Xmas-2 protein, a core protein of the TREX-2 mRNA export complex, is not determined the specificity of Ras2 mRNA binding by the complex

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The TREX-2 complex of eukaryotes is responsible for the export of a wide range of mRNAs from the nucleus to the cytoplasm. Previously, we showed that a subunit of the D. melanogaster TREX-2 complex, the PCID2 protein, has a domain that specifically interacts with RNA. However, it remains unknown whether other components of the complex are involved in interaction with and recognition of the target mRNA. In the present work, we determined the role of Xmas-2, the core structural subunit of the complex, in the specific recognition of ras2 mRNA fragments. In this work, we showed that Xmas-2, interacts with ras2 mRNA independently of other subunits of the complex. We showed that RNA-binding domains are located in both the N-terminal domain and the C-terminal domain of Xmas-2. However, the interaction of the protein with ras2 mRNA fragments is independent of RNA sequence and structure and is nonspecific. Thus, the Xmas-2 subunit is not involved in the recognition of specific RNA sequences by the complex.

作者简介

M. Kurshakova

Engelhardt Institute of Molecular Biology, Russian Academy of Sciences

Email: d_dmitrieva@mail.ru
俄罗斯联邦, Moscow

Y. Vdovina

Engelhardt Institute of Molecular Biology, Russian Academy of Sciences

Email: d_dmitrieva@mail.ru
俄罗斯联邦, Moscow

S. Georgieva

Engelhardt Institute of Molecular Biology, Russian Academy of Sciences

Email: d_dmitrieva@mail.ru

Academician of the RAS

俄罗斯联邦, Moscow

D. Kopytova

Engelhardt Institute of Molecular Biology, Russian Academy of Sciences

编辑信件的主要联系方式.
Email: d_dmitrieva@mail.ru
俄罗斯联邦, Moscow

参考

  1. Fischer T. 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. Vol. 21, № 21. P. 5843–5852.
  2. Kurshakova M.M. et al. SAGA and a novel Drosophila export complex anchor efficient transcription and mRNA export to NPC // EMBO Journal. 2007. Vol. 26, № 24.
  3. Lu Q. 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. Vol. 61, № 2. P. 259–270.
  4. Luna R., Gonzalez-Aguilera C., Aguilera A. Transcription at the proximity of the nuclear pore: a role for the THP1-SAC3-SUS1-CDC31 (THSC) complex. // RNA biology. United States, 2009. Vol. 6, № 2. P. 145–148.
  5. Wickramasinghe V.O. et al. mRNA export from mammalian cell nuclei is dependent on GANP. // Current biology : CB. England, 2010. Vol. 20, № 1. P. 25–31.
  6. Kopytova D. 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.
  7. Gordon J.M.B., Aibara S., Stewart M. Structure of the Sac3 RNA-binding M-region in the Saccharomyces cerevisiae TREX-2 complex. // Nucleic acids research. 2017. Vol. 45, № 9. P. 5577–5585.
  8. Aibara S., Bai X.-C., Stewart M. The Sac3 TPR-like region in the Saccharomyces cerevisiae TREX-2 complex is more extensive but independent of the CID region. // Journal of structural biology. 2016. Vol. 195, № 3. P. 316–324.
  9. Ellisdon A.M. 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. Vol. 19, № 3. P. 328–336.
  10. Jani D. 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. Vol. 33, № 6. P. 727–737.
  11. Stewart M. Structure and Function of the TREX-2 Complex. // Sub-cellular biochemistry. United States, 2019. Vol. 93. P. 461–470.
  12. Wickramasinghe V.O. et al. Selective nuclear export of specific classes of mRNA from mammalian nuclei is promoted by GANP. // Nucleic acids research. England, 2014. Vol. 42, № 8. P. 5059–5071.
  13. Vdovina Y.A. et al. PCID2 Subunit of the Drosophila TREX-2 Complex Has Two RNA-Binding Regions. // Current issues in molecular biology. Switzerland, 2023. Vol. 45, № 7. P. 5662–5676.
  14. Kurshakova M.M., Georgieva S.G., Kopytova D.V. The Xmas-2 Protein of Drosophila melanogaster Undergoes Cleavage into Two Fragments. // Doklady Biochemistry and biophysics. United States, 2023. Vol. 509, № 1. P. 37–40.

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