Abstract
A mammalian protein of approximately 220 kDa (p220) was UV-crosslinked to precursor mRNAs (pre-mRNAs) under splicing conditions. The kinetics and biochemical requirements of the UV-crosslinking of p220 corresponded to the kinetics and biochemical requirements of spliceosome formation. On Western blots, antibodies against the yeast splicing factor PRP8 recognized a doublet of proteins, the faster migrating of which comigrated with p220. Furthermore, UV-crosslinked p220 was immunoprecipitated with anti-PRP8 antisera. These results suggest structural conservation of the splicing factor PRP8 from yeast to mammals and show that this protein is in close proximity to the pre-mRNA in the spliceosome.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 3082-3086 |
| Number of pages | 5 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Volume | 87 |
| Issue number | 8 |
| DOIs | |
| State | Published - Apr 1990 |
| Externally published | Yes |
Keywords
- Pre-mRNA splicing
- UV-crosslinking
ASJC Scopus subject areas
- General
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