Reference: Rao BS and Parker R (2017) Numerous interactions act redundantly to assemble a tunable size of P bodies in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 114(45):E9569-E9578

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Abstract


Eukaryotic cells contain multiple RNA-protein assemblies referred to as RNP granules, which are thought to form through multiple protein-protein interactions analogous to a liquid-liquid phase separation. One class of RNP granules consists of P bodies, which consist of nontranslating mRNAs and the general translation repression and mRNA degradation machinery. P bodies have been suggested to form predominantly through interactions of EDC3 and a prion-like domain on LSM4. In this work, we provide evidence that P-body assembly can be driven by multiple different protein-protein and/or protein-RNA interactions, including interactions involving DHH1, PSP2, and PBY1. Moreover, the relative importance of specific interactions can vary with different growth conditions. Based on these observations, we develop a summative model wherein the P-body assembly phenotype of a given mutant can be predicted from the number of currently known protein-protein interactions between P-body components.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Rao BS, Parker R
Primary Lit For
PAB1 | DHH1 | LSM1 | DCP2

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