| http://purl.uniprot.org/citations/12970423 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12970423 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12970423 | http://www.w3.org/2000/01/rdf-schema#comment | "Tacaribe virus (TV) is the prototype of the New World group of arenaviruses. The TV genome encodes four proteins, the nucleoprotein (N), the glycoprotein precursor, the polymerase (L), and a small RING finger protein (Z). Using a reverse genetic system, we recently demonstrated that TV N and L are sufficient to drive transcription and full-cycle RNA replication mediated by TV-like RNAs and that Z is a powerful inhibitor of these processes (N. López, R. Jácamo, and M. T. Franze-Fernández, J. Virol. 65:12241-12251, 2001). In the present study we investigated whether Z might interact with either of the proteins, N and L, required for RNA synthesis. To that end, we used coimmunoprecipitation with monospecific antibodies against the viral proteins and coimmunoprecipitation with serum against glutathione S-transferase (GST) and binding to glutathione-Sepharose beads when Z was expressed as a fusion protein with GST. We demonstrated that Z interacted with L but not with N and that Z inhibitory activity was dependent on its ability to bind to L. We also evaluated the contribution of different Z regions to its binding ability and functional activity. We found that integrity of the RING structure is essential for Z binding to L and for Z inhibitory activity. Mutants with deletions at the N and C termini of Z showed that amino acids within the C-terminal region and immediately adjacent to the RING domain N terminus contribute to efficient Z-L interaction and are required for inhibitory activity. The data presented here provide the first evidence of an interaction between Z and L, suggesting that Z interferes with viral RNA synthesis by direct interaction with L. In addition, coimmunoprecipitation studies revealed a previously unreported interaction between N and L."xsd:string |
| http://purl.uniprot.org/citations/12970423 | http://purl.org/dc/terms/identifier | "doi:10.1128/jvi.77.19.10383-10393.2003"xsd:string |
| http://purl.uniprot.org/citations/12970423 | http://purl.org/dc/terms/identifier | "doi:10.1128/jvi.77.19.10383-10393.2003"xsd:string |
| http://purl.uniprot.org/citations/12970423 | http://purl.uniprot.org/core/author | "Franze-Fernandez M.T."xsd:string |
| http://purl.uniprot.org/citations/12970423 | http://purl.uniprot.org/core/author | "Franze-Fernandez M.T."xsd:string |
| http://purl.uniprot.org/citations/12970423 | http://purl.uniprot.org/core/author | "Jacamo R."xsd:string |
| http://purl.uniprot.org/citations/12970423 | http://purl.uniprot.org/core/author | "Jacamo R."xsd:string |
| http://purl.uniprot.org/citations/12970423 | http://purl.uniprot.org/core/author | "Lopez N."xsd:string |
| http://purl.uniprot.org/citations/12970423 | http://purl.uniprot.org/core/author | "Lopez N."xsd:string |
| http://purl.uniprot.org/citations/12970423 | http://purl.uniprot.org/core/author | "Wilda M."xsd:string |
| http://purl.uniprot.org/citations/12970423 | http://purl.uniprot.org/core/author | "Wilda M."xsd:string |
| http://purl.uniprot.org/citations/12970423 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12970423 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12970423 | http://purl.uniprot.org/core/name | "J. Virol."xsd:string |
| http://purl.uniprot.org/citations/12970423 | http://purl.uniprot.org/core/name | "J. Virol."xsd:string |
| http://purl.uniprot.org/citations/12970423 | http://purl.uniprot.org/core/pages | "10383-10393"xsd:string |
| http://purl.uniprot.org/citations/12970423 | http://purl.uniprot.org/core/pages | "10383-10393"xsd:string |
| http://purl.uniprot.org/citations/12970423 | http://purl.uniprot.org/core/title | "Tacaribe virus Z protein interacts with the L polymerase protein to inhibit viral RNA synthesis."xsd:string |
| http://purl.uniprot.org/citations/12970423 | http://purl.uniprot.org/core/title | "Tacaribe virus Z protein interacts with the L polymerase protein to inhibit viral RNA synthesis."xsd:string |
| http://purl.uniprot.org/citations/12970423 | http://purl.uniprot.org/core/volume | "77"xsd:string |
| http://purl.uniprot.org/citations/12970423 | http://purl.uniprot.org/core/volume | "77"xsd:string |
| http://purl.uniprot.org/citations/12970423 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12970423 |
| http://purl.uniprot.org/citations/12970423 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12970423 |