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Updated: Jul 15, 2026

Analysis of mRNA Nuclear Export Kinetics in Mammalian Cells by Microinjection
Published on: December 4, 2010
Nuclear export of ribosomal 60S subunits by the general mRNA export receptor Mex67-Mtr2
Wei Yao1, Daniela Roser, Alwin Köhler
1Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany.
Abstract:
The yeast Mex67-Mtr2 complex and its homologous metazoan counterpart TAP-p15 operate as nuclear export receptors by binding and translocating mRNA through the nuclear pore complexes. Here, we show how Mex67-Mtr2 can also function in the nuclear export of the ribosomal 60S subunit. Biochemical and genetic studies reveal a previously unrecognized interaction surface on the NTF2-like scaffold of the Mex67-Mtr2 heterodimer, which in vivo binds to pre-60S particles and in vitro can interact with 5S rRNA. Crucial structural requirements for this binding platform are loop insertions in the middle domain of Mex67 and Mtr2, which are absent from human TAP-p15. Notably, when the positively charged amino acids in the Mex67 loop are mutated, interaction of Mex67-Mtr2 with pre-60S particles and 5S rRNA is inhibited, and 60S subunits, but not mRNA, accumulate in the nucleus. Thus, the general mRNA exporter Mex67-Mtr2 contains a distinct electrostatic interaction surface for transporting 60S preribosomal cargo.
Insights
The Mex67-Mtr2 complex exports mRNA and also functions in ribosomal 60S subunit export. A novel interaction surface on Mex67-Mtr2 binds pre-60S particles and 5S rRNA, crucial for nuclear export.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- The Mex67-Mtr2 complex is a key mRNA nuclear export receptor in yeast.
- Its metazoan homolog, TAP-p15, also functions in mRNA export.
Purpose of the Study:
- To investigate the role of the yeast Mex67-Mtr2 complex beyond mRNA export.
- To identify novel interaction partners and functions of Mex67-Mtr2.
Main Methods:
- Biochemical assays to study protein-protein and protein-RNA interactions.
- Genetic studies in yeast to analyze nuclear export pathways.
- Structural analysis of the Mex67-Mtr2 complex.
Main Results:
- Mex67-Mtr2 mediates the nuclear export of the ribosomal 60S subunit.
- A new interaction surface on Mex67-Mtr2 binds pre-60S particles and 5S rRNA.
- Mutations in specific loops of Mex67-Mtr2 disrupt 60S subunit export, causing nuclear accumulation.
Conclusions:
- The Mex67-Mtr2 complex possesses a dual role in nuclear export, handling both mRNA and ribosomal subunits.
- A distinct electrostatic interaction surface on Mex67-Mtr2 is responsible for binding 60S preribosomal cargo.
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