| Literature DB >> 12101094 |
Patrick Aloy1, Francesca D Ciccarelli, Christina Leutwein, Anne-Claude Gavin, Giulio Superti-Furga, Peer Bork, Bettina Bottcher, Robert B Russell.
Abstract
We present a model of the yeast exosome based on the bacterial degradosome component polynucleotide phosphorylase (PNPase). Electron microscopy shows the exosome to resemble PNPase but with key differences likely related to the position of RNA binding domains, and to the location of domains unique to the exosome. We use various techniques to reduce the many possible models of exosome subunits based on PNPase to just one. The model suggests numerous experiments to probe exosome function, particularly with respect to subunits making direct atomic contacts and conserved, possibly functional residues within the predicted central pore of the complex.Entities:
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Year: 2002 PMID: 12101094 PMCID: PMC1084189 DOI: 10.1093/embo-reports/kvf135
Source DB: PubMed Journal: EMBO Rep ISSN: 1469-221X Impact factor: 8.807