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  Mpp6 Incorporation in the Nuclear Exosome Contributes to RNA Channeling through the Mtr4 Helicase

Falk, S., Bonneau, F., Ebert, J., Kögel, A., & Conti, E. (2017). Mpp6 Incorporation in the Nuclear Exosome Contributes to RNA Channeling through the Mtr4 Helicase. Cell Reports, 20(10), 2279-2286. doi:10.1016/j.celrep.2017.08.033.

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 Creators:
Falk, Sebastian1, Author           
Bonneau, Fabien1, Author           
Ebert, Judith1, Author           
Kögel, Alexander1, Author           
Conti, Elena1, Author           
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1Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              

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Free keywords: RIBOSOMAL-RNA; PONTOCEREBELLAR HYPOPLASIA; SACCHAROMYCES-CEREVISIAE; CRYSTAL-STRUCTURE; COMPLEX; YEAST; DEGRADATION; REVEALS; MUTATIONS; RECONSTITUTIONCell Biology;
 Abstract: The RNA-degrading exosome mediates the processing and decay of many cellular transcripts. In the yeast nucleus, the ubiquitous 10-subunit exosome core complex (Exo-9-Rrp44) functions with four conserved cofactors (Rrp6, Rrp47, Mtr4, and Mpp6). Biochemical and structural studies to date have shed insights into the mechanisms of the exosome core and its nuclear cofactors, with the exception of Mpp6. We report the 3.2-angstrom resolution crystal structure of a S. cerevisiae Exo-9-Mpp6 complex, revealing how linear motifs in the Mpp6 middle domain bind Rrp40 via evolutionary conserved residues. In particular, Mpp6 binds near a tryptophan residue of Rrp40 that is mutated in human patients suffering from pontocerebellar hypoplasia. Using biochemical assays, we show that Mpp6 is required for the ability of Mtr4 to extend the trajectory of an RNA entering the exosome core, suggesting that it promotes the channeling of substrates from the nuclear helicase to the processive RNase.

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Language(s): eng - English
 Dates: 2017
 Publication Status: Published in print
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Title: Cell Reports
Source Genre: Journal
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Publ. Info: Maryland Heights, MO : Cell Press
Pages: - Volume / Issue: 20 (10) Sequence Number: - Start / End Page: 2279 - 2286 Identifier: Other: 2211-1247
CoNE: https://pure.mpg.de/cone/journals/resource/2211-1247