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The structure of the Pan2-Pan3 core complex reveals cross-talk between deadenylase and pseudokinase

Ingmar B Schäfer1, Michaela Rode1, Fabien Bonneau1

  • 1Structural Cell Biology Department, Max Planck Institute of Biochemistry, Martinsried, Germany.

Nature Structural & Molecular Biology
|June 2, 2014
PubMed

Insights

The Pan2-Pan3 complex shortens mRNA poly(A) tails for turnover. Structural analysis reveals its unique 1:2 stoichiometry and how its nuclease and regulator domains cooperate for efficient deadenylation.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • The Pan2-Pan3 complex is crucial for eukaryotic mRNA turnover.
  • It initiates mRNA decay by shortening poly(A) tails.

Purpose of the Study:

  • To elucidate the structural basis of Pan2-Pan3 complex function.
  • To understand the mechanism of deadenylation mediated by Pan2-Pan3.

Main Methods:

  • Recombinant protein expression and purification.
  • In vitro RNA deadenylation assays.
  • X-ray crystallography of the Pan2-Pan3 core complex.

Main Results:

  • Recombinant Saccharomyces cerevisiae Pan2-Pan3 complex deadenylates RNA in vitro without Pab1.
  • The crystal structure reveals a 1:2 Pan2:Pan3 stoichiometry due to Pan3 homodimer asymmetry.
  • Interactions between Pan2 domains and Pan3 orient the active site for efficient deadenylation.

Conclusions:

  • The Pan2-Pan3 complex's molecular architecture facilitates synergistic action between its nuclease and pseudokinase components.
  • This structure provides mechanistic insights into mRNA deadenylation and turnover.

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