Skip to main content
SpringerLink
Log in

Balnase, a New Dimer-Forming Ribonuclease from Bacillus altitudinis

  • Published:
BioNanoScience Aims and scope Submit manuscript

Abstract

Current cancer treatments still remain ineffective and cause side effects which ruinously affect healthy cells. Among new promising anticancer drugs, special attention is paid to the ribonucleases (RNases) which possess selective cytotoxicity against malignant cells. It is found that besides enzymatic activity conformational state of RNase molecules plays a role in the anticancer activity. Balnase, a new RNase from Bacillus altitudinis, is a close homolog of Bacillus pumilus RNase (binase) which selectively kills malignant cells expressing oncogenes KIT, ras, AML1/ETO, and FLT3. Earlier, homogeneous sample of balnase was obtained. Here, we have characterized structural organization of balnase. It was shown that it is a natural dimer. The enzyme has the same conformational state as binase but balnase dimers are less stable.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1

Similar content being viewed by others

References

  1. Mitkevich, V., Ilinskaya, O., Makarov, A. (2015). Antitumor RNases: killer’s secrets. Cell Cycle, 14, 931–932.

    Article  Google Scholar 

  2. Mitkevich, V., Burnysheva, K., Ilinskaya, O., Pace, C., Makarov, A. (2014). Cytotoxicity of RNase Sa to the acute myeloid leukemia Kasumi-1 cells depends on the net charge. Oncoscience, 11, 738–744.

    Article  Google Scholar 

  3. Ilinskaya, O., Dreyer, F., Mitkevich, V., Shaw, K., Pace, C., Makarov, A. (2002). Changing the net charge from negative to positive makes ribonuclease Sa cytotoxic. Protein Science, 11, 2522–2525.

    Article  Google Scholar 

  4. Makarov, A., Kolchinsky, A., Ilinskaya, O. (2008). Binase and other microbial RNases as potential anticancer agents. Bioessays, 8, 781–790.

    Article  Google Scholar 

  5. Ardelt, W., Ardelt, B., Darzynkiewicz, Z. (2009). Ribonucleases as potential modalities in anticancer therapy. European Journal of Pharmacology, 625, 181–189.

    Article  Google Scholar 

  6. Zuo, Y., & Deutscher, M. (2002). Mechanism of action of RNase T. II. A structural and functional model of the enzyme. The Journal of biological chemistry, 277, 50160–50164.

    Article  Google Scholar 

  7. Garvie, C., Vasanthavada, K., Xiang, Q. (2013). Mechanistic insights into RNase L through use of an MDMX-derived multi-functional protein domain. Biochimica et Biophysica Acta, 1834, 1562–1571.

    Article  Google Scholar 

  8. Lin, R., Chien, H., Lin, S., Chang, B., Yu, H., Tang, W., et al. (2013). MCPIP-1 ribonuclease exhibits broad-spectrum antiviral effects through viral RNA binding and degradation. Nucleic Acids Research, 41, 3314–3326.

    Article  Google Scholar 

  9. Gotte G., Mahmoud Helmy A., Ercole C., Spadaccini R., Laurents D., Donadelli M., Picone D. (2012) Double domain swapping in bovine seminal RNase: formation of distinct N- and C-swapped tetramers and multimers with increasing biological activities. PloS One 7: doi:10.1371/journal.pone.0046804

  10. Ilinskaya, O., Decker, K., Koschinski, A., Dreyer, F., Repp, H. (2001). Changing the net charge from negative to positive makes ribonuclease Sa cytotoxic. Toxicology, 156, 101–107.

    Article  Google Scholar 

  11. Mitkevich, V., Petrushanko, I., Kretova, O., Zelenikhin, P., Prassolov, V., Tchurikov, N., et al. (2010). Oncogenic c-kit transcript is a target for binase. Cell Cycle, 9, 2674–2678.

    Article  Google Scholar 

  12. Mitkevich, V., Petrushanko, I., Spirin, P., Fedorova, T., Kretova, O., Tchurikov, N., et al. (2011). Sensitivity of acute myeloid leukemia Kasumi-1 cells to binase toxic action depends on the expression of KIT and AML1-ETO oncogenes. Cell Cycle, 10, 4090–4097.

    Article  Google Scholar 

  13. Mitkevich, V., Schulga, A., Trofimov, A., Dorovatovskii, P., Goncharuk, D., et al. (2013). Structure and functional studies of the ribonuclease binase Glu43Ala/Phe81Ala mutant. Acta Cryst D Biol Crystallogr, 69, 991–996.

    Article  Google Scholar 

  14. Dudkina, E., Kayumov, A., Ulyanova, V., Ilinskaya, O. (2014). New insight into secreted ribonuclease structure: binase is a natural dimer. PloS One, 12, e115818.

    Article  Google Scholar 

  15. Dementiev, A., Orlov, V., Shlyapnikov, S. (1993). Complete primary structure of an extracellular ribonuclease of Bacillus thuringiensis. Russ J Bioorganic Chem, 19, 853–861.

    Google Scholar 

  16. Dudkina, E., Ulyanova, V., Shah, M. R., Khodzhaeva, V., Dao, L., Vershinina, V., et al. (2016). Three-step procedure for preparation of pure Bacillus altitudinis ribonuclease. FEBS Open Bio, 6, 24–32.

    Article  Google Scholar 

  17. Ilinskaya, O., Karamova, N., Ivanchenko, O., Kipenskaya, L. (1996). SOS-inducing ability of native and mutant microbial ribonucleases. Mutation Research, 354, 203–209.

    Article  Google Scholar 

  18. Laemmli, U. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680–685.

    Article  Google Scholar 

Download references

Acknowledgments

The study was performed within the Russian Government Program of Competitive Growth of Kazan Federal University and was supported by the Russian Science Foundation (project no. 141400522).

Author information

Authors and Affiliations

  1. Institute of Fundamental Medicine and Biology, Kazan Federal University, 18 Kremlevskaya Str., Kazan, 420008, Russia

    Elena Dudkina, Vera Ulyanova & Olga Ilinskaya

Authors
  1. Elena Dudkina
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Vera Ulyanova
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Olga Ilinskaya
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Elena Dudkina.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Dudkina, E., Ulyanova, V. & Ilinskaya, O. Balnase, a New Dimer-Forming Ribonuclease from Bacillus altitudinis . BioNanoSci. 7, 127–129 (2017). https://doi.org/10.1007/s12668-016-0305-y

Download citation

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s12668-016-0305-y

Keywords

Search

Navigation