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Method for the Isolation and Identification of mRNAs, microRNAs and Protein Components of Ribonucleoprotein Complexes from Cell Extracts using RIP-Chip
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Method for the Isolation and Identification of mRNAs, microRNAs and Protein Components of Ribonucleoprotein Complexes from Cell Extracts using RIP-Chip

Published on: September 29, 2012

Structural and functional analysis of the interaction between the nucleoporin Nup98 and the mRNA export factor Rae1

Yi Ren1, Hyuk-Soo Seo, Günter Blobel

  • 1Laboratory of Cell Biology, Howard Hughes Medical Institute, The Rockefeller University, New York, NY 10065, USA.

Proceedings of the National Academy of Sciences of the United States of America
|May 26, 2010
PubMed

Insights

The crystal structure reveals how Ribonucleic acid export 1 (Rae1) and Nup98 interact to bind messenger ribonucleoprotein particles (mRNPs). This interaction is crucial for mRNA export, a key step in gene expression.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Cell Biology

Background:

  • Messenger RNA (mRNA) export from the nucleus is essential for protein synthesis.
  • Ribonucleic acid export 1 (Rae1) and Nup98 are key proteins involved in mRNA export.
  • Viral proteins can hijack these export factors to disrupt host cell function.

Purpose of the Study:

  • To determine the structural basis of the interaction between human Rae1 and the Nup98 Gle2-binding sequence (GLEBS).
  • To elucidate the role of this complex in the mRNA export pathway.

Main Methods:

  • X-ray crystallography was used to determine the structure of the Rae1-Nup98(GLEBS) complex at 1.65 A resolution.

Main Results:

  • The structure reveals Rae1 as a seven-bladed beta-propeller that binds the Nup98 GLEBS motif via its C-terminal arm.
  • A tandem glutamate element in the Nup98 C-terminal arm is critical for binding to a hydrophobic surface on Rae1.
  • The Rae1-Nup98 complex exhibits single-stranded RNA-binding capability.

Conclusions:

  • The Rae1-Nup98 complex directly binds to messenger ribonucleoprotein particles (mRNPs).
  • This interaction likely plays a significant role at multiple stages of the mRNA export pathway.
  • Understanding this interaction provides insights into nuclear export mechanisms and potential viral interference strategies.

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