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Poly(A)-binding proteins play important roles in mRNA metabolism in eukaryotic cells. We examined the role of the Schizosaccharomyces pombe homologue of the Saccharomyces cerevisiae poly(A)-binding protein, Pab1p, in cellular growth and mRNA export. In contrast to PAB1, the sppabp gene is not essential for cellular viability. Like the human hPABP1 protein, spPABP is cytoplasmically localized and can shuttle between the nucleus and the cytoplasm. We found that a spPABP-GFP fusion protein expressed from a multicopy plasmid could suppress the growth and mRNA export defect of rae1-16 7 nup184-1 synthetic lethal mutations. However, about 20-25% of cells in the population exhibited a pronounced nuclear accumulation of poly(A)(+) RNA. The same cells also localized the spPABP-GFP fusion to the nucleus, suggesting that the shuttling ability of spPABP is related to its function in mRNA export. When a heterologous nuclear export activity from spMex67p was fused to spPABP-GFP fusion protein, it overcame the nuclear retention but did not increase nuclear mRNA export. We discuss the implications of these observations in relation to how spPABP could function in mRNA export. Published in 2002 by John Wiley & Sons, Ltd.

Original publication




Journal article



Publication Date





803 - 810


Biological Transport, Cell Nucleus, Cytoplasm, Gene Deletion, Poly(A)-Binding Proteins, RNA, Messenger, RNA-Binding Proteins, Receptors, Cytoplasmic and Nuclear, Schizosaccharomyces