Abstract
Dss1p is an evolutionarily conserved small protein that interacts with BRCA2, a tumor suppressor protein, in humans. The Schizosaccharomyces pombe strain lacking the dss1 + gene (Δ dss1) shows a temperature-sensitive growth defect and accumulation of bulk poly(A) + RNA in the nucleus at a nonpermissive temperature. In situ hybridization using probes for several specific mRNAs, however, revealed that the analyzed mRNAs were exported normally to the cytoplasm in Δ dss1, suggesting that Dss1p is required for export of some subsets of mRNAs. We identified the pad1 + gene, which encodes a component of the 26S proteasome, as a suppressor for the ts − phenotype of Δ dss1. Unexpectedly, overexpression of Pad1p could suppress neither the defect in nuclear mRNA export nor a defect in proteasome function. In addition, loss of proteasome functions does not cause defective nuclear mRNA export. Dss1p seems to be a multifunctional protein involved in nuclear export of specific sets of mRNAs and the ubiquitin-proteasome pathway in fission yeast.
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