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  The pentatricopeptide repeat protein Rmd9 recognizes the dodecameric element in the 3′-UTRs of yeast mitochondrial mRNAs

Hillen, H. S., Markov, D. A., Wojtas, I. D., Hofmann, K. B., Lidschreiber, M., Cowan, A. T., et al. (2021). The pentatricopeptide repeat protein Rmd9 recognizes the dodecameric element in the 3′-UTRs of yeast mitochondrial mRNAs. Proceedings of the National Academy of Sciences of the USA, 118(15): e2009329118. doi:10.1073/pnas.2009329118.

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 Creators:
Hillen, H. S.1, Author              
Markov, D. A., Author
Wojtas, I. D., Author
Hofmann, K. B.2, Author              
Lidschreiber, M.2, Author              
Cowan, A. T., Author
Jones, J. L., Author
Temiakov, D. , Author
Cramer, P.2, Author              
Anikin, M., Author
Affiliations:
1Research Group Structure and Function of Molecular Machines, MPI for Biophysical Chemistry, Max Planck Society, ou_3265856              
2Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1863498              

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Free keywords: itochondria; gene expression; PPR proteins; protein-RNA complex; PAR-CLIP
 Abstract: Stabilization of messenger RNA is an important step in posttranscriptional gene regulation. In the nucleus and cytoplasm of eukaryotic cells it is generally achieved by 5′ capping and 3′ polyadenylation, whereas additional mechanisms exist in bacteria and organelles. The mitochondrial mRNAs in the yeast Saccharomyces cerevisiae comprise a dodecamer sequence element that confers RNA stability and 3′-end processing via an unknown mechanism. Here, we isolated the protein that binds the dodecamer and identified it as Rmd9, a factor that is known to stabilize yeast mitochondrial RNA. We show that Rmd9 associates with mRNA around dodecamer elements in vivo and that recombinant Rmd9 specifically binds the element in vitro. The crystal structure of Rmd9 bound to its dodecamer target reveals that Rmd9 belongs to the family of pentatricopeptide (PPR) proteins and uses a previously unobserved mode of specific RNA recognition. Rmd9 protects RNA from degradation by the mitochondrial 3′-exoribonuclease complex mtEXO in vitro, indicating that recognition and binding of the dodecamer element by Rmd9 confers stability to yeast mitochondrial mRNAs.

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Language(s): deu - German
 Dates: 2021-04-052021-04-13
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: DOI: 10.1073/pnas.2009329118
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Title: Proceedings of the National Academy of Sciences of the USA
Source Genre: Journal
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Pages: 8 Volume / Issue: 118 (15) Sequence Number: e2009329118 Start / End Page: - Identifier: -