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Related Experiment Videos

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

C T DeMaria1, Y Sun, L Long

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

The Journal of Biological Chemistry
|November 5, 1997
PubMed
Summary
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The RNA-binding protein AUF1 (AU-rich element binding factor 1) requires specific domains beyond its RNA recognition motifs for high-affinity binding to mRNA. Protein-protein interactions are crucial for AUF1

Area of Science:

  • Molecular Biology
  • Gene Regulation
  • Protein-RNA Interactions

Background:

  • AUF1 (AU-rich element binding factor 1) is an RNA-binding protein with two RNA recognition motifs (RRMs).
  • AUF1 binds to A+U-rich elements (AREs) in mRNAs, influencing the processing and degradation of transcripts.
  • This regulation affects mRNAs encoding critical proteins like cytokines, oncoproteins, and G protein-coupled receptors.

Purpose of the Study:

  • To identify the specific domains of AUF1 responsible for its high-affinity binding to AREs.
  • To elucidate the role of different AUF1 domains in RNA binding and protein-protein interactions.

Main Methods:

  • Analysis of RNA binding affinities of various AUF1 mutants.
  • Examination of the role of N-terminal and C-terminal regions in ARE binding.

Related Experiment Videos

  • Investigation of AUF1 dimerization and oligomerization states.

    • Main Results:

    • Both RRMs of AUF1 are necessary but not sufficient for high-affinity binding to the human c-fos ARE.
    • An N-terminal alanine-rich region and a C-terminal glutamine-rich region are essential for maximal binding.
    • The N-terminus mediates dimerization, and AUF1 binds AREs as a hexamer, highlighting the importance of protein-protein interactions.

    Conclusions:

    • High-affinity ARE binding by AUF1 depends on a complex interplay between its RRMs, specific terminal regions, and oligomeric state.
    • Protein-protein interactions, particularly hexamer formation, are critical for the functional binding of AUF1 to target mRNAs.
    • These findings provide insights into the molecular mechanisms governing mRNA decay pathways regulated by AUF1.