A cap-binding protein complex mediating U snRNA export
Identifieur interne : 003371 ( Main/Exploration ); précédent : 003370; suivant : 003372A cap-binding protein complex mediating U snRNA export
Auteurs : Elisa Izaurralde [Pologne] ; Joe Lewis [Pologne] ; Chiara Gamberi [Pologne] ; Artur Jarmolowski ; Caroline Mcguigan [Pologne] ; Iain W. MattajSource :
- Nature [ 0028-0836 ] ; 1995-08-24.
Abstract
CAP structures are added cotranscriptionally to all RNA polymer-ase II transcripts1,2. They affect several processes including RNA stability35, pre-messenger RNA splicing611, RNA export from the nucleus1214 and translation initiation1517. The effect of the cap on translation is mediated by the initiation factor eIF-4F (refs 1519), 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.
Url:
DOI: 10.1038/376709a0
Affiliations:
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Mattaj</name></author></analytic><monogr></monogr><series><title level="j" type="main">Nature</title><imprint><publisher>Nature Publishing Group</publisher><date when="1995-08-24">1995-08-24</date><biblScope unit="vol">376</biblScope><biblScope unit="issue">6542</biblScope><biblScope unit="page" from="709">709</biblScope><biblScope unit="page" to="712">712</biblScope><date type="Copyright" when="2002">2002</date></imprint><idno type="ISSN">0028-0836</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0028-0836</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract">CAP structures are added cotranscriptionally to all RNA polymer-ase II transcripts1,2. They affect several processes including RNA stability35, pre-messenger RNA splicing611, RNA export from the nucleus1214 and translation initiation1517. The effect of the cap on translation is mediated by the initiation factor eIF-4F (refs 1519), 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. 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