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Molecular architecture of LSM14 interactions involved in the assembly of mRNA silencing complexes

Tobias Brandmann1, Hana Fakim2,3, Zoya Padamsi2,3

  • 1Department of Biochemistry, University of Zurich, Zurich, Switzerland.

The EMBO Journal
|March 8, 2018
PubMed

Insights

The LSM14 protein interacts with 4E-T and DDX6, crucial for mRNA silencing and P-body assembly. Structural studies reveal LSM14

Area of Science:

  • Molecular and Cellular Biology
  • Structural Biology
  • RNA Biology

Background:

  • LSM14/Rap55 is vital for mRNA decapping, translational repression, and P-body formation.
  • The precise interactions of LSM14 with mRNA silencing factors like 4E-T and DDX6 remain unclear.

Purpose of the Study:

  • To elucidate the structural basis of LSM14 interactions with 4E-T and DDX6.
  • To understand how these interactions contribute to mRNA silencing complex formation and P-body assembly.

Main Methods:

  • X-ray crystallography was used to determine the structures of LSM14 bound to 4E-T and DDX6.
  • Mutational analyses and proteomic studies were employed to validate structural findings.

Main Results:

  • The crystal structure of LSM14's LSM domain bound to a 4E-T C-terminal fragment revealed a bi-partite motif interaction.
  • The crystal structure of LSM14 bound to DDX6's C-terminal domain showed a unique, non-contiguous binding motif.
  • LSM14 utilizes a divergent binding mode with DDX6 compared to other interacting proteins.

Conclusions:

  • LSM14 employs distinct structural mechanisms to bind 4E-T and DDX6.
  • These unique interactions are essential for the assembly of mRNA silencing complexes and P-bodies.
  • The findings provide critical insights into the regulation of gene expression by RNA granules.
Keywords:
P‐bodiesSLIMsmRNA decappingprotein–protein interaction networkstranslational repression

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