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HuR biological function involves RRM3-mediated dimerization and RNA binding by all three RRMs.

Marta Pabis1,2,3, Grzegorz M Popowicz1,2, Ralf Stehle1,2

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • HuR (ELAVL1) is an RNA-binding protein crucial for cellular differentiation and stress response by stabilizing mRNA targets.
  • The structural and RNA-binding mechanisms of HuR's RRM3 domain and full-length protein are not well understood.

Purpose of the Study:

  • To elucidate the structural basis of RNA recognition by HuR, particularly focusing on the RRM3 domain and its role in full-length protein function.
  • To investigate the conformational changes of HuR upon RNA binding and the significance of RRM3 dimerization.

Main Methods:

  • X-ray crystallography to determine structures of RRM3 (free and RNA-bound) and tandem RRM1,2-RNA complexes.
  • Nuclear Magnetic Resonance (NMR) and Small-Angle X-ray Scattering (SAXS) to analyze protein dynamics and conformation.
  • Biochemical assays and mutational analysis to assess RNA binding, dimerization, and functional activity.

Main Results:

  • Crystal structures reveal RRM3's canonical RNA interactions and a dimerization interface.
  • NMR and SAXS show flexible RRM connections in free HuR, becoming more compact upon RNA binding.
  • A structural model for RNA recognition by all three HuR RRMs is proposed.
  • RRM3 dimerization and RNA binding are essential for HuR's in vitro activity and in vivo mRNA regulation.

Conclusions:

  • The RRM3 domain plays a critical role in HuR's RNA binding, dimerization, and overall function.
  • HuR undergoes significant conformational changes upon RNA binding, mediated by inter-RRM flexibility.
  • These findings provide insights into the fine-tuning mechanisms of HuR activity in human cells.