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Ty3 nuclear entry is initiated by viruslike particle docking on GLFG nucleoporins

Nadejda Beliakova-Bethell1, Laura J Terry, Virginia Bilanchone

  • 1Department of Biological Chemistry, University of California, Irvine, CA 92697, USA.

Journal of Virology
|September 18, 2009
PubMed

Insights

Yeast retrotransposons like Ty3 use nuclear pore complexes for nuclear entry. Interactions between Ty3 Gag3 proteins and GLFG nucleoporins facilitate this transport, crucial for transposition.

Area of Science:

  • Molecular biology
  • Cell biology
  • Virology

Background:

  • Yeast retrotransposons replicate within intracellular particles.
  • Nuclear transport is essential for retrotransposon replication in yeast due to intact nuclear membranes during mitosis.
  • Ty3 retrotransposon particles associate with perinuclear P-body foci and interact with nuclear pore complexes (NPCs).

Purpose of the Study:

  • To investigate the role of FG (Phe-Gly) repeat domains in nucleoporins (Nups) for Ty3 nuclear transport.
  • To identify specific interactions between Ty3 virus-like particles and Nups.

Main Methods:

  • In vitro interaction assays between GLFG Nup domains and Ty3 Gag3 protein.
  • Analysis of Ty3 transposition in yeast strains with deleted GLFG repeats.
  • Examination of Gag3 domains and their localization within the cell.

Main Results:

  • GLFG Nup domains directly interacted with Ty3 Gag3 protein in vitro.
  • Mutations in the N-terminal domain of Gag3 disrupted the interaction with GLFG Nups.
  • Deletion of GLFG repeats reduced Ty3 transposition efficiency.
  • The spacer-nucleocapsid domain of Gag3 interacted with GLFG repeats, and nucleocapsid localized to the nucleus.

Conclusions:

  • Ty3 particle docking to NPCs is mediated by Gag3 interactions with GLFG Nups.
  • Nuclear entry of the preintegration complex is enhanced by nuclear localization signals in the nucleocapsid and integrase.

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