Email this article Multifunctional ENY2 protein interacts with RNA helicase MLE
- Authors: Nikolenko JV.1, Kurshakova M.M.1, Krasnov A.N.1
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Affiliations:
- Institute of Gene Biology of the Russian Academy of Sciences
- Issue: Vol 489, No 6 (2019)
- Pages: 637-640
- Section: Biochemistry, biophysics, molecular biology
- URL: https://journals.eco-vector.com/0869-5652/article/view/18901
- DOI: https://doi.org/10.31857/S0869-56524896637-640
- ID: 18901
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Abstract
ENY2 protein of Drosophila melanogaster was previously discovered and characterized in our laboratory [1]. It was found that ENY2 is a subunit of several multiprotein complexes and connects various stages of gene expression [2-4]. This work is devoted to studying the interaction of ENY2 with RNA helicase MLE. This interaction was confirmed by independent methods. Data were obtained indicating that this interaction is conserved in evolution and is important for the functioning of MLE in both sexes.
Keywords
About the authors
J V. Nikolenko
Institute of Gene Biology of the Russian Academy of Sciences
Author for correspondence.
Email: julia.v.nikolenko@gmail.com
Russian Federation, 34/5, Vavilova street, Moscow, 119334
M. M. Kurshakova
Institute of Gene Biology of the Russian Academy of Sciences
Email: julia.v.nikolenko@gmail.com
Russian Federation, 34/5, Vavilova street, Moscow, 119334
A. N. Krasnov
Institute of Gene Biology of the Russian Academy of Sciences
Email: julia.v.nikolenko@gmail.com
Russian Federation, 34/5, Vavilova street, Moscow, 119334
References
- Georgieva S., Nabirochkina E., Dilworth F.J., et al. // Mol Cell Biol. 2001. V. 2. № 15. P. 5223-5231.
- Kopytova D.V., Krasnov A.N., Orlova A.V., et al. // Cell Cycle. 2010. V. 9. № 3. P. 479-81.
- Kopytova D.V., Orlova A.V., Krasnov A.N., et al. // Genes Dev. 2010. V. 24. № 1. P. 86-96.
- Krasnov A.N., Mazina M.Y., Nikolenko J.V., et al. // Cell Biosci. 2016. V. 6. P. 15.
- Gurskiy D., Orlova A., Vorobyeva N., et al. // Nucleic Acids Research. 2012. V. 40. № 21. P. 10 689-10 700.
- Lee C.G., Hurwitz J. // J. Biol. Chem. 1993. V. 268. P. 16 822-16 830.
- Kuroda M.I., Kernan M.J., Kreber R., et al. // Cell. 1991. V. 66. № 5. P. 935-947.
- Kernan M.J., Kuroda M.I., Kreber R., et al. // Cell. 1991. V. 66. № 5. P. 949-959.
- Morra R., Yokoyama R., Ling H., et al. // Epigenet. Chromatin. 2011. V. 4. № 6.
- Kotlikova I.V., Demakova O.V., Semeshin V.F., et al. // Genetics. 2006. V. 172. № 2. P. 963-974.
- Reenan R.A., Hanrahan C.J., Ganetzky B. // Neuron. 2000. V. 25. P. 139-149.
- Cugusi S., Kallappagoudar S., Ling H., et al. // Mol. Cell Proteomics. 2015. V. 14. № 6. P. 1478-1488.
- Cugusi S., Li Y., Jin P., et al. // PLoS Genet. 2016. V. 12. № 1.
- Boeras I., Song Z., Moran A., et al. // J. Mol. Biol. 2016. V. 428. № 11. P. 2418-2429.
- Fidaleo M., De Paola E., Paronetto M.P. // Oncotarget. 2016. V. 7. № 19. P. 28 711-28 723.
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