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    Genes Dev. 2000 Dec 1;14(23):2944-9.

    Cap methyltransferase selective binding and methylation of GpppG-RNA are stimulated by importin-alpha.

    Wen Y, Shatkin AJ.

    Center for Advanced Biotechnology and Medicine, University of Medicine and Dentistry of New Jersey, Piscataway, New Jersey 08854, USA.

    We screened a human cDNA library for proteins that bind mRNA cap methyltransferase (MT) and isolated nuclear transporter importin-alpha (Impalpha). This direct association was confirmed by glutathione S-transferase (GST) pulldown, coimmunoprecipitation, and nuclear colocalization. In gel shift assays, MT selectively bound RNA containing 5'-terminal GpppG, and binding was inhibited by GpppG and not by m(7)GpppC. Impalpha markedly enhanced MT binding to GpppG-RNA and stimulated MT activity. MT/RNA/Impalpha complexes were dissociated by importin-beta, which also blocked the stimulation of cap methylation by Impalpha. The presence of RanGTP but not RanGDP prevented these effects of importin-beta. These findings indicate that importins play a novel role in mRNA biogenesis at the level of cap methylation.

    PMID: 11114884 [PubMed - indexed for MEDLINE]

    PMCID: 317093

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