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The breast cancer tumor suppressor BRCA2-interacting protein, DSS1, and its homologs are critical for DNA recombination in eukaryotic cells. We found that Dss1p, along with Mlo3p and Uap56p, Schizosaccharomyces pombe homologs of two messenger RNA (mRNA) export factors of the NXF-NXT pathway, is required for mRNA export in S. pombe. Previously, we showed that the nuclear pore-associated Rae1p is an essential mRNA export factor in S. pombe. Here, we show that Dss1p and Uap56p function by linking mRNA adapter Mlo3p to Rae1p for targeting mRNA-protein complex (mRNP) to the proteins of the nuclear pore complex (NPC). Dss1p preferentially recruits to genes in vivo and interacts with -FG (phenylalanine glycine) nucleoporins in vivo and in vitro. Thus, Dss1p may function at multiple steps of mRNA export, from mRNP biogenesis to their targeting and translocation through the NPC.

Original publication




Journal article


Embo j

Publication Date





2512 - 2523


Adaptor Proteins, Signal Transducing, Biological Transport, DEAD-box RNA Helicases, DNA, Fungal, Exoribonucleases, Nuclear Matrix-Associated Proteins, Nuclear Proteins, Nucleocytoplasmic Transport Proteins, Protein Binding, Protein Interaction Mapping, Protein Structure, Tertiary, RNA Helicases, RNA, Messenger, RNA-Binding Proteins, Saccharomyces cerevisiae Proteins, Schizosaccharomyces, Schizosaccharomyces pombe Proteins, Structural Homology, Protein