pubmed-article:17522196 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17522196 | lifeskim:mentions | umls-concept:C0035736 | lld:lifeskim |
pubmed-article:17522196 | lifeskim:mentions | umls-concept:C1081254 | lld:lifeskim |
pubmed-article:17522196 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
pubmed-article:17522196 | lifeskim:mentions | umls-concept:C0035681 | lld:lifeskim |
pubmed-article:17522196 | lifeskim:mentions | umls-concept:C0243041 | lld:lifeskim |
pubmed-article:17522196 | lifeskim:mentions | umls-concept:C0243044 | lld:lifeskim |
pubmed-article:17522196 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
pubmed-article:17522196 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
pubmed-article:17522196 | lifeskim:mentions | umls-concept:C0013138 | lld:lifeskim |
pubmed-article:17522196 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
pubmed-article:17522196 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
pubmed-article:17522196 | pubmed:issue | 16 | lld:pubmed |
pubmed-article:17522196 | pubmed:dateCreated | 2007-7-26 | lld:pubmed |
pubmed-article:17522196 | pubmed:abstractText | The molecular chaperone heat shock protein 90 (Hsp90) is involved in multiple cellular processes including protein maturation, complex assembly and disassembly, and intracellular transport. We have recently shown that a disruption of Hsp90 activity in cultured Drosophila melanogaster cells suppresses Flock House virus (FHV) replication and the accumulation of protein A, the FHV RNA-dependent RNA polymerase. In the present study, we investigated whether the defect in FHV RNA polymerase accumulation induced by Hsp90 suppression was secondary to an effect on protein A synthesis, degradation, or intracellular membrane association. Treatment with the Hsp90-specific inhibitor geldanamycin selectively reduced FHV RNA polymerase synthesis by 80% in Drosophila S2 cells stably transfected with an inducible protein A expression plasmid. The suppressive effect of geldanamycin on protein A synthesis was not attenuated by proteasome inhibition, nor was it sensitive to changes in either the mRNA untranslated regions or protein A intracellular membrane localization. Furthermore, geldanamycin did not promote premature protein A degradation, nor did it alter the extremely rapid kinetics of protein A membrane association. These results identify a novel role for Hsp90 in facilitating viral RNA polymerase synthesis in Drosophila cells and suggest that FHV subverts normal cellular pathways to assemble functional replication complexes. | lld:pubmed |
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pubmed-article:17522196 | pubmed:language | eng | lld:pubmed |
pubmed-article:17522196 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17522196 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17522196 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:17522196 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17522196 | pubmed:month | Aug | lld:pubmed |
pubmed-article:17522196 | pubmed:issn | 0022-538X | lld:pubmed |
pubmed-article:17522196 | pubmed:author | pubmed-author:MillerDavid... | lld:pubmed |
pubmed-article:17522196 | pubmed:author | pubmed-author:CastorenaKath... | lld:pubmed |
pubmed-article:17522196 | pubmed:author | pubmed-author:WeeksSpencer... | lld:pubmed |
pubmed-article:17522196 | pubmed:author | pubmed-author:StaplefordKen... | lld:pubmed |
pubmed-article:17522196 | pubmed:author | pubmed-author:CadwalladerAm... | lld:pubmed |
pubmed-article:17522196 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17522196 | pubmed:volume | 81 | lld:pubmed |
pubmed-article:17522196 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17522196 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17522196 | pubmed:pagination | 8412-20 | lld:pubmed |
pubmed-article:17522196 | pubmed:dateRevised | 2010-9-16 | lld:pubmed |
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