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Heterologous Expression of Histidine Acid Phytase from Pantoea sp. 3.5.1 in Yarrowia lipolytica

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Abstract

The dimorphic yeasts Yarrowia lipolytica are used as effective expression system and are characterized by a high level of production of heterologous protein. In this work, we aimed to clone and express Pantoea sp. 3.5.1 agpP phytase gene in Yarrowia lipolytica. Genetic constructs containing the native phytase gene (agpP) under the control of the strong hybrid promoter hp4d and the signal peptide of the alkaline extracellular protease XPR2 gene, as well as the optimized gene (agpP-opt) of phytase under the control of two signal peptides—bacterial and yeast were obtained. Recombinant Y. lipolytica strains with integrated bacterial phytase genes were obtained and expression of phytase was analyzed.

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References

  1. Suzuki, U., Yoshimura, K., & Takaishi, M. (1907). Über ein enzym ‘Phytase’ das anhydro-oxy-methylen diphosphorsaure’ spalter. Bulletin of the College of Agriculture, Tokyo Imperial University, 7, 503–512.

    Google Scholar 

  2. Hayakawa, T., Suzuki, K., Miura, H., Ohno, T., & Igaue, I. (1990). Myo-inositol polyphosphate intermediates in the dephosphorylation of Phytic acid by acid phosphatase with phytase activity from rice bran. Agricultural and Biological Chemistry, 54(2), 279–286.

    Google Scholar 

  3. Thomas, M. P., Mills, S. J., & Potter, B. V. L. (2016). The “other” Inositols and their phosphates: synthesis, biology, and medicine (with recent advances in myoInositol chemistry). Angewandte Chemie, International Edition, 55, 1614–1650. https://doi.org/10.1002/anie.201502227.

    Article  Google Scholar 

  4. Irvine, R. F., & Schell, M. J. (2001). Back in the water: the return of the inositol phosphates. Nature Reviews, 1, 327–338. https://doi.org/10.1038/35073015.

    Article  Google Scholar 

  5. Haefner, S., Knietsch, A., Scholten, E., Braun, J., Lohscheidt, M., & Zelder, O. (2005). Biotechnological production and applications of phytases. Applied Microbiology and Biotechnology, 68, 588–597. https://doi.org/10.1007/s00253-005-0005-y.

    Article  Google Scholar 

  6. Dvorakova, J., Kopecky, J., Havlicek, V., & Kren, V. (2000). Formation of myo-inositol phosphates by Aspergillus niger 3-phytase. Folia Microbiologica, 45(2), 128–132.

    Article  Google Scholar 

  7. Siren M. (1986a). Stabilized pharmaceutical and biological material composition. Pat. SE 003165.

  8. Siren M. (1986b). New myo-inositol triphosphoric acid isomer. Pat.SW 052950.

  9. Suleimanova, A. D., Beinhauer, A., Valeeva, L. R., Chastukhina, I. B., Balaban, N. P., Shakirov, E. V., Greiner, R., & Sharipova, M. R. (2015). Novel glucose-1-phosphatase with high phytase activity and unusual metal ion activation from soil bacterium Pantoea sp. strain 3.5.1. Applied and Environmental Microbiology, 81, 6790–6799. https://doi.org/10.1128/AEM.01384-15.

    Article  Google Scholar 

  10. Yan, J., Han, B., Gui, X., Wang, G., Xu, L., Yan, Y., Madzak, C., Pan, D., Wang, Y., Zha, G., & Jiao, L. (2018). Engineering Yarrowia lipolytica to simultaneously produce lipase and single cell protein from agroindustrial wastes for feed. Scientific Reports, 8, 758.

    Article  Google Scholar 

  11. Groenewald, M., Boekhout, T., Neuvéglise, C., Gaillardin, C., van Dijck, P. W., & Wyss, M. (2014). Yarrowia lipolytica: safety assessment of an oleaginous yeast with a great industrial potential. Critical Reviews in Microbiology, 40(3), 187–206.

    Article  Google Scholar 

  12. Madzak, C., Treton, B., & Blanchin-Roland, S. (2000). Strong hybrid promoters and integrative expression/secretion vectors for quasiconstitutive expression of heterologous proteins in the yeast Yarrowia lipolytica. Journal of Molecular Microbiology and Biotechnology, 2, 207–216.

    Google Scholar 

  13. Sambrook, J., & Russell, D. W. (2001). Molecular cloning: a laboratory manual. Cold: Cold Spring Harbor Laboratory Press.

    Google Scholar 

  14. Greiner, R. (2004). Degradation of myo-inositol hexakisphosphate by a phytate-degrading enzyme from Pantoea agglomerans. The Protein Journal, 23, 577–585.

    Article  Google Scholar 

  15. Yao, X., Peijun, M., Premal, S., Antonis, R., & Yi, L. (2013). Non-optimal codon usage is a mechanism to achieve circadian clock conditionality. Nature, 495, 116–120.

    Article  Google Scholar 

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Acknowledgments

This work was performed in accordance with the Russian Government Program of Competitive Growth of the Kazan Federal University and supported by the Russian Foundation for Basic Research (project no. 16-34-60191).

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Authors and Affiliations

  1. Kazan (Volga region) Federal University, Kazan, Russia

    Aliya D. Suleimanova, Daria S. Troshagina & Margarita R. Sharipova

  2. Université Paris-Saclay, Thiverval-Grignon, France

    Catherine Madzak

Authors
  1. Aliya D. Suleimanova
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  2. Daria S. Troshagina
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  3. Catherine Madzak
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  4. Margarita R. Sharipova
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Correspondence to Aliya D. Suleimanova.

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Suleimanova, A.D., Troshagina, D.S., Madzak, C. et al. Heterologous Expression of Histidine Acid Phytase from Pantoea sp. 3.5.1 in Yarrowia lipolytica. BioNanoSci. 9, 44–47 (2019). https://doi.org/10.1007/s12668-018-0574-8

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  • DOI: https://doi.org/10.1007/s12668-018-0574-8

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