QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

Vol. 19, Issue 3, 984-993, March 2008

This Article Full Text Full Text (PDF) All Versions of this Article: E07-09-0954v1 19/3/984    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Google Scholar Articles by Beckham, C. Articles by Parker, R. PubMed PubMed Citation Articles by Beckham, C. Articles by Parker, R.

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

Carla Beckham^*, Angela Hilliker^,, Anne-Marie Cziko, Amine Noueiry^||, Mani Ramaswami^,, and Roy Parker^,

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

Submitted September 24, 2007; Revised November 27, 2007; Accepted December 19, 2007
Monitoring Editor: Thomas Fox

Recent results suggest that cytoplasmic mRNAs can form translationally repressed messenger ribonucleoprotein particles (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)