SGD Paper 
Thakurta AG, et al. (2007) The Nuclear Export Signal of Splicing Factor Uap56p Interacts with Nuclear Pore-associated Protein Rae1p for mRNA Export in Schizosaccharomyces pombe. J Biol Chem 282(24):17507-16
Abstract: Mammalian UAP56 or its homolog Sub2p in Saccharomyces cerevisiae (S. cerevisiae) are members of the ATP-dependant RNA helicase family and are required for splicing and nuclear export of messenger RNA (mRNA). Previously we showed that in Schizosaccharomyces pombe (S. pombe) Uap56p is critical for mRNA export. It links the mRNA adapter Mlo3p, a homolog of Yra1p in S. cerevisiae or Aly in mammals, to nuclear pore associated mRNA export factor Rae1p. In this report we show that, in contrast to S. cerevisiae, Uap56p in S. pombe, is not required for pre- mRNA splicing. The putative RNA helicase function of Uap56p is not required for mRNA export. However, the RNA-binding motif of Uap56p is critical for nuclear export of mRNA. Within Uap56p we identified nuclear import and export signals that may allow it to shuttle between the nucleus and the cytoplasm. We found that Uap56p interacts with Rae1p directly via its nuclear export signal and this interaction is critical for Uap56p's nuclear export activity as well as for exporting mRNA. RNA binding and the ability to shuttle between the nucleus and cytoplasm are important features of mRNA export carriers such as HIV-Rev. Our results suggest that Uap56p could function similarly as an export carrier of mRNA in S. pombe.
| Status: Published | Type: Journal Article | PubMed ID: 17449473 |
Topics addressed in this paper
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