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Related Experiment Video

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Synthesis of an Intein-mediated Artificial Protein Hydrogel
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Amyloid-like interactions within nucleoporin FG hydrogels.

Christian Ader1, Steffen Frey, Werner Maas

  • 1Bijvoet Center for Biomolecular Research, Utrecht University, 3584 CH Utrecht, The Netherlands.

Proceedings of the National Academy of Sciences of the United States of America
|March 23, 2010
PubMed
Summary

The nucleoporin Nsp1p FG hydrogel barrier relies on Asn-rich beta-sheets for stability, not just hydrophobic interactions. These structures regulate nuclear transport receptor passage and prevent passive molecule flux.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Biophysics

Background:

  • The nuclear pore complex (NPC) regulates transport between the nucleus and cytoplasm.
  • Nucleoporins with FG repeats form a hydrogel barrier controlling molecular passage.
  • Previous models emphasized hydrophobic interactions for FG hydrogel formation.

Purpose of the Study:

  • To elucidate the structural basis of the Nsp1p FG hydrogel permeability barrier.
  • To identify novel intragel interactions beyond hydrophobic collapse.
  • To understand the role of Asn-rich regions in FG hydrogel stability and function.

Main Methods:

  • Solid-state NMR spectroscopy was employed to investigate FG hydrogel structure.
  • Analysis of FG repeat domain interactions, including N-terminal and C-terminal regions.
  • Comparison of FG hydrogel properties with yeast prion protein structures.

Main Results:

  • Identified intermolecular beta-sheets between Asn-rich spacer regions as kinetically stable structures.
  • Discovered transient hydrophobic interactions between Phe and methyl side chains.
  • Demonstrated that Asn-rich beta-structures are crucial for barrier integrity and nuclear transport receptor (NTR) passage.
  • Observed trans-interactions between FG repeats and yeast prion domains.

Conclusions:

  • Intermolecular beta-sheets in Asn-rich regions are key to FG hydrogel stability and function.
  • These beta-structures provide kinetic stability to suppress passive flux while allowing NTR passage.
  • Suggests a novel role for interchain beta-structures in maintaining nuclear pore permeability.