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http://purl.uniprot.org/citations/10523645http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10523645http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10523645http://www.w3.org/2000/01/rdf-schema#comment"Decapping is a rate-limiting step in the decay of many yeast mRNAs; the activity of the decapping enzyme therefore plays a significant role in determining RNA stability. Using an in vitro decapping assay, we have identified a factor, Vps16p, that regulates the activity of the yeast decapping enzyme, Dcp1p. Mutations in the VPS16 gene result in a reduction of decapping activity in vitro and in the stabilization of both wild-type and nonsense-codon-containing mRNAs in vivo. The mrt1-3 allele, previously shown to affect the turnover of wild-type mRNAs, results in a similar in vitro phenotype. Extracts from both vps16 and mrt1 mutant strains inhibit the activity of purified Flag-Dcp1p. We have identified a 70-kDa protein which copurifies with Flag-Dcp1p as the abundant Hsp70 family member Ssa1p/2p. Intriguingly, the interaction with Ssa1p/2p is enhanced in strains with mutations in vps16 or mrt1. We propose that Hsp70s may be involved in the regulation of mRNA decapping."xsd:string
http://purl.uniprot.org/citations/10523645http://purl.org/dc/terms/identifier"doi:10.1128/mcb.19.11.7568"xsd:string
http://purl.uniprot.org/citations/10523645http://purl.org/dc/terms/identifier"doi:10.1128/mcb.19.11.7568"xsd:string
http://purl.uniprot.org/citations/10523645http://purl.uniprot.org/core/author"Zhang S."xsd:string
http://purl.uniprot.org/citations/10523645http://purl.uniprot.org/core/author"Zhang S."xsd:string
http://purl.uniprot.org/citations/10523645http://purl.uniprot.org/core/author"Williams C.J."xsd:string
http://purl.uniprot.org/citations/10523645http://purl.uniprot.org/core/author"Williams C.J."xsd:string
http://purl.uniprot.org/citations/10523645http://purl.uniprot.org/core/author"Peltz S.W."xsd:string
http://purl.uniprot.org/citations/10523645http://purl.uniprot.org/core/author"Peltz S.W."xsd:string
http://purl.uniprot.org/citations/10523645http://purl.uniprot.org/core/author"Hagan K."xsd:string
http://purl.uniprot.org/citations/10523645http://purl.uniprot.org/core/author"Hagan K."xsd:string
http://purl.uniprot.org/citations/10523645http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10523645http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10523645http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/10523645http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/10523645http://purl.uniprot.org/core/pages"7568-7576"xsd:string
http://purl.uniprot.org/citations/10523645http://purl.uniprot.org/core/pages"7568-7576"xsd:string
http://purl.uniprot.org/citations/10523645http://purl.uniprot.org/core/title"Mutations in VPS16 and MRT1 stabilize mRNAs by activating an inhibitor of the decapping enzyme."xsd:string
http://purl.uniprot.org/citations/10523645http://purl.uniprot.org/core/title"Mutations in VPS16 and MRT1 stabilize mRNAs by activating an inhibitor of the decapping enzyme."xsd:string
http://purl.uniprot.org/citations/10523645http://purl.uniprot.org/core/volume"19"xsd:string
http://purl.uniprot.org/citations/10523645http://purl.uniprot.org/core/volume"19"xsd:string
http://purl.uniprot.org/citations/10523645http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10523645
http://purl.uniprot.org/citations/10523645http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10523645