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Structure of a Human 4E-T/DDX6/CNOT1 Complex Reveals the Different Interplay of DDX6-Binding Proteins with the

Sevim Ozgur1, Jérôme Basquin1, Anastasiia Kamenska2

  • 1Department of Structural Cell Biology, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried/Munich, Germany.

Cell Reports
|October 23, 2015
PubMed

Insights

DEAD-box protein DDX6 is key for translational repression. Its interaction with 4E-T protein, revealed by structural analysis, highlights a complex regulatory network involving other repressors like Edc3 and Pat1.

Area of Science:

  • Molecular biology
  • Structural biology
  • Gene regulation

Background:

  • DEAD-box protein DDX6 is crucial for translational repression in oocytes and somatic cells.
  • DDX6 interacts with the CCR4-NOT complex and regulators like Edc3, Pat1, and 4E-T.

Purpose of the Study:

  • To elucidate the structural basis of 4E-T's interaction with DDX6 and CNOT1.
  • To compare the binding modes of different DDX6-interacting proteins.

Main Methods:

  • X-ray crystallography to determine the ternary complex structure at 2.1 Å resolution.
  • Biochemical assays to study protein-protein interactions in vitro.

Main Results:

  • The conserved CUP-homology domain (CHD) of 4E-T directly binds DDX6, independent of CNOT1's MIF4G domain.
  • Structural data reveals how 4E-T CHD interacts with DDX6 and CNOT1.
  • 4E-T CHD shares a DDX6-binding surface with Edc3 and Pat1, but exhibits distinct binding dynamics with CNOT1.

Conclusions:

  • 4E-T utilizes a conserved surface on DDX6, but its interaction with the CCR4-NOT complex differs from Edc3 and Pat1.
  • This suggests a complex network of simultaneous and mutually exclusive interactions governing DDX6-mediated repression.

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