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Structural and Dynamic Insights into Redundant Function of YTHDF Proteins

Yaozong Li1,2, Rajiv K Bedi1, Elena V Moroz-Omori1

  • 1Department of Biochemistry, University of Zurich, CH-8057 Zurich, Switzerland.

Journal of Chemical Information and Modeling
|October 19, 2020
PubMed

Insights

Three YTH-domain proteins (YTHDF1-3) interact identically with N-methyladenosine (m6A) RNA. Structural and simulation data reveal redundant cellular functions for these m6A readers.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • The YTH domain family, comprising YTHDF1, YTHDF2, and YTHDF3, are known to bind N-methyladenosine (m6A)-modified RNA.
  • The functional redundancy among these three m6A reader proteins has been a subject of ongoing debate in cellular biology.

Discussion:

  • This study employed X-ray crystallography and molecular dynamics (MD) simulations to elucidate the interaction between YTHDF proteins and m6A-containing RNA.
  • Analysis of the structural data and simulation trajectories revealed conserved binding modes and intrinsic protein plasticity across YTHDF1, YTHDF2, and YTHDF3.

Key Insights:

  • The three YTHDF proteins exhibit identical interaction patterns with m6A-modified RNA.
  • Similar intrinsic plasticity observed in YTHDF1, YTHDF2, and YTHDF3 suggests overlapping functional capabilities.
  • These findings provide structural evidence supporting the redundant roles of YTHDF proteins in cellular processes involving m6A RNA recognition.

Outlook:

  • Further investigation into the specific cellular contexts and downstream pathways where YTHDF redundancy is critical.
  • Exploring potential differential roles or regulatory mechanisms that might fine-tune the functions of these seemingly redundant proteins.
  • Understanding the implications of YTHDF protein redundancy for mRNA regulation and cellular responses to m6A modification.

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