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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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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-FADD-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-FADE-3
Genre: Journal Article

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 Creators:
Gebhardt, Anna1, Author              
Habjan, Matthias1, Author              
Benda, Christian2, Author              
Meiler, Arno1, Author              
Haas, Darya A.1, Author              
Hein, Marco Y.3, Author              
Mann, Angelika1, Author              
Mann, Matthias3, Author              
Habermann, Bianca4, Author              
Pichlmair, Andreas1, Author              
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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Free keywords: POLY(A)-SPECIFIC RIBONUCLEASE; BAC TRANSGENEOMICS; CRYSTAL-STRUCTURE; MAMMALIAN-CELLS; GENE-EXPRESSION; NUCLEAR EXPORT; CANCER-CELLS; RRM DOMAIN; PROTEIN; RECOGNITION
 Abstract: 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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Language(s): eng - English
 Dates: 2015
 Publication Status: Published online
 Pages: 13
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: ISI: 000363017100020
DOI: 10.1038/ncomms9192
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Title: NATURE COMMUNICATIONS
Source Genre: Journal
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Publ. Info: MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND : NATURE PUBLISHING GROUP
Pages: - Volume / Issue: 6 Sequence Number: 8192 Start / End Page: - Identifier: ISSN: 2041-1723