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PUF proteins bind Pop2p to regulate messenger RNAs

Aaron C Goldstrohm1, Brad A Hook, Daniel J Seay

  • 1Department of Biochemistry, 433 Babcock Drive, University of Wisconsin, Madison, Wisconsin 53706, USA.

Nature Structural & Molecular Biology
|May 23, 2006
PubMed

Insights

PUF proteins bind Pop2p to enhance mRNA deadenylation and decay. This conserved interaction recruits deadenylase complexes, controlling gene expression via mRNA stability.

Area of Science:

  • Molecular Biology
  • Gene Regulation
  • RNA Biology

Background:

  • PUF proteins are RNA-binding proteins that regulate mRNA translation and stability.
  • PUF proteins commonly induce mRNA decay through poly(A) tail removal (deadenylation).

Purpose of the Study:

  • To investigate the mechanism by which PUF proteins enhance deadenylation and mRNA decay.
  • To identify the specific protein interactions involved in PUF-mediated mRNA regulation.

Main Methods:

  • Biochemical assays to test protein-protein interactions.
  • In vitro reconstitution of deadenylation.
  • Functional assays in yeast, C. elegans, and human cells.

Main Results:

  • A yeast PUF protein physically binds Pop2p, a component of the Ccr4p-Pop2p-Not deadenylase complex.
  • Pop2p is essential for PUF protein-mediated repression of gene expression.
  • PUF proteins recruit the Ccr4p deadenylase, Dcp1p, and Dhh1p to target mRNAs via Pop2p.
  • The PUF-Pop2p interaction is evolutionarily conserved across yeast, worms, and humans.

Conclusions:

  • The interaction between PUF proteins and Pop2p is a key mechanism for regulated deadenylation and mRNA decay.
  • This interaction facilitates the recruitment of multiple mRNA regulatory enzymes, leading to repression of gene expression.
  • The conserved nature of this interaction highlights its fundamental importance in eukaryotic gene regulation.

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