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

J Cell Biol. 2007 Nov 5;179(3):437-49. doi: 10.1083/jcb.200704147.

Abstract

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

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

Substances

  • EDC3 protein, S cerevisiae
  • LSM4 protein, S cerevisiae
  • Oligonucleotides
  • Ribonucleoprotein, U4-U6 Small Nuclear
  • Ribonucleoproteins
  • Saccharomyces cerevisiae Proteins
  • messenger ribonucleoprotein
  • Glutamine
  • Asparagine