Abstract
uvi15+ is induced by various stresses including exposure to UV-light. Previously, we demonstrated that the UV-induction is mainly regulated at the post-transcriptional level through a cis-acting element in the pre-mRNA. Here we show that deletion analyses define an 18-nt element responsible for the UV-induction. RNA gel mobility shift assay showed that a specific protein(s) could form a complex with the 54-nt element but its binding ability is moderately decreased in response to UV-light. Using yeast three-hybrid screen, we isolated a homolog of fibrillarin as a protein interacting with the 54-nt element, which is a key nucleolar protein for pre-rRNA processing. We further showed that the recombinant fibrillarin specifically binds to the element in a sequence-specific manner. Thus, the data suggest that fission yeast fibrillarin might regulate uvi15+ mRNA stability via binding with the 54-nt element in the pre-mRNA, implying that fibrillarin is involved in both pre-mRNA and pre-rRNA processing.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1184-1190 |
| Number of pages | 7 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 294 |
| Issue number | 5 |
| DOIs | |
| State | Published - 2002 |
| Externally published | Yes |
Keywords
- Fibrillarin
- Fission yeast
- Pre-mRNA
- RNA-protein interaction
- uvi15
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
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