| pubmed-article:17170452 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17170452 | lifeskim:mentions | umls-concept:C0035236 | lld:lifeskim |
| pubmed-article:17170452 | lifeskim:mentions | umls-concept:C0337611 | lld:lifeskim |
| pubmed-article:17170452 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:17170452 | lifeskim:mentions | umls-concept:C1167298 | lld:lifeskim |
| pubmed-article:17170452 | lifeskim:mentions | umls-concept:C0035548 | lld:lifeskim |
| pubmed-article:17170452 | lifeskim:mentions | umls-concept:C0042736 | lld:lifeskim |
| pubmed-article:17170452 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:17170452 | lifeskim:mentions | umls-concept:C0205410 | lld:lifeskim |
| pubmed-article:17170452 | lifeskim:mentions | umls-concept:C1136161 | lld:lifeskim |
| pubmed-article:17170452 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
| pubmed-article:17170452 | pubmed:issue | Pt 1 | lld:pubmed |
| pubmed-article:17170452 | pubmed:dateCreated | 2006-12-15 | lld:pubmed |
| pubmed-article:17170452 | pubmed:abstractText | The respiratory syncytial virus (RSV) phosphoprotein (P) is a major polymerase co-factor that interacts with both the large polymerase fragment (L) and the nucleoprotein (N). The N-binding domain of RSV P has been investigated by co-expression of RSV P and N proteins in Escherichia coli. Pull-down assays performed with a series of truncated forms of P fused to glutathione S-transferase (GST) revealed that the region comprising the last nine C-terminal amino acid residues of P (233-DNDLSLEDF-241) is sufficient for efficient binding to N. Site-directed mutagenesis shows that the last four residues of this peptide are crucial for binding and must be present at the end of a flexible C-terminal tail. The presence of the P oligomerization domain (residues 100-160) was an important stabilizing factor for the interaction. The tetrameric full-length P fused to GST was able to pull down both helical and ring structures, whereas a monomeric C-terminal fragment of P (residues 161-241) fused to GST pulled down exclusively RNA-N rings. Electron-microscopy analysis of the purified rings showed the presence of two types of complex: undecamers (11N) and decamers (10N). Mass-spectrometry analysis of the RNA extracted from rings after RNase A treatment showed two peaks of 22,900 and 24,820 Da, corresponding to a mean RNA length of 67 and 73 bases, respectively. These results suggest strongly that each N subunit contacts 6 nt, with an extra three or four bases further protected from nuclease digestion by the ring structure at both the 5' and 3' ends. | lld:pubmed |
| pubmed-article:17170452 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17170452 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17170452 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17170452 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17170452 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17170452 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17170452 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17170452 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17170452 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17170452 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:17170452 | pubmed:issn | 0022-1317 | lld:pubmed |
| pubmed-article:17170452 | pubmed:author | pubmed-author:VarelaPaloma... | lld:pubmed |
| pubmed-article:17170452 | pubmed:author | pubmed-author:BerkenkampSte... | lld:pubmed |
| pubmed-article:17170452 | pubmed:author | pubmed-author:BhellaDavidD | lld:pubmed |
| pubmed-article:17170452 | pubmed:author | pubmed-author:GrosclaudeJea... | lld:pubmed |
| pubmed-article:17170452 | pubmed:author | pubmed-author:ReyFelix AFA | lld:pubmed |
| pubmed-article:17170452 | pubmed:author | pubmed-author:ChilmonczykSt... | lld:pubmed |
| pubmed-article:17170452 | pubmed:author | pubmed-author:CastagnéNatha... | lld:pubmed |
| pubmed-article:17170452 | pubmed:author | pubmed-author:BernardJulieJ | lld:pubmed |
| pubmed-article:17170452 | pubmed:author | pubmed-author:EléouëtJean-F... | lld:pubmed |
| pubmed-article:17170452 | pubmed:author | pubmed-author:TranThi-LanTL | lld:pubmed |
| pubmed-article:17170452 | pubmed:author | pubmed-author:BenhamoVaness... | lld:pubmed |
| pubmed-article:17170452 | pubmed:author | pubmed-author:GrznarovaKata... | lld:pubmed |
| pubmed-article:17170452 | pubmed:author | pubmed-author:NespoulosClau... | lld:pubmed |
| pubmed-article:17170452 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17170452 | pubmed:volume | 88 | lld:pubmed |
| pubmed-article:17170452 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17170452 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17170452 | pubmed:pagination | 196-206 | lld:pubmed |
| pubmed-article:17170452 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:17170452 | pubmed:meshHeading | pubmed-meshheading:17170452... | lld:pubmed |
| pubmed-article:17170452 | pubmed:meshHeading | pubmed-meshheading:17170452... | lld:pubmed |
| pubmed-article:17170452 | pubmed:meshHeading | pubmed-meshheading:17170452... | lld:pubmed |
| pubmed-article:17170452 | pubmed:meshHeading | pubmed-meshheading:17170452... | lld:pubmed |
| pubmed-article:17170452 | pubmed:meshHeading | pubmed-meshheading:17170452... | lld:pubmed |
| pubmed-article:17170452 | pubmed:meshHeading | pubmed-meshheading:17170452... | lld:pubmed |
| pubmed-article:17170452 | pubmed:meshHeading | pubmed-meshheading:17170452... | lld:pubmed |
| pubmed-article:17170452 | pubmed:meshHeading | pubmed-meshheading:17170452... | lld:pubmed |
| pubmed-article:17170452 | pubmed:meshHeading | pubmed-meshheading:17170452... | lld:pubmed |
| pubmed-article:17170452 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17170452 | pubmed:articleTitle | The nine C-terminal amino acids of the respiratory syncytial virus protein P are necessary and sufficient for binding to ribonucleoprotein complexes in which six ribonucleotides are contacted per N protein protomer. | lld:pubmed |
| pubmed-article:17170452 | pubmed:affiliation | Unité de Virologie et Immunologie Moléculaires, INRA, 78350 Jouy-en-Josas, France. | lld:pubmed |
| pubmed-article:17170452 | pubmed:publicationType | Journal Article | lld:pubmed |
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