INTERACTION OF MRNA WITH THE C-TERMINAL DOMAIN OF PCID2, A SUBUNIT OF THE TREX-2 COMPLEX, IS REQUIRED FOR ITS EXPORT FROM THE NUCLEUS TO THE CYTOPLASM IN DROSOPHILA MELANOGASTER

Cover Page

Cite item

Full Text

Open Access Open Access
Restricted Access Access granted
Restricted Access Subscription Access

Abstract

Following the transcription step, the newly synthesized mRNA is exported from the nucleus to the cytoplasm and further to the translation site. The TREX-2 complex is involved in the step of mRNA export from the nucleus to the cytoplasm. This complex in Drosophila melanogaster consists of four proteins: Xmas-2, PCID2, ENY2, Sem1p. In our work, we have shown that deletion of the C-terminal sequence of PCID2 leads to a decrease in the interaction of the protein with RNA and to impaired mRNA export from the nucleus to the cytoplasm in D. melanogaster.

About the authors

Y. A. Vdovina

Institute of Molecular Biology, Russian Academy of Sciences

Author for correspondence.
Email: yuvdov2020@gmail.com
Russian Federation, Moscow

S. G. Georgieva

Institute of Molecular Biology, Russian Academy of Sciences

Email: d_dmitrieva@mail.ru
Russian Federation, Moscow

D. V. Kopytova

Institute of Molecular Biology, Russian Academy of Sciences

Author for correspondence.
Email: d_dmitrieva@mail.ru
Russian Federation, Moscow

References

  1. Kopytova D., Popova V., Kurshakova M., et al. ORC interacts with THSC/TREX-2 and its subunits promote Nxf1 association with mRNP and mRNA export in Drosophila. // Nucleic acids research. 2016. V. 44. №10. P. 4920–4933.
  2. Kurshakova M.M., Krasnov A.N., Kopytova D.V., et al. SAGA and a novel Drosophila export complex anchor efficient transcription and mRNA export to NPC // EMBO Journal. 2007. V. 26, № 24. P. 14956–65.
  3. Stewart M. Structure and Function of the TREX-2 Complex. // Sub-cellular biochemistry. United States, 2019. V. 93. P. 461–470.
  4. Pascual-Garcia P., Govind C.K., Queralt E., al. Sus1 is recruited to coding regions and functions during transcription elongation in association with SAGA and TREX2. // Genes & development. United States, 2008. V. 22. № 20. P. 2811–2822.
  5. Georgieva S., Nabirochkina E., Dilworth F.J., et al. The novel transcription factor e(y)2 interacts with TAF(II)40 and potentiates transcription activation on chromatin templates. // Molecular and cellular biology. United States, 2001. V. 21. № 15. P. 5223–5231.
  6. Kopytova D.V., Orlova A.V., Krasnov A.N., et al. Multifunctional factor ENY2 is associated with the THO complex and promotes its recruitment onto nascent mRNA. // Genes & development. United States, 2010. V. 24. № 1. P. 86–96.
  7. Kurshakova M., Maksimenko O., Golovnin A., et al. Evolutionarily conserved E(y)2/Sus1 protein is essential for the barrier activity of Su(Hw)-dependent insulators in Drosophila. // Molecular cell. United States, 2007. V. 27. № 2. P. 332–338.
  8. Maksimenko O., Kyrchanova O., Bonchuk A., et al. Highly conserved ENY2/Sus1 protein binds to Drosophila CTCF and is required for barrier activity. // Epigenetics. 2014. V. 9. № 9. P. 1261–1270.
  9. Farny N.G., Hurt J.A., Silver P.A. Definition of global and transcript-specific mRNA export pathways in metazoans. // Genes & development. United States, 2008. V. 22. № 1. P. 66–78.
  10. Glukhova A.A., Kurshakova M.M., Nabirochkina E.N. et al. PCID2, a subunit of the Drosophila TREX-2 nuclear export complex, is essential for both mRNA nuclear export and its subsequent cytoplasmic trafficking // RNA Biology. United States, 2021. V. 18, № 11. P. 1969–1980.
  11. Jani D., Lutz S., Hurt E., et al. Functional and structural characterization of the mammalian TREX-2 complex that links transcription with nuclear messenger RNA export. // Nucleic acids research. England, 2012. V. 40. № 10. P. 4562–4573.
  12. Jani D., Lutz S, Marshall N.J., et al. Sus1, Cdc31, and the Sac3 CID region form a conserved interaction platform that promotes nuclear pore association and mRNA export. // Molecular cell. United States, 2009. V. 33. № 6. P. 727–737.
  13. Jani D., Valkov E., Stewart M. Structural basis for binding the TREX2 complex to nuclear pores, GAL1 localisation and mRNA export. // Nucleic acids research. England, 2014. V. 42. № 10. P. 6686–6697.
  14. Fischer T., Strasser K., Racz A., et al. The mRNA export machinery requires the novel Sac3p-Thp1p complex to dock at the nucleoplasmic entrance of the nuclear pores. // The EMBO journal. England, 2002. V. 21. № 21. P. 5843–5852.
  15. Gonzalez-Aguilera C., Tous C., Gomez-Gonzalez B., et al. The THP1-SAC3-SUS1-CDC31 complex works in transcription elongation-mRNA export preventing RNA-mediated genome instability. // Molecular biology of the cell. United States, 2008. V. 19. № 10. P. 4310–4318.
  16. Lu Q., Tang X., Tian G., et al. Arabidopsis homolog of the yeast TREX-2 mRNA export complex: components and anchoring nucleoporin. // The Plant journal: for cell and molecular biology. England, 2010. V. 61. № 2. P. 259–270.
  17. Rodríguez-Navarro S., Fischer T., Luo M.-J., et al. Sus1, a functional component of the SAGA histone acetylase complex and the nuclear pore-associated mRNA export machinery. // Cell. United States, 2004. V. 116. № 1. P. 75–86.
  18. Ellisdon A.M., Dimitrova L., Hurt E., et al. Structural basis for the assembly and nucleic acid binding of the TREX-2 transcription-export complex. // Nature structural & molecular biology. United States, 2012. V. 19. № 3. P. 328–336.

Supplementary files

Supplementary Files
Action
1. JATS XML
Download
2.

Download (163KB)
Indexing metadata
3.

Download (384KB)
Indexing metadata

Copyright (c) 2023 Ю.А. Вдовина, С.Г. Георгиева, Д.В. Копытова