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Increased Synthesis of a Magnesium Transporter MgtA During Recombinant Autotransporter Expression in Escherichia coli

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Abstract

Overproduction of the membrane proteins in Escherichia coli cells is a common approach to obtain sufficient material for their functional and structural studies. However, the efficiency of this process can be limited by toxic effects which decrease the viability of the host and lead to low yield of the product. During the expression of the esterase autotransporter AT877 from Psychrobacter cryohalolentis K5T, we observed significant growth inhibition of the C41(DE3) cells in comparison with the same cells producing other recombinant proteins. Induction of AT877 synthesis also resulted in the elevated expression of a magnesium transporter MgtA and decreased ATP content of the cells. To characterize the response to overexpression of the autotransporter in bacterial cells, we performed a comparative analysis of their proteomic profile by mass spectrometry. According to the obtained data, E. coli cells which synthesize AT877 experience complex stress condition presumably associated with secretion apparatus overloading and improper localization of the recombinant protein. Several response pathways were shown to be activated by AT877 overproduction including Cpx, PhoP/PhoQ, Psp, and σE The obtained results open new opportunities for optimization of the recombinant membrane protein expression in E. coli for structural studies and biotechnological applications.

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The data that support the findings of this study are available from the corresponding author upon reasonable request.

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Acknowledgements

The MS experiments were carried out using the equipment of the Shared-Access Equipment Centre “Bioorganika” of Shemyakin & Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences.

Funding

The work was funded by the Ministry of Science and Higher Education of Russia, Research Project N075-15–2020-795, local identifier 13.1902.21.0027.

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Authors and Affiliations

  1. Shemyakin & Ovchinnikov Institute of Bioorganic , Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya, 16/10, Moscow, 117997, Russia

    Lada E. Petrovskaya, Rustam H. Ziganshin, Elena A. Kryukova, Alexander V. Zlobinov, Sultan Sh. Gapizov, Lyudmila N. Shingarova, Dmitriy A. Dolgikh & Mikhail P. Kirpichnikov

  2. Emanuel Institute of Biochemical Physics, Kosygina str., 4, Moscow, 119334, Russia

    Elena A. Kryukova, Sultan Sh. Gapizov & Dmitriy A. Dolgikh

  3. Department of Biology, M. V. Lomonosov Moscow State University, Leninskie gory, 1, Moscow, 119234, Russia

    Sultan Sh. Gapizov, Dmitriy A. Dolgikh & Mikhail P. Kirpichnikov

  4. Roche Diagnostics Rus LLC, Letnikovskaya str. 2/2, Moscow, 115114, Russia

    Vasiliy A. Mironov

  5. Department of Chemistry, M. V. Lomonosov Moscow State University, Leninskie Gory, 1/3, Moscow, 119991, Russia

    Galina Yu. Lomakina

  6. Bauman Moscow State Technical University, Baumanskaya 2-ya, 5/1, Moscow, 105005, Russia

    Galina Yu. Lomakina

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  1. Lada E. Petrovskaya
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  2. Rustam H. Ziganshin
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  3. Elena A. Kryukova
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  4. Alexander V. Zlobinov
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  5. Sultan Sh. Gapizov
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  7. Vasiliy A. Mironov
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  8. Galina Yu. Lomakina
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  9. Dmitriy A. Dolgikh
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  10. Mikhail P. Kirpichnikov
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Contributions

L. E. Petrovskaya and R. H. Ziganshin designed the research and analyzed data. L. E. Petrovskaya, R. H. Ziganshin, E. A. Kryukova, L. N. Shingarova, A. V. Zlobinov, and S. Sh. Gapizov carried out the experiments. V. A. Mironov and G. Yu. Lomakina advised and supervised measurements. Project administration, L. E. Petrovskaya, D. A. Dolgikh, and M. P. Kirpichnikov. All authors interpreted data and wrote the manuscript. All authors read and approved the final manuscript.

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Correspondence to Lada E. Petrovskaya.

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Petrovskaya, L.E., Ziganshin, R.H., Kryukova, E.A. et al. Increased Synthesis of a Magnesium Transporter MgtA During Recombinant Autotransporter Expression in Escherichia coli. Appl Biochem Biotechnol 193, 3672–3703 (2021). https://doi.org/10.1007/s12010-021-03634-5

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