| pubmed-article:15994785 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15994785 | lifeskim:mentions | umls-concept:C0038164 | lld:lifeskim |
| pubmed-article:15994785 | lifeskim:mentions | umls-concept:C0035685 | lld:lifeskim |
| pubmed-article:15994785 | lifeskim:mentions | umls-concept:C0597717 | lld:lifeskim |
| pubmed-article:15994785 | lifeskim:mentions | umls-concept:C1515655 | lld:lifeskim |
| pubmed-article:15994785 | pubmed:issue | 14 | lld:pubmed |
| pubmed-article:15994785 | pubmed:dateCreated | 2005-7-4 | lld:pubmed |
| pubmed-article:15994785 | pubmed:abstractText | Flock house virus (FHV) is the best-characterized member of the Nodaviridae, a family of small, positive-strand RNA viruses. Unlike most RNA viruses, FHV encodes only a single polypeptide, protein A, that is required for RNA replication. Protein A contains a C-proximal RNA-dependent RNA polymerase domain and localizes via an N-terminal transmembrane domain to the outer mitochondrial membrane, where FHV RNA replication takes place in association with invaginations referred to as spherules. We demonstrate here that protein A self-interacts in vivo by using flow cytometric analysis of fluorescence resonance energy transfer (FRET), spectrofluorometric analysis of bioluminescence resonance energy transfer, and coimmunoprecipitation. Several nonoverlapping protein A sequences were able to independently direct protein-protein interaction, including an N-terminal region previously shown to be sufficient for localization to the outer mitochondrial membrane (D. J. Miller and P. Ahlquist, J. Virol. 76:9856-9867, 2000). Mutations in protein A that diminished FRET also diminished FHV RNA replication, a finding consistent with an important role for protein A self-interaction in FHV RNA synthesis. Thus, the results imply that FHV protein A functions as a multimer rather than as a monomer at one or more steps in RNA replication. | lld:pubmed |
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| pubmed-article:15994785 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15994785 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15994785 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15994785 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15994785 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15994785 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:15994785 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:15994785 | pubmed:author | pubmed-author:AhlquistPaulP | lld:pubmed |
| pubmed-article:15994785 | pubmed:author | pubmed-author:MillerDavid... | lld:pubmed |
| pubmed-article:15994785 | pubmed:author | pubmed-author:DyeBilly TBT | lld:pubmed |
| pubmed-article:15994785 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15994785 | pubmed:volume | 79 | lld:pubmed |
| pubmed-article:15994785 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15994785 | pubmed:authorsComplete | Y | lld:pubmed |
