Fission Yeast Puf2, a Pumilio and FBF Family RNA-Binding Protein, Links Stress Granules to Processing Bodies
| Autor: | Wan-Yi Hsiao, Yi-Ting Wang, Shao-Win Wang |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Cytoplasm
RNA Stability RNA-binding protein Biology Cytoplasmic Granules Poly(A)-Binding Proteins Green fluorescent protein 03 medical and health sciences 0302 clinical medicine Stress granule Stress Physiological Schizosaccharomyces RNA Messenger Molecular Biology 030304 developmental biology Ribonucleoprotein 0303 health sciences Binding protein RNA-Binding Proteins RNA Fungal Translation (biology) Cell Biology biology.organism_classification Yeast Cell biology Ribonucleoproteins Schizosaccharomyces pombe RNA Schizosaccharomyces pombe Proteins 030217 neurology & neurosurgery Transcription Factors Research Article |
| Zdroj: | Mol Cell Biol |
| ISSN: | 1098-5549 |
| Popis: | Stress granules (SGs) are cytoplasmic aggregates formed upon stress when untranslated messenger ribonucleoproteins accumulate in the cells. In a green fluorescent protein library screening of the fission yeast SG proteins, Puf2 of the PUF family of RNA-binding proteins was identified that is required for SG formation after deprivation of glucose. Accordingly, the puf2 mutant is defective in recovery from glucose starvation with a much longer lag to reenter the cell cycle. In keeping with these results, Puf2 contains several low-complexity and intrinsically disordered protein regions with a tendency to form aggregates and, when overexpressed, it represses translation to induce aggregation of poly(A) binding protein Pabp, the signature constituent of SGs. Intriguingly, overexpression of Puf2 also enhances the structure of processing bodies (PBs), another type of cytoplasmic RNA granule, a complex of factors involved in mRNA degradation. In this study, we demonstrate a function of the fission yeast PB in SG formation and show Puf2 may provide a link between these two structures. |
| Databáze: | OpenAIRE |
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