LRPPRC-mediated folding of the mitochondrial transcriptome.
Identifieur interne : 000911 ( Main/Exploration ); précédent : 000910; suivant : 000912LRPPRC-mediated folding of the mitochondrial transcriptome.
Auteurs : Stefan J. Siira [Australie] ; Henrik Sp Hr [Allemagne] ; Anne-Marie J. Shearwood [Australie] ; Benedetta Ruzzenente [Allemagne] ; Nils-Göran Larsson [Allemagne] ; Oliver Rackham [Australie] ; Aleksandra Filipovska [Australie]Source :
- Nature communications [ 2041-1723 ] ; 2017.
Abstract
The expression of the compact mammalian mitochondrial genome requires transcription, RNA processing, translation and RNA decay, much like the more complex chromosomal systems, and here we use it as a model system to understand the fundamental aspects of gene expression. Here we combine RNase footprinting with PAR-CLIP at unprecedented depth to reveal the importance of RNA-protein interactions in dictating RNA folding within the mitochondrial transcriptome. We show that LRPPRC, in complex with its protein partner SLIRP, binds throughout the mitochondrial transcriptome, with a preference for mRNAs, and its loss affects the entire secondary structure and stability of the transcriptome. We demonstrate that the LRPPRC-SLIRP complex is a global RNA chaperone that stabilizes RNA structures to expose the required sites for translation, stabilization, and polyadenylation. Our findings reveal a general mechanism where extensive RNA-protein interactions ensure that RNA is accessible for its biological functions.
DOI: 10.1038/s41467-017-01221-z
PubMed: 29146908
Affiliations:
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Here we combine RNase footprinting with PAR-CLIP at unprecedented depth to reveal the importance of RNA-protein interactions in dictating RNA folding within the mitochondrial transcriptome. We show that LRPPRC, in complex with its protein partner SLIRP, binds throughout the mitochondrial transcriptome, with a preference for mRNAs, and its loss affects the entire secondary structure and stability of the transcriptome. We demonstrate that the LRPPRC-SLIRP complex is a global RNA chaperone that stabilizes RNA structures to expose the required sites for translation, stabilization, and polyadenylation. Our findings reveal a general mechanism where extensive RNA-protein interactions ensure that RNA is accessible for its biological functions.</div></front></TEI><affiliations><list><country><li>Allemagne</li><li>Australie</li></country><region><li>District de Cologne</li><li>Rhénanie-du-Nord-Westphalie</li></region><settlement><li>Cologne</li></settlement></list><tree><country name="Australie"><noRegion><name sortKey="Siira, Stefan J" sort="Siira, Stefan J" uniqKey="Siira S" first="Stefan J" last="Siira">Stefan J. Siira</name></noRegion><name sortKey="Filipovska, Aleksandra" sort="Filipovska, Aleksandra" uniqKey="Filipovska A" first="Aleksandra" last="Filipovska">Aleksandra Filipovska</name><name sortKey="Rackham, Oliver" sort="Rackham, Oliver" uniqKey="Rackham O" first="Oliver" last="Rackham">Oliver Rackham</name><name sortKey="Shearwood, Anne Marie J" sort="Shearwood, Anne Marie J" uniqKey="Shearwood A" first="Anne-Marie J" last="Shearwood">Anne-Marie J. 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