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

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Schlagwörter: HUMAN PM-SCL; YEAST EXOSOME; ARCHAEAL EXOSOME; CORE EXOSOME; DEGRADATION; SUBUNIT; EXORIBONUCLEASE; RECONSTITUTION; PURIFICATION; RECRUITMENT
 Zusammenfassung: 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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Sprache(n): eng - English
 Datum: 2013-03-07
 Publikationsstatus: Erschienen
 Seiten: 6
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: ISI: 000316039800041
DOI: 10.1038/nature11870
 Art des Abschluß: -

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Titel: NATURE
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND : NATURE PUBLISHING GROUP
Seiten: - Band / Heft: 495 (7439) Artikelnummer: - Start- / Endseite: 70 - 75 Identifikator: ISSN: 0028-0836