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Published online November 5, 2007
doi:10.1083/jcb.200704147
The Journal of Cell Biology, Vol. 179, No. 3, 437-449
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Decker et al.
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Article

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



Carolyn J. Decker, Daniela Teixeira, and Roy Parker

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

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

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.

D. Teixeira's present address is Instituto de Ciencias Biomedica Abel Salazar, Universidade do Porto, Porto 4099-003, Portugal.

Abbreviations used in this paper: miRNA, microRNA; P-body, processing body; Q/N, glutamine/asparagine; SC, synthetic medium; YP, yeast extract/peptone medium.


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