dc.contributor.author | Mitchell, Philip | |
dc.contributor.author | Tollervey, David | |
dc.coverage.spatial | 4 | en |
dc.date.accessioned | 2005-03-17T15:22:06Z | |
dc.date.available | 2005-03-17T15:22:06Z | |
dc.date.issued | 2000-10 | |
dc.identifier.citation | Mitchell P, Tollervey D, NATURE STRUCTURAL BIOLOGY, 7 (10): 843-846 OCT 2000 | en |
dc.identifier.uri | http://structbio.nature.com | |
dc.identifier.uri | http://hdl.handle.net/1842/734 | |
dc.description.abstract | The 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.extent | 255178 bytes | |
dc.format.mimetype | application/pdf | |
dc.language.iso | en | |
dc.publisher | Nature Publishing Group | en |
dc.subject | structural | en |
dc.subject | organisation | en |
dc.subject | exosome | en |
dc.subject | complex | en |
dc.subject | RNA | en |
dc.subject | degradation | en |
dc.title | Musing on the structural organization of the exosome complex | en |
dc.type | Article | en |