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Related Experiment Videos

Structural determination in AUF1 required for high affinity binding to A + U-rich elements

C T DeMaria1, Y Sun, B J Wagner

  • 1Department of Microbiology and Immunology, Bowman Gray School of Medicine of Wake Forest University, Winston-Salem, NC 27157-1064, USA.

Nucleic Acids Symposium Series
|January 1, 1997
PubMed
Summary
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The RNA-binding protein AUF1 (AU-rich element binding protein 1) binds messenger RNAs containing AU-rich elements. Highest affinity binding requires specific protein domains and multimerization, impacting mRNA degradation.

Area of Science:

  • Molecular Biology
  • RNA Biology
  • Protein-RNA Interactions

Background:

  • AUF1 (AU-rich element binding protein 1) is a key RNA-binding protein.
  • It interacts with AU-rich elements (AREs) found in the 3' untranslated regions of specific mRNAs.
  • This interaction is critical for regulating the stability and degradation of mRNAs encoding cytokines, oncoproteins, and G protein-coupled receptors.

Purpose of the Study:

  • To identify the specific domains of AUF1 responsible for high-affinity binding to AREs.
  • To elucidate the role of protein structure and interactions in AUF1's ARE-binding activity.

Main Methods:

  • Analysis of AUF1 mutants with altered domain structures.
  • Assessment of binding affinities of wild-type and mutant AUF1 to AREs.

Related Experiment Videos

  • Investigation of AUF1 oligomerization states during ARE binding.

    • Main Results:

    • Both RNA recognition motifs (RRMs) of AUF1 are necessary but not sufficient for high-affinity ARE binding.
    • Optimal binding requires an N-terminal alanine/glycine-rich region and a C-terminal glutamine-rich region.
    • AUF1 dimerization, mediated by the N-terminus, is essential, and the protein binds AREs as a hexamer.

    Conclusions:

    • High-affinity binding of AUF1 to AREs is a complex process.
    • It depends not only on RNA recognition motifs but also on specific N- and C-terminal regions.
    • Protein-protein interactions and multimerization into a hexameric complex are crucial for AUF1's regulatory function.