THE HUMAN TREX-2 COMPLEX INTERACTS WITH SUBUNITS OF THE ORC COMPLEX

Cover Page

Cite item

Full Text

Open Access Open Access
Restricted Access Access granted
Restricted Access Subscription or Fee 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

  1. Kurshakova M.M., Krasnov A.N., Kopytova D.V. et al. // The EMBO journal. 2007. V. 26. № 24. P. 4956–4965.
  2. Fischer T., Strasser K., Racz A. et al. // The EMBO journal. 2002. V. 21. № 21. P. 5843–5852.
  3. Rodríguez-Navarro S., Fischer T., Luo M.J. et al. // Cell. 2004. V. 116. № 1. P. 75–86.
  4. Jani D., Lutz S., Hurt E., et al. // Nucleic acids research. 2012. V. 40. № 10. P. 4562–4573.
  5. Jani D., Lutz S., Marshall N.J., et al. // Molecular cell. 2009. V. 33. № 6. P. 727–737.
  6. Ellisdon A.M., Dimitrova L., Hurt E. and Stuwart M. // Nature structural & molecular biology. 2012. V. 19. № 3. P. 328–336.
  7. Dimitrova L., Valkov E., Aibara S. et al. // Structure. 2015. V. 23. № 7. P. 1246–1257.
  8. Jani D., Valkov E., Stewart M. // Nucleic acids research. 2014. V. 42. № 10. P. 6686–6697.
  9. Kopytova D., Popova V., Kurshakova M. et al. // Nucleic acids research. 2016. V. 44. № 10. P. 4920–4933.
  10. Bell S.P. and Stillman B. // Nature. 1992. V. 357. P. 128–134.
  11. Bleichert F. // Current opinions in structural biology. 2019. V. 59. P. 195–204.
  12. Sasaki T. and Gilbert D.M. // Current opinions in cell biology. 2007. V.19. № 3. P. 337–343.
  13. Hoshina S., Yura K., Teranishi H. et al. // Journal of Biological Chemistry. 2013. V. 288. P. 30161–30171.
  14. Bleichert F., Botchan M.R., Berger J.M. // Nature. 2015. V. 519. P. 321–326.
  15. Thome K.C., Dhar S.K., Quintana D.G. et al. // Journal of Biological Chemistry. 2000. V. 275. № 45. P. 35233–35241.
  16. Popova V.V., Georgieva S.G., Kopytova D.V. // Biochemistry and molecular biology journal. 2016. V. 2. P. 2–14.
  17. Куршакова М.М., Копытова Д.В. Георгиева С.Г. // Доклады АН. 2021. Т. 496, С. 66–69.
  18. Wickramasinghe V.O., McMurtrie P., Marr J. et al. // Journal of molecular biology. 2011. V. 406. № 3. P. 355–361.
  19. Куршакова М.М., Георгиева С.Г., Копытова Д.В. // Доклады АН. 2023. Т. 509. № 1. С. 166–169.
  20. Glukhova A.A., Kurshakova M.M., Nabirochkina E.N. et al. // RNA Biology. 2021. V. 19. P. 1–12.

Supplementary files

Supplementary Files
Action
1. JATS XML
2.

Download (240KB)
3.

Download (403KB)

Copyright (c) 2023 М.М. Куршакова, С.Г. Георгиева, Д.В. Копытова