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  The exosome-binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase.

Schuch, B., Feigenbutz, M., Makino, D. L., Falk, S., Basquin, C., Mitchell, P., et al. (2014). The exosome-binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase. The EMBO journal, 33(23), 2829-2846. doi:10.15252/embj.201488757.

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 Creators:
Schuch, Benjamin1, Author              
Feigenbutz, Monika2, Author
Makino, Debora L.1, Author              
Falk, Sebastian1, Author              
Basquin, Claire1, Author              
Mitchell, Phil2, Author
Conti, Elena1, Author              
Affiliations:
1Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              
2external, ou_persistent22              

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Free keywords: RNA degradation; X‐ray crystallography; nuclear exosome; yeast genetics
 Abstract: The exosome is a conserved multi-subunit ribonuclease complex that functions in 3' end processing, turnover and surveillance of nuclear and cytoplasmic RNAs. In the yeast nucleus, the 10-subunit core complex of the exosome (Exo-10) physically and functionally interacts with the Rrp6 exoribonuclease and its associated cofactor Rrp47, the helicase Mtr4 and Mpp6. Here, we show that binding of Mtr4 to Exo-10 in vitro is dependent upon both Rrp6 and Rrp47, whereas Mpp6 binds directly and independently of other cofactors. Crystallographic analyses reveal that the N-terminal domains of Rrp6 and Rrp47 form a highly intertwined structural unit. Rrp6 and Rrp47 synergize to create a composite and conserved surface groove that binds the N-terminus of Mtr4. Mutation of conserved residues within Rrp6 and Mtr4 at the structural interface disrupts their interaction and inhibits growth of strains expressing a C-terminal GFP fusion of Mtr4. These studies provide detailed structural insight into the interaction between the Rrp6-Rrp47 complex and Mtr4, revealing an important link between Mtr4 and the core exosome. 2014 The Authors.

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Language(s): eng - English
 Dates: 2014
 Publication Status: Published in print
 Pages: 18
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 25319414
DOI: 10.15252/embj.201488757
 Degree: -

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Title: The EMBO journal
Source Genre: Journal
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Pages: - Volume / Issue: 33 (23) Sequence Number: - Start / End Page: 2829 - 2846 Identifier: ISSN: 1460-2075