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MBC in Press, published online ahead of print December 27, 2007
Mol. Biol. Cell 10.1091/mbc.E07-09-0954

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Submitted on September 24, 2007
Revised on November 27, 2007
Accepted on December 19, 2007

The DEAD-Box RNA Helicase Ded1p Affects and Accumulates in Saccharomyces cerevisiae P-Bodies

Carla Beckham,* Angela Hilliker,{dagger}{ddagger} Anne-Marie Cziko,{sect} Amine Noueiry,|| Mani Ramaswami,{dagger}{sect} and Roy Parker{dagger}{ddagger}

*Department of Cell Biology and Anatomy, {dagger}Department of Molecular and Cellular Biology, {sect}Program in Neuroscience, and {ddagger}Howard Hughes Medical Institute, University of Arizona, Tucson, AZ 85721-0206; ||Davis College of Agriculture, Forestry and Consumer Science, West Virginia University, Morgantown, WV 26506-6010

Monitoring Editor: Thomas Fox

Recent results suggest that cytoplasmic mRNAs can form translationally repressed mRNPs capable of decapping and degradation, or accumulation into cytoplasmic processing bodies (P-bodies), which can function as sites of mRNA storage. The proteins that function in transitions between the translationally repressed mRNPs that accumulate in P-bodies and mRNPs engaged in translation are largely unknown. Herein, we demonstrate that the yeast translation initiation factor Ded1p can localize to P-bodies. Moreover, depletion of Ded1p leads to defects in P-body formation. Overexpression of Ded1p results in increased size and number of P-bodies and inhibition of growth in a manner partially suppressed by loss of Pat1p, Dhh1p, or Lsm1p. Mutations that inactivate the ATPase activity of Ded1p increase the overexpression growth inhibition of Ded1p, and prevent Ded1p from localizing in P-bodies. Combined with earlier work showing Ded1p can have a positive effect on translation, these results suggest that Ded1p is a bifunctional protein that can affect both translation initiation and P-body formation.

Address correspondence to: Roy Parker (rrparker{at}u.arizona.edu)






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