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dc.contributor.authorMitchell, Philip
dc.contributor.authorTollervey, David
dc.coverage.spatial4en
dc.date.accessioned2005-03-17T15:22:06Z
dc.date.available2005-03-17T15:22:06Z
dc.date.issued2000-10
dc.identifier.citationMitchell P, Tollervey D, NATURE STRUCTURAL BIOLOGY, 7 (10): 843-846 OCT 2000en
dc.identifier.urihttp://structbio.nature.com
dc.identifier.urihttp://hdl.handle.net/1842/734
dc.description.abstractThe exosome complex of 3′→5′ exoribonucleases functions in both the precise processing of 3′ extended precursor molecules to mature stable RNAs and the complete degradation of other RNAs. Both processing and degradative activities of the exosome depend on additional cofactors, notably the putative RNA helicases Mtr4p and Ski2p. It is not known how these factors regulate exosome function or how the exosome distinguishes RNAs destined for processing events from substrates that are to be completely degraded. Here we review the available data concerning the modes of action of the exosome and relate these to possible structural arrangements for the complex. As no detailed structural data are yet available for the exosome complex, or any of its constituent enzymes, this discussion will rely heavily on rather speculative models.en
dc.format.extent255178 bytes
dc.format.mimetypeapplication/pdf
dc.language.isoen
dc.publisherNature Publishing Groupen
dc.subjectstructuralen
dc.subjectorganisationen
dc.subjectexosomeen
dc.subjectcomplexen
dc.subjectRNAen
dc.subjectdegradationen
dc.titleMusing on the structural organization of the exosome complexen
dc.typeArticleen


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