Email this article 
THE HUMAN TREX-2 COMPLEX INTERACTS WITH SUBUNITS OF THE ORC COMPLEX
- Authors: Kurshakova M.M.1, Georgieva S.G.1, Kopytova D.V.1
-
Affiliations:
- Institute of Molecular Biology RAS
- Issue: Vol 513, No 1 (2023)
- Pages: 604-608
- Section: Articles
- URL: https://jdigitaldiagnostics.com/2686-7389/article/view/651064
- DOI: https://doi.org/10.31857/S2686738923600607
- EDN: https://elibrary.ru/GQISDZ
- ID: 651064
Cite item
Open Access
Access granted
Subscription Access
Abstract
The TREX-2 protein complex is the key complex involved in the export of mRNA from the nucleus to the cytoplasm through the nuclear pores. Previously, a joint protein complex of TREX-2 with ORC was isolated in D. melanogaster, it was shown that the interaction of TREX-2 with ORC is necessary for efficient mRNA export from the nucleus to the cytoplasm. In this work, we show that the TREX2-ORC joint complex is also formed in human cells.
About the authors
M. M. Kurshakova
Institute of Molecular Biology RAS
Author for correspondence.
Email: kursha@mail.ru
Russian Federation, Moscow
S. G. Georgieva
Institute of Molecular Biology RAS
Email: kursha@mail.ru
Russian Federation, Moscow
D. V. Kopytova
Institute of Molecular Biology RAS
Email: kursha@mail.ru
Russian Federation, Moscow
References
- Kurshakova M.M., Krasnov A.N., Kopytova D.V. et al. // The EMBO journal. 2007. V. 26. № 24. P. 4956–4965.
- Fischer T., Strasser K., Racz A. et al. // The EMBO journal. 2002. V. 21. № 21. P. 5843–5852.
- Rodríguez-Navarro S., Fischer T., Luo M.J. et al. // Cell. 2004. V. 116. № 1. P. 75–86.
- Jani D., Lutz S., Hurt E., et al. // Nucleic acids research. 2012. V. 40. № 10. P. 4562–4573.
- Jani D., Lutz S., Marshall N.J., et al. // Molecular cell. 2009. V. 33. № 6. P. 727–737.
- Ellisdon A.M., Dimitrova L., Hurt E. and Stuwart M. // Nature structural & molecular biology. 2012. V. 19. № 3. P. 328–336.
- Dimitrova L., Valkov E., Aibara S. et al. // Structure. 2015. V. 23. № 7. P. 1246–1257.
- Jani D., Valkov E., Stewart M. // Nucleic acids research. 2014. V. 42. № 10. P. 6686–6697.
- Kopytova D., Popova V., Kurshakova M. et al. // Nucleic acids research. 2016. V. 44. № 10. P. 4920–4933.
- Bell S.P. and Stillman B. // Nature. 1992. V. 357. P. 128–134.
- Bleichert F. // Current opinions in structural biology. 2019. V. 59. P. 195–204.
- Sasaki T. and Gilbert D.M. // Current opinions in cell biology. 2007. V.19. № 3. P. 337–343.
- Hoshina S., Yura K., Teranishi H. et al. // Journal of Biological Chemistry. 2013. V. 288. P. 30161–30171.
- Bleichert F., Botchan M.R., Berger J.M. // Nature. 2015. V. 519. P. 321–326.
- Thome K.C., Dhar S.K., Quintana D.G. et al. // Journal of Biological Chemistry. 2000. V. 275. № 45. P. 35233–35241.
- Popova V.V., Georgieva S.G., Kopytova D.V. // Biochemistry and molecular biology journal. 2016. V. 2. P. 2–14.
- Куршакова М.М., Копытова Д.В. Георгиева С.Г. // Доклады АН. 2021. Т. 496, С. 66–69.
- Wickramasinghe V.O., McMurtrie P., Marr J. et al. // Journal of molecular biology. 2011. V. 406. № 3. P. 355–361.
- Куршакова М.М., Георгиева С.Г., Копытова Д.В. // Доклады АН. 2023. Т. 509. № 1. С. 166–169.
- Glukhova A.A., Kurshakova M.M., Nabirochkina E.N. et al. // RNA Biology. 2021. V. 19. P. 1–12.
