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The nucleus restricts several proteins within and allows others to pass. The restricted proteins possess a nuclear retention sequence or NRS, anchoring them to the nuclear lamins and preventing their transport to the cytosol. The non-restricted proteins, after their synthesis, are transported to their site of action, such as the cytosol or other organelles, with the help of nuclear export signals or NES.
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Before mRNAs are exported to the cytoplasm, it is crucial to check each mRNA for structural and functional integrity. Eukaryotic cells use several different mechanisms, collectively known as mRNA surveillance, to look for irregularities in mRNAs. Irregular or aberrant mRNA are rapidly degraded by various enzymes. If a defective mRNA escapes the surveillance, it would be translated into a protein which would either be non-functional or not function properly. One of the primary irregularities in...
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The RNA export factor Mex67 functions as a mobile nucleoporin.

Carina Patrizia Derrer1, Roberta Mancini1, Pascal Vallotton1

  • 1Institute of Biochemistry, ETH Zürich, Zurich, Switzerland.

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|November 23, 2019
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Summary

The RNA export factor Mex67 is crucial for mRNA transport through the nuclear pore complex (NPC). This study reveals Mex67 acts as a mobile NPC component, facilitating mRNA translocation to the cytoplasm.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Messenger RNA (mRNA) export from the nucleus is vital for gene expression.
  • The RNA export factor Mex67 is essential for mRNA transport via the nuclear pore complex (NPC) in yeast.
  • The precise molecular mechanism of Mex67-mediated mRNA export remains unclear.

Purpose of the Study:

  • To investigate the molecular mechanism by which Mex67 facilitates mRNA export.
  • To elucidate the role of Mex67's interaction with mRNA and the NPC.
  • To determine the functional localization of Mex67 during mRNA export.

Main Methods:

  • Quantitative fluorescence microscopy in live budding yeast cells.
  • Analysis of Mex67 localization and interaction with mRNA and NPC components.
  • Functional complementation assays using Mex67-Nup116 fusion protein.

Main Results:

  • Mex67 shows minimal interaction with mRNA in the nucleus and localizes to the NPC independently of mRNA.
  • Mex67 binds to FG repeats within the NPC, and this interaction is unaffected by the ATPase Dbp5.
  • The essential function of Mex67 is localized to the NPC, as demonstrated by rescuing a MEX67 deletion with a Mex67-Nup116 fusion.

Conclusions:

  • Mex67 functions as a mobile component of the NPC.
  • Mex67 receives mRNA export substrates within the NPC's central channel.
  • This mechanism facilitates the translocation of mRNA from the nucleus to the cytoplasm.