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Актуальная биотехнология

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БЕЛОК LEPA НЕ СПАСАЕТ ESCHERICHIA COLI ОТ АНТИБИОТИКОВ

https://doi.org/10.20914/2304-4691-2025-2-12-15

Об авторах

Е. М. Максимова
ФГБУН Институт белка РАН
Россия


И. А. Остерман
МГУ имени М. В. Ломоносова
Россия


Е. А. Столбоушкина
ФГБУН Институт белка РАН
Россия


Список литературы

1. Baba T., Ara T., Hasegawa M. et al. Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection // Molecular Systems Biology. 2006. Vol. 2. 2006.0008. doi: 10.1038/msb4100050

2. Bachmann B.J. Pedigrees of some mutant strains of Escherichia coli K-12 // Bacteriological Reviews. 1972. Vol. 36. № 4. P. 525-557.

3. Badu-Nkansah A., Sello J.K. Deletion of the elongation factor 4 gene (lepA) in Streptomyces coelicolor enhances the production of the calcium-dependent antibiotic // FEMS Microbiology Letters. 2010. Vol. 311. № 2. P. 147-151.

4. Balakrishnan R., Oman K., Shoji S. et al. The conserved GTPase LepA contributes mainly to translation initiation in Escherichia coli // Nucleic Acids Research. 2014. Vol. 42. № 21. P. 13370-13383.

5. Blattner F.R., Plunkett G., Bloch C.A. et al. The complete genome sequence of Escherichia coli K-12 // Science. 1997. Vol. 277. № 5331. P. 1453-1462.

6. Gagnon M.G., Lin J., Bulkley D., Steitz T.A. Ribosome structure. Crystal structure of elongation factor 4 bound to a clockwise-ratcheted ribosome // Science. 2014. Vol. 345. № 6197. P. 684-687.

7. Gagnon M.G., Lin J., Steitz T.A. Elongation factor 4 remodels the A-site tRNA on the ribosome // Proceedings of the National Academy of Sciences of the United States of America. 2016. Vol. 113. № 18. P. 4994-4999.

8. Gibbs M.R., Moon K.M., Chen M. et al. Conserved GTPase LepA (Elongation Factor 4) functions in biogenesis of the 30S subunit of the 70S ribosome // Proceedings of the National Academy of Sciences of the United States of America. 2017. Vol. 114. № 5. P. 980-985

9. Liu B., Chen C. Translation Elongation Factor 4 (LepA) Contributes to Tetracycline Susceptibility by Stalling Elongating Ribosomes // Antimicrobial Agents and Chemotherapy. 2018. Vol. 62. № 8. e02356-17

10. Liu H., Chen C., Zhang H. et al. The conserved protein EF4 (LepA) modulates the elongation cycle of protein synthesis // Proceedings of the National Academy of Sciences of the United States of America. 2011. Vol. 108. № 39. P. 16223-16228.

11. Osterman I.A., Prokhorova I.V., Sysoev V.O. et al. Attenuation-based dual-fluorescent-protein reporter for screening translation inhibitors // Antimicrobial Agents and Chemotherapy. 2012. Vol. 56. № 4. P. 1774-1783.

12. Qin Y., Polacek N., Vesper O. et al. The highly conserved LepA is a ribosomal elongation factor that back- translocates the ribosome // Cell. 2006. Vol. 127. № 4. P. 721-733.

13. Wang B., Zhu J., Javid B. Clinically relevant mutations in mycobacterial LepA cause rifampicin-specific phenotypic resistance // Scientific Reports. 2020. Vol. 10. 8402.

14. Bauerschmitt H., Funes S., Herrmann J.M. The membrane-bound GTPase Guf1 promotes mitochondrial protein synthesis under suboptimal conditions // Journal of Biological Chemistry. 2008. Vol. 283. № 25. P. 17139-17146.

15. Bijlsma J.J., Lie-A-Ling M., Nootenboom I.C. et al. Identification of loci essential for the growth of Helicobacter pylori under acidic conditions // Journal of Infectious Diseases. 2000. Vol. 182. № 5. P. 1566-1569.

16. Gao Y., Bai X., Zhang D. et al. Mammalian elongation factor 4 regulates mitochondrial translation essential for spermatogenesis // Nature Structural & Molecular Biology. 2016. Vol. 23. № 5. P. 441-449.

17. Heller J.L.E., Kamalampeta R., Wieden H. Taking a Step Back from Back-Translocation: an Integrative View of LepA/EF4's Cellular Function // Molecular and Cellular Biology. 2017. Vol. 37. № 12. e00653-16.

18. Ji D.L., Lin H., Chi W., Zhang L.X. CpLEPA is critical for chloroplast protein synthesis under suboptimal conditions in Arabidopsis thaliana // PLoS One. 2012. Vol. 7. № 11. e49746.

19. Kumar V., Ero R., Ahmed T. et al. Structure of the GTP Form of Elongation Factor 4 (EF4) Bound to the Ribosome // Journal of Biological Chemistry. 2016. Vol. 291. № 25. P. 12943-12950.

20. Liu H., Pan D., Pech M., Cooperman B.S. Interrupted catalysis: the EF4 (LepA) effect on back-translocation // Journal of Molecular Biology. 2011. Vol. 396. №

21. Pech M., Karim Z., Yamamoto H. et al. Elongation factor 4 (EF4/LepA) accelerates protein synthesis at increased Mg2+ concentrations // Proceedings of the National Academy of Sciences of the United States of America. 2011. Vol. 108. № 8. P. 3199-3203

22. Zhang D., Yan K., Liu G. et al. EF4 disengages the peptidyl-tRNA CCA end and facilitates back-translocation on the 70S ribosome // Nature Structural & Molecular Biology. 2016. Vol. 23. № 2. P. 125-131.


Рецензия

Для цитирования:


Максимова Е.М., Остерман И.А., Столбоушкина Е.А. БЕЛОК LEPA НЕ СПАСАЕТ ESCHERICHIA COLI ОТ АНТИБИОТИКОВ. Актуальная биотехнология. 2025;(2):12-15. https://doi.org/10.20914/2304-4691-2025-2-12-15

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