Point mutations in the M-domainof PCID2 impair its functionin mRNA exportin Drosophila melanogaster

Capa

Citar

Texto integral

Acesso aberto Acesso aberto
Acesso é fechado Acesso está concedido
Acesso é fechado Somente assinantes

Resumo

PCID2 protein is a component of the eukaryotic TREX-2 complex responsible for mRNA export from the nucleus to the cytoplasm. Previously, we showed that PCID2 of D. melanogaster is involved in specific mRNA recognition and identified key amino acids responsible for interaction with the RNA of the ras2 gene. In this work, we show that point mutations of these amino acids disrupt the interaction of the protein with cellular RNA and the export of polyA-containing mRNA from the nucleus to the cytoplasm in Drosophila cells.

Sobre autores

Y. Vdovina

Institute of Molecular Biology, Russian Academy of Sciences

Autor responsável pela correspondência
Email: d_dmitrieva@mail.ru
Rússia, Moscow

S. Georgieva

Institute of Molecular Biology, Russian Academy of Sciences

Email: d_dmitrieva@mail.ru

Academician of the RAS

Rússia, Moscow

D. Kopytova

Institute of Molecular Biology, Russian Academy of Sciences

Email: d_dmitrieva@mail.ru
Rússia, Moscow

Bibliografia

  1. Kramer S. Nuclear mRNA maturation and mRNA export control: from trypanosomes to opisthokonts. // Parasitology. England, 2021. Vol. 148, № 10. P. 1196–1218.
  2. Wilmes G.M. et al. A genetic interaction map of RNA-processing factors reveals links between Sem1/Dss1-containing complexes and mRNA export and splicing. // Molecular cell. United States, 2008. Vol. 32, № 5. P. 735–746.
  3. Santos-Pereira J.M. et al. A genome-wide function of THSC/TREX-2 at active genes prevents transcription-replication collisions. // Nucleic acids research. England, 2014. Vol. 42, № 19. P. 12000–12014.
  4. 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.
  5. 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.
  6. 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.
  7. Rodríguez-Navarro S. et al. Sus1, a functional component of the SAGA histone acetylase complex and the nuclear pore-associated mRNA export machinery. // Cell. United States, 2004. Vol. 116, № 1. P. 75–86.
  8. Chekanova J.A. et al. Sus1, Sac3, and Thp1 mediate post-transcriptional tethering of active genes to the nuclear rim as well as to non-nascent mRNP. // RNA (New York, NY). 2008. Vol. 14, № 1. P. 66–77.
  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. Fischer T. et al. Yeast centrin Cdc31 is linked to the nuclear mRNA export machinery. // Nature cell biology. England, 2004. Vol. 6, № 9. P. 840–848.
  11. Jani D. 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. Vol. 40, № 10. P. 4562–4573.
  12. Glukhova A.A. 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. Vol. 18, № 11. P. 1969–1980.
  13. 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. Vol. 44, № 10.
  14. 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.
  15. Vdovina Y.A., Georgieva S.G., Kopytova D.V. 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. // Doklady Biochemistry and biophysics. United States, 2023. Vol. 513, № 1. P. 328–331.

Arquivos suplementares

Arquivos suplementares
Ação
1. JATS XML
Baixar

Declaração de direitos autorais © Russian Academy of Sciences, 2024