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Human CSTF2 RNA Recognition Motif Domain Binds to a U-Rich RNA Sequence through a Multistep Binding Process.

Elahe Masoumzadeh1, Michael P Latham1,2

  • 1Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, Texas 79409, United States.

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The CSTF2 RNA recognition motif (RRM) binds U-rich RNA through a multistep process. This study reveals dynamic interactions and structural changes crucial for regulating mRNA cleavage and polyadenylation.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • The RNA recognition motif (RRM) is a key RNA-binding domain involved in various mRNA processing events.
  • The CSTF2 RRM specifically recognizes U- or G/U-rich sequences in pre-mRNA, regulating cleavage and polyadenylation.
  • Alternative cleavage and polyadenylation significantly contribute to mRNA diversity, but the CSTF2 RRM binding mechanism remains unclear.

Purpose of the Study:

  • To elucidate the molecular mechanism by which the CSTF2 RRM domain interacts with U-rich RNA ligands.
  • To characterize the binding process and identify key structural and dynamic features involved in RNA recognition.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) titration and spin relaxation experiments were employed.
  • Paramagnetic relaxation enhancement (PRE) measurements and rigid-body docking were utilized to complement NMR data.

Main Results:

  • A multistep RNA binding process for the CSTF2 RRM was revealed.
  • Significant differences in picosecond-to-nanosecond (ps-ns) timescale dynamics were observed.
  • Potential structural alterations, particularly in the C-terminal α-helix, were identified during ligand binding.

Conclusions:

  • The study provides novel insights into the dynamic binding of the CSTF2 RRM to U-rich RNA.
  • Understanding these interactions is crucial for comprehending the regulation of pre-mRNA cleavage and polyadenylation.
  • This work lays the foundation for further structural and mechanistic studies of RRM-RNA interactions.