The mammalian analogue of the yeast PRP8 splicing protein is present in the U4/5/6 small nuclear ribonucleoprotein particle and the spliceosome.
Copyright policy )The mammalian analogue of the yeast PRP8 splicing protein is present in the U4/5/6 small nuclear ribonucleoprotein particle and the spliceosome.
HeLa cell nuclear extracts contain a protein reactive with antibodies against PRP8, a polypeptide essential for pre-mRNA splicing in yeast and a specific component of the yeast U5 small nuclear ribonucleoprotein (snRNP) [Lossky, M., Anderson, G. J., Jackson, S. P. & Beggs, J. (1987) Cell 51, 1019-1026]. The mammalian protein appears as a doublet at approximately 200 kDa, smaller than the 260-kDa yeast protein, and possesses an Sm epitope as determined by immunoblotting. Its association with a snRNP of the Sm class other than U1 or U2 is indicated by its immunoprecipitation by anti-Sm and anti-trimethylguanosine antibodies but not by anti-(U1) or anti-(U2) RNP sera. Gradient fractionation of splicing extracts demonstrates that the 200-kDa protein is a component of the U4/5/6 snRNP complex and of U5 snRNPs. It is also present in affinity-purified spliceosomes.
- Yale University United States
- Howard Hughes Medical Institute United States
Cell Nucleus, RNA Splicing, Ribonuclease H, Antibodies, Monoclonal, Saccharomyces cerevisiae, Ribonucleoproteins, Small Nuclear, Fungal Proteins, Molecular Weight, Epitopes, Ribonucleoproteins, Endoribonucleases, Centrifugation, Density Gradient, Humans, HeLa Cells
Cell Nucleus, RNA Splicing, Ribonuclease H, Antibodies, Monoclonal, Saccharomyces cerevisiae, Ribonucleoproteins, Small Nuclear, Fungal Proteins, Molecular Weight, Epitopes, Ribonucleoproteins, Endoribonucleases, Centrifugation, Density Gradient, Humans, HeLa Cells
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