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A cap-binding protein complex mediating U snRNA export

Nature volume 376, pages 709–712 (1995)Cite this article

Abstract

CAP structures are added cotranscriptionally to all RNA polymer-ase II transcripts1,2. They affect several processes including RNA stability3–5, pre-messenger RNA splicing6–11, RNA export from the nucleus12–14 and translation initiation15–17. The effect of the cap on translation is mediated by the initiation factor eIF-4F (refs 15–19), whereas the effect on pre-mRNA splicing involves a nuclear complex (CBC) composed of two cap binding proteins, CBP80 and CBP2011. A role for CBC in the nuclear export of capped RNAs has also been proposed11,13. We report here the characterization of human and Xenopus CBP20s. Antibodies against recombinant CBP20 prevent interaction of CBC with capped RNAs in vitro. Following microinjection into Xenopus oocytes, the antibodies inhibit both pre-mRNA splicing and export of U small nuclear RNAs to the cytoplasm. These results demonstrate that CBC mediates the effect of the cap structure in U snRNA export, and provide direct evidence for the involvement of a cellular RNA-binding factor in the transport of RNA to the cytoplasm.

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Author notes

  1. Artur Jarmolowski

    Present address: Institute of Molecular Biology and Biotechnology, Department of Biopolymer Biochemistry, Miedzychodzka 5, 60371, Poznan, Poland

Authors and Affiliations

  1. European Molecular Biology Laboratory (EMBL), Meyerhofstrasse 1, 69117, Heidelberg, Germany

    Elisa Izaurralde, Joe Lewis, Chiara Gamberi, Artur Jarmolowski, Caroline McGuigan & Iain W. Mattaj

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  1. Elisa Izaurralde
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  5. Caroline McGuigan
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  6. Iain W. Mattaj
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Izaurralde, E., Lewis, J., Gamberi, C. et al. A cap-binding protein complex mediating U snRNA export. Nature 376, 709–712 (1995). https://doi.org/10.1038/376709a0

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