Zähner, H., J. Gen. Microbiol., 1993, vol. 139, pp. 2159–2165.
Yamamoto, S., Okujo, N., Fujita, Y., Saito, M., Yoshida, T., and Shinoda, S., J. Biochem., 1993, vol. 113, pp. 538–544.
Mullis, K.B., Pollack, J.R., and Neilands, J.B., Biochemistry, 1971, vol. 10, pp. 4894–4898.
Wong, D.K., Gobin, J., Horwitz, M.A., and Gibson, B.W., J. Bacteriol., 1996, vol. 178, pp. 6394–6398.
Fiedler, H.P., Krastel, P., Müller, J., Gebhardt, K., and Zeeck, A., FEMS Microbiol. Lett., 2001, vol. 196, pp. 147–151.
Peters, W.J. and Warren, R.A.J., J. Bacteriol., 1968, vol. 95, pp. 360–368.
May, J.J., Wendrich, T.M., and Marahiel, M.A., J. Biol. Chem., 2001, vol. 276, pp. 7209–7217.
Guerry, P., Perez-Casal, J., Yao, R., McVeigh, A., and Trust, T.J., J. Bacteriol., 1997, vol. 179, pp. 3997–4002.
Schwyn, B. and Neilands, J.B., Anal. Biochem., 1987, vol. 160, pp. 47–56.
Bsat, N., Herbig, A., Casillas-Martinez, L., Setlow, P., and Helmann, J.D., Mol. Microbiol., 1998, vol. 29, pp. 189–198.
Inaoka, T., Matsumura, Y., and Tsuchido, T., J. Bacteriol., 1998, vol. 180, pp. 3697–3703.
Touati, D., Arch. Biochem. Biophys., 2000, vol. 373, pp. 1–6.
Cornish, A.S. and Page, W.J., Microbiology, 1998, vol. 144, pp. 1747–1754.
Dussurget, O., Rodriguez, M., and Smith, I., Mol. Microbiol., 1996, vol. 22, pp. 535–544.
Rioux, C., Jordan, D.C., and Rattray, J.B.M., Anal. Biochem., 1983, vol. 133, pp. 163–169.
Walsh, B.L. and Warren, R.A.J., Can. J. Microbiol., 1971, vol. 17, pp. 175–177.
Barnum, D.W., Anal. Chem. Acta, 1977, vol. 89, pp. 157–166.
Dawson, R., Elliott, D., Elliott, W., and Jones, K., Data for Biochemical Research, Oxford: Clarendon, 1986. Translated under the title Spravochnik biokhimika, Moscow: Mir, 1991
Rance, M., Sorensen, O.W., Bodenhausen, G., Wagner, C., Ernst, R.R., and Wüthrich, K., Biochem. Biophys. Res. Commun., 1983, vol. 117, pp. 479–485.
Bax, A. and Davis, D.G., J. Magn. Reson., 1985, vol. 65, pp. 355–366.
Wagner, R. and Berge, S., J. Magn. Reson., 1996, vol. 123, pp. 229–232.
States, D.J., Habercorn, R.A., and Ruben, D.J., J. Magn. Reson., 1982, vol. 48, pp. 286–292.
Piotto, M., Saudek, V., and Sklenar, V., J. Biomol. NMR, 1992, vol. 2, pp. 661–665.
Bax, A., Griffey, R.H., and Hawkins, B.L., J. Magn. Reson., 1983, vol. 55, pp. 301–315.
Bax, A. and Subramania, S., J. Magn. Reson., 1986, vol. 67, pp. 565–569.
Bax, A. and Summers, M.F., J. Am. Chem. Soc., 1986, vol. 108, pp. 2093–2094.
Wishart, D.S., Bigam, C.G., Yao, J., Abildgaard, F., Dyson, H.J., Oldfeld, E., Markley, J.L., and Sykes, B.D., J. Biomol. NMR, 1995, vol. 6, pp. 135–140.
Wüthrich, K., NMR of Proteins and Nucleic Acids, New York: Wiley, 1986.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Temirov, Y.V., Esikova, T.Z., Kashparov, I.A. et al. A Catecholic Siderophore Produced by the Thermoresistant Bacillus licheniformis VK21 Strain. Russian Journal of Bioorganic Chemistry 29, 542–549 (2003). https://doi.org/10.1023/B:RUBI.0000008894.80972.2e
Issue Date:
DOI: https://doi.org/10.1023/B:RUBI.0000008894.80972.2e