P-bodies are cytoplasmic RNA granules containing the Dcp1-Dcp2 decapping-enzymes where mRNA decay can occur. Here we described the characterization of P-bodies in the fission yeast Schizosaccharomyces pombe. Most informations on the property and function of P-bodies stem from studies in the distant related budding yeast Saccharomyces cerevisiae, and Edc3 was identified as a scaffold protein required for P-body assembly. However, we found that, unlike in S. cerevisiae, fission yeast Edc3 was dispensable for P-body formation. Pdc1, a novel partner of the fission yeast decapping-enzyme, with a limited-similarity to plant Edc4/Varicose that required for the assembly of P-body was identified (TAP-MALDI/MS/MS). Pdc1 interacts with Dcp2 through its C-terminal and contains a colied-coli region for self-interaction to mediate P-body formation. In line with the model that Pdc1 cross-bridging different proteins, additional interactions can be demonstrated with components such as Edc3 and Ste13. Although not required for the interaction between Dcp1 and Dcp2, our data suggests that Pdc1 acts as a functional homologue of Edc4, a third component of the decapping-enzymes that is thought to be absent from fungi. Together, these results highlight the diverse P-body protein composition between different species and might help to provide insight into their evolutional path.
Date:
2013-03
Relation:
Molecular and Cellular Biology. 2013 Mar;33(6):1244-1253.
