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.
|Number of pages||7|
|Journal||Biochemical and Biophysical Research Communications|
|Publication status||Published - 2002|
Bibliographical noteFunding Information:
We thank Drs. Marvin Wickens and M. Yamamoto for providing yeast strains and plasmids used in three-hybrid assay and S. pombe cell strain, respectively. We also thank Dr. O. Hwang for critical reading of the manuscript. This work was supported in part by a grant for the leading scientists from the Korea Science and Engineering Foundation (2001) to S.D. Park., M.K., and S.D.P. are supported by a BK21 Research Fellowship from the Korea Ministry of Education.
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology