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Published online
doi:10.1083/jcb.200807043
The Journal of Cell Biology, Vol. 183, No. 3, 441-455
The Rockefeller University Press, 0021-9525 $30.00
© Buchan et al.
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Article

P bodies promote stress granule assembly in Saccharomyces cerevisiae



J. Ross Buchan, Denise Muhlrad, and Roy Parker

Department of Molecular and Cellular Biology, and Howard Hughes Medical Institute, University of Arizona, Tucson, AZ 85721

Correspondence to Roy Parker: rrparker{at}u.arizona.edu

Recent results indicate that nontranslating mRNAs in eukaryotic cells exist in distinct biochemical states that accumulate in P bodies and stress granules, although the nature of interactions between these particles is unknown. We demonstrate in Saccharomyces cerevisiae that RNA granules with similar protein composition and assembly mechanisms as mammalian stress granules form during glucose deprivation. Stress granule assembly is dependent on P-body formation, whereas P-body assembly is independent of stress granule formation. This suggests that stress granules primarily form from mRNPs in preexisting P bodies, which is also supported by the kinetics of P-body and stress granule formation both in yeast and mammalian cells. These observations argue that P bodies are important sites for decisions of mRNA fate and that stress granules, at least in yeast, primarily represent pools of mRNAs stalled in the process of reentry into translation from P bodies.

Abbreviations used in this paper: mRNP, messenger ribonucleoprotein; Pabp, poly(A) binding protein; YEPD, yeast extract peptone dextrose.

© 2008 Buchan et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).


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