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The Mtr2-Mex67 NTF2-like domain complex. Structural insights into a dual role of Mtr2 for yeast nuclear export

Claire Senay1, Paul Ferrari, Corinne Rocher

  • 1AFMB CNRS, UMR 6098, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France.

The Journal of Biological Chemistry
|September 25, 2003
PubMed

Insights

The Mtr2-Mex67 heterodimer is crucial for yeast mRNA export. Structural analysis reveals novel features in Mtr2, suggesting distinct roles in nuclear export and potential differences between yeast and human systems.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Cell Biology

Background:

  • The Mtr2-Mex67 heterodimer is essential for mRNA export in yeast.
  • This complex acts as a key nuclear component for transporting mRNA between nuclear and cytoplasmic compartments via the nuclear pore complex.

Purpose of the Study:

  • To determine the crystal structures of apo-Mtr2 from Candida albicans and its complex with the Mex67 NTF2-like domain.
  • To investigate the structural features of Mtr2 and its role in nuclear export.

Main Methods:

  • X-ray crystallography was used to obtain the structures of Mtr2 and the Mtr2-Mex67 complex.
  • Structural comparison with other NTF2 fold family members was performed.

Main Results:

  • The crystal structures of apo-Mtr2 and the Mtr2-Mex67 NTF2-like domain complex were determined.
  • Mtr2 exhibits novel structural features, including involvement in large ribosomal subunit export.
  • Three putative Phe-Gly repeat binding sites were identified in the complex, with one at the heterodimer interface.

Conclusions:

  • The study highlights the adaptability of the NTF2 fold and identifies novel structural determinants in the yeast Mtr2-Mex67 complex.
  • Findings suggest potential differences between yeast and human mRNA export machineries.
  • Mtr2 appears to have a dual functional role in yeast nuclear export events.

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