Abstract
Parallel Investigations of yeast and metazoan pre-mRNA splicing have documented enormous complexity in the nucleic acid and protein components of the cellular splicing apparatus, the spliceosome. The degree to which yeast and metazoan spliceosomal proteins differ in composition and structure is currently unknown. In this report we demonstrate that the human small nuclear ribonucleoproteln (snRNP) polypeptide D1 complements the cell lethality, splicing deficiency, and snRNA instability phenotypes associated with a yeast smd1 null allele. Mutational analysis of yeast SMD1, guided by a comparison of the predicted yeast and human proteins, reveals that a large, nonconserved portion of Smd1p is dispensable for biological activity. These observations firmly establish D1 as an essential component of the cellular splicing apparatus and suggest that yeast and metazoa are remarkably similar in the polypeptides guiding early snRNP assembly.
Original language | English |
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Pages (from-to) | 3501-3505 |
Number of pages | 5 |
Journal | Nucleic Acids Research |
Volume | 21 |
Issue number | 15 |
DOIs | |
State | Published - Jul 25 1993 |
Bibliographical note
Funding Information:We thank H.Wu and S.Zu for excellent technical assistance. This work was supported by National Institutes of Health award GM42476 to BCR.
ASJC Scopus subject areas
- Genetics