RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/24569876http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24569876http://www.w3.org/2000/01/rdf-schema#comment"Numerous mRNAs are degraded in processing bodies (P bodies) in Saccharomyces cerevisiae. In logarithmically growing cells, only 0-1 P bodies per cell are detectable. However, the number and appearance of P bodies change once the cell encounters stress. Here, we show that the polysome-associated mRNA-binding protein Scp160 interacts with P body components, such as the decapping protein Dcp2 and the scaffold protein Pat1, presumably, on polysomes. Loss of either Scp160 or its interaction partner Bfr1 caused the formation of Dcp2-positive structures. These Dcp2-positive foci contained mRNA, because their formation was inhibited by the presence of cycloheximide. In addition, Scp160 was required for proper P body formation because only a subset of bona fide P body components could assemble into the Dcp2-positive foci in Δscp160 cells. In either Δbfr1 or Δscp160 cells, P body formation was uncoupled from translational attenuation as the polysome profile remained unchanged. Collectively, our data suggest that Bfr1 and Scp160 prevent P body formation under normal growth conditions."xsd:string
http://purl.uniprot.org/citations/24569876http://purl.org/dc/terms/identifier"doi:10.1242/jcs.142083"xsd:string
http://purl.uniprot.org/citations/24569876http://purl.uniprot.org/core/author"Spang A."xsd:string
http://purl.uniprot.org/citations/24569876http://purl.uniprot.org/core/author"Wang C."xsd:string
http://purl.uniprot.org/citations/24569876http://purl.uniprot.org/core/author"Estrada A.F."xsd:string
http://purl.uniprot.org/citations/24569876http://purl.uniprot.org/core/author"Prescianotto-Baschong C."xsd:string
http://purl.uniprot.org/citations/24569876http://purl.uniprot.org/core/author"Weidner J."xsd:string
http://purl.uniprot.org/citations/24569876http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24569876http://purl.uniprot.org/core/name"J Cell Sci"xsd:string
http://purl.uniprot.org/citations/24569876http://purl.uniprot.org/core/pages"1992-2004"xsd:string
http://purl.uniprot.org/citations/24569876http://purl.uniprot.org/core/title"The polysome-associated proteins Scp160 and Bfr1 prevent P body formation under normal growth conditions."xsd:string
http://purl.uniprot.org/citations/24569876http://purl.uniprot.org/core/volume"127"xsd:string
http://purl.uniprot.org/citations/24569876http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24569876
http://purl.uniprot.org/citations/24569876http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/24569876
http://purl.uniprot.org/uniprot/#_P06105-mappedCitation-24569876http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24569876
http://purl.uniprot.org/uniprot/#_P38934-mappedCitation-24569876http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24569876
http://purl.uniprot.org/uniprot/P06105http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/24569876
http://purl.uniprot.org/uniprot/P38934http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/24569876