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Split-BioID &#8212; Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment
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Published on: April 20, 2018

A split active site couples cap recognition by Dcp2 to activation.

Stephen N Floor1, Brittnee N Jones, Gail A Hernandez

  • 1Graduate Group in Biophysics, University of California, San Francisco, California, USA.

Nature Structural & Molecular Biology
|August 17, 2010
PubMed
Summary
This summary is machine-generated.

Decapping by Dcp2, crucial for mRNA decay, involves a conformational change. This study reveals cap binding stabilizes the active site, with Dcp1 enhancing catalysis and promoting closure for efficient decapping.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Yeast Genetics

Background:

  • Decapping by Dcp2 is a critical step in the 5'-to-3' mRNA decay pathway.
  • The mechanism linking Dcp2's conformational changes (open-to-closed transition) to its catalytic activity in yeast remains unclear.

Purpose of the Study:

  • To elucidate the structural basis of cap binding by Dcp2.
  • To understand the role of Dcp1 in Dcp2 decapping activity and conformational changes.
  • To determine the relationship between Dcp2 closure and catalytic efficiency.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy to study cap binding.
  • Site-directed mutagenesis to probe cap-binding site residues.
  • Enzyme kinetics to measure catalytic activity.

Main Results:

  • NMR data show conserved residues on both catalytic and regulatory domains of Dcp2 bind the mRNA cap.
  • Mutations in the regulatory domain's cap-binding site significantly reduce catalytic activity and prevent Dcp2 closure.
  • Dcp1 enhances Dcp2's catalytic step by 10-fold and promotes the closed state.

Conclusions:

  • mRNA cap binding and Dcp2 closure are integral to the rate-limiting catalytic step of decapping.
  • Closure juxtaposes cap-binding regions from both domains, forming a composite active site.
  • Coactivators like Dcp1 may regulate decapping by stabilizing this composite active site.