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Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae.

Processing bodies (P-bodies) are cytoplasmic RNA granules that contain translationally repressed messenger ribonucleoproteins (mRNPs) and messenger RNA (mRNA) decay factors. The physical interactions that form the individual mRNPs within P-bodies and how those mRNPs assemble into larger P-bodies are unresolved. We identify direct protein interactions that could contribute to the formation of an mRNP complex that consists of core P-body components. Additionally, we demonstrate that the formation of P-bodies that are visible by light microscopy occurs either through Edc3p, which acts as a scaffold and cross-bridging protein, or via the "prionlike" domain in Lsm4p. Analysis of cells defective in P-body formation indicates that the concentration of translationally repressed mRNPs and decay factors into microscopically visible P-bodies is not necessary for basal control of translation repression and mRNA decay. These results suggest a stepwise model for P-body assembly with the initial formation of a core mRNA-protein complex that then aggregates through multiple specific mechanisms.

Pubmed ID: 17984320


  • Decker CJ
  • Teixeira D
  • Parker R


The Journal of cell biology

Publication Data

November 5, 2007

Associated Grants

  • Agency: NCRR NIH HHS, Id: P41 RR1183
  • Agency: NIGMS NIH HHS, Id: R37 GM45443

Mesh Terms

  • Asparagine
  • Cytoplasm
  • Glutamine
  • Models, Biological
  • Oligonucleotides
  • Protein Biosynthesis
  • Protein Structure, Tertiary
  • RNA Stability
  • Ribonucleoprotein, U4-U6 Small Nuclear
  • Ribonucleoproteins
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Two-Hybrid System Techniques