A role for Q/N-rich aggregation-prone regions in P-body localization

Martin A. M. Reijns, Ross D. Alexander, Michael P. Spiller, Jean D. Beggs

Research output: Contribution to journalArticle

Abstract

P-bodies are cytoplasmic foci that are sites of mRNA degradation and translational repression. It is not known what causes the accumulation of RNA-degradation factors in P-bodies, although RNA is required. The yeast Lsm1-7p complex (comprising Lsm1p to Lsm7p) is recruited to P-bodies under certain stress conditions. It is required for efficient decapping and degradation of mRNAs, but not for the assembly of P-bodies. Here we show that the Lsm4p subunit and its asparagine-rich C-terminus are prone to aggregation, and that this tendency to aggregate promotes efficient accumulation of Lsm1-7p in P-bodies. The presence of glutamine- and/or asparagine-rich (Q/N-rich) regions in other P-body components suggests a more general role for aggregation-prone residues in P-body localization and assembly. This is supported by reduced P-body accumulation of Ccr4p, Pop2p and Dhh1p after deletion of these domains, and by the observed aggregation of the Q/N-rich region from Ccr4p.

Original languageEnglish
Pages (from-to)2463-2472
Number of pages10
JournalJournal of Cell Science
Volume121
Issue number15
DOIs
Publication statusPublished - 2008

Keywords

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Asparagine/analysis
  • Cytoplasm/metabolism
  • Cytoplasmic Granules/metabolism
  • Glutamine/analysis
  • Molecular Sequence Data
  • RNA Stability/physiology
  • RNA, Messenger/metabolism
  • Ribonucleoprotein, U4-U6 Small Nuclear/chemistry
  • Saccharomyces cerevisiae/genetics
  • Saccharomyces cerevisiae Proteins/chemistry

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