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Related Experiment Video

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Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
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UHM-ULM interactions in the RBM39-U2AF65 splicing-factor complex.

Galina A Stepanyuk1, Pedro Serrano1, Eigen Peralta2

  • 1Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.

Acta Crystallographica. Section D, Structural Biology
|April 7, 2016
PubMed
Summary

RNA-binding protein 39 (RBM39) is crucial for cancer progression. This study reveals the structural basis of RBM39

Keywords:
CAPERαHCC1RBM39RNA-binding protein 39RNA-binding proteinsU2AF homology motifU2AF5UHMULMalternative splicing

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Cancer Research

Background:

  • RNA-binding protein 39 (RBM39) functions as a splicing factor and transcriptional co-activator, implicated in cancer progression.
  • The RBM39 C-terminal RRM domain contains a U2AF homology motif (UHM) that mediates protein interactions via a UHM-ligand motif (ULM).

Purpose of the Study:

  • To elucidate the structural basis of RBM39-U2AF65 interactions.
  • To understand the specificity of UHM-ULM interactions in splicing factors.

Main Methods:

  • X-ray crystallography to determine structures of RBM39-UHM and its complex with U2AF65-ULM.
  • Solution NMR spectroscopy for RBM39-UHM structure determination.
  • Co-immunoprecipitation, isothermal titration calorimetry, and NMR chemical shift perturbation to confirm protein interactions.

Main Results:

  • Crystal and NMR structures of the RBM39-UHM domain were determined.
  • The crystal structure of the RBM39-UHM/U2AF65-ULM complex revealed specific binding interfaces.
  • Experimental methods confirmed the RBM39-U2AF65 interaction and characterized its binding thermodynamics and kinetics.

Conclusions:

  • The study establishes a structural foundation for specific UHM-ULM interactions involving splicing factors.
  • This work provides insights into the molecular mechanisms governing alternative splicing in diseases.