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Genes to Cells (2007) 12, 35-47. doi:10.1111/j.1365-2443.2006.01032.x
© 2007 Blackwell Publishing or its licensors

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Participation of XPB/Ptr8p, a component of TFIIH, in nucleocytoplasmic transport of mRNA in fission yeast

Fumitaka Mizuki1, Takeshi Namiki2, Hiroshi Sato1, Hiromi Furukawa2, Tadao Matsusaka1, Yasumi Ohshima2,a, Ryoko Ishibashi1, Tomoko Andoh1 and Tokio Tani1,*

1 Department of Biological Sciences, Graduate School of Science and Technology, Kumamoto University, Kumamoto 860-8555, Japan
2 Department of Biology, Faculty of Science, Kyushu University, Fukuoka 812-8581, Japan

To identify novel factors involved in nuclear mRNA export in Schizosaccharomyces pombe, we isolated and characterized the ptr8+ gene, mutation of which causes nuclear accumulation of poly (A)+ RNA. The ptr8+ gene encodes an S. pombe homologue of human XPB, a component of TFIIH involved in nucleotide excision repair (NER) and transcription. A temperature-sensitive mutant of ptr8+ (ptr8-1) was highly sensitive to UV irradiation, as are human XPB cells. Northern blot analysis demonstrated that the amount of total poly (A)+ mRNAs does not decrease significantly at the nonpermissive temperature in ptr8-1 cells, whereas a pulse-labeling assay using 35S-methionine showed that protein synthesis decreases rapidly after incubation of cells at the nonpermissive temperature, suggesting that ptr8-1 cells have a defect in nuclear mRNA export. In Saccharomyces cerevisiae, a mutation in the SSL2 gene encoding a homologue of Ptr8p also causes a block of mRNA export at the nonpermissive temperature. In addition, expression of human XPB in ptr8-1 cells rescued the ts phenotype and the mRNA export defects, suggesting that human XPB may also play a role in mRNA export. Furthermore, we revealed a functional interaction between Ptr8p and Tho2p, a component of the TREX complex involved in mRNA export. These results suggest that XPB/Ptr8p plays roles not only in NER and transcription, but also plays a conserved role in mRNA export.


Communicated by: Masayuki Yamamoto

aPresent address: Department of Applied Life Science, Faculty of Biotechnology and Life Science, Sojo University, Kumamoto 860-0082, Japan

* Correspondence: E-mail: ttani{at}sci.kumamoto-u.ac.jp







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