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  Crystal structure of an RNA-bound 11-subunit eukaryotic exosome complex

Makino, D. L., Baumgärtner, M., & Conti, E. (2013). Crystal structure of an RNA-bound 11-subunit eukaryotic exosome complex. NATURE, 495(7439), 70-75. doi:10.1038/nature11870.

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 Creators:
Makino, Debora L.1, Author           
Baumgärtner, Marc1, Author           
Conti, Elena1, Author           
Affiliations:
1Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              

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Free keywords: HUMAN PM-SCL; YEAST EXOSOME; ARCHAEAL EXOSOME; CORE EXOSOME; DEGRADATION; SUBUNIT; EXORIBONUCLEASE; RECONSTITUTION; PURIFICATION; RECRUITMENT
 Abstract: The exosome is the major 3'-5' RNA-degradation complex in eukaryotes. The ubiquitous core of the yeast exosome (Exo-10) is formed by nine catalytically inert subunits (Exo-9) and a single active RNase, Rrp44. In the nucleus, the Exo-10 core recruits another nuclease, Rrp6. Here we crystallized an approximately 440-kilodalton complex of Saccharomyces cerevisiae Exo-10 bound to a carboxy-terminal region of Rrp6 and to an RNA duplex with a 3'-overhang of 31 ribonucleotides. The 2.8 angstrom resolution structure shows how RNA is funnelled into the Exo-9 channel in a single-stranded conformation by an unwinding pore. Rrp44 adopts a closed conformation and captures the RNA 3'-end that exits from the side of Exo-9. Exo-9 subunits bind RNA with-sequence-unspecific interactions reminiscent of archaeal exosomes. The substrate binding and channelling mechanisms of 3'-5' RNA degradation complexes are conserved in all kingdoms of life.

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Language(s): eng - English
 Dates: 2013-03-07
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000316039800041
DOI: 10.1038/nature11870
 Degree: -

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Title: NATURE
Source Genre: Journal
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Publ. Info: MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND : NATURE PUBLISHING GROUP
Pages: - Volume / Issue: 495 (7439) Sequence Number: - Start / End Page: 70 - 75 Identifier: ISSN: 0028-0836