A mammalian protein of 220 kDa binds pre-mRNAs in the spliceosome: a potential homologue of the yeast PRP8 protein.
AUTOR(ES)
Garcia-Blanco, M A
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=53838Documentos Relacionados
- The yeast PRP8 protein interacts directly with pre-mRNA.
- Stabilization and ribosome association of unspliced pre-mRNAs in a yeast upf1- mutant.
- Recognition of polyadenylation sites in yeast pre-mRNAs by cleavage and polyadenylation factor
- The mammalian analogue of the yeast PRP8 splicing protein is present in the U4/5/6 small nuclear ribonucleoprotein particle and the spliceosome.
- In vitro splicing pathways of pre-mRNAs containing multiple intervening sequences?