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  mRNA export through an additional cap-binding complex consisting of NCBP1 and NCBP3

Gebhardt, A., Habjan, M., Benda, C., Meiler, A., Haas, D. A., Hein, M. Y., et al. (2015). mRNA export through an additional cap-binding complex consisting of NCBP1 and NCBP3. NATURE COMMUNICATIONS, 6: 8192. doi:10.1038/ncomms9192.

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Gebhardt, Anna1, Autor           
Habjan, Matthias1, Autor           
Benda, Christian2, Autor           
Meiler, Arno1, Autor           
Haas, Darya A.1, Autor           
Hein, Marco Y.3, Autor           
Mann, Angelika1, Autor           
Mann, Matthias3, Autor           
Habermann, Bianca4, Autor           
Pichlmair, Andreas1, Autor           
Affiliations:
1Pichlmair, Andreas / Innate Immunity, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565166              
2Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              
3Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              
4Habermann, Bianca / Computational Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1832284              

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Schlagwörter: POLY(A)-SPECIFIC RIBONUCLEASE; BAC TRANSGENEOMICS; CRYSTAL-STRUCTURE; MAMMALIAN-CELLS; GENE-EXPRESSION; NUCLEAR EXPORT; CANCER-CELLS; RRM DOMAIN; PROTEIN; RECOGNITION
 Zusammenfassung: The flow of genetic information from DNA to protein requires polymerase-II-transcribed RNA characterized by the presence of a 5'-cap. The cap-binding complex (CBC), consisting of the nuclear cap-binding protein (NCBP) 2 and its adaptor NCBP1, is believed to bind all capped RNA and to be necessary for its processing and intracellular localization. Here we show that NCBP1, but not NCBP2, is required for cell viability and poly(A) RNA export. We identify C17orf85 (here named NCBP3) as a cap-binding protein that together with NCBP1 forms an alternative CBC in higher eukaryotes. NCBP3 binds mRNA, associates with components of the mRNA processing machinery and contributes to poly(A) RNA export. Loss of NCBP3 can be compensated by NCBP2 under steady-state conditions. However, NCBP3 becomes pivotal under stress conditions, such as virus infection. We propose the existence of an alternative CBC involving NCBP1 and NCBP3 that plays a key role in mRNA biogenesis.

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Sprache(n): eng - English
 Datum: 2015
 Publikationsstatus: Online veröffentlicht
 Seiten: 13
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: ISI: 000363017100020
DOI: 10.1038/ncomms9192
 Art des Abschluß: -

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Titel: NATURE COMMUNICATIONS
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND : NATURE PUBLISHING GROUP
Seiten: - Band / Heft: 6 Artikelnummer: 8192 Start- / Endseite: - Identifikator: ISSN: 2041-1723