| pubmed-article:10405356 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10405356 | lifeskim:mentions | umls-concept:C0520502 | lld:lifeskim |
| pubmed-article:10405356 | lifeskim:mentions | umls-concept:C0026649 | lld:lifeskim |
| pubmed-article:10405356 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:10405356 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:10405356 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:10405356 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:10405356 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:10405356 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:10405356 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:10405356 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:10405356 | pubmed:dateCreated | 1999-8-24 | lld:pubmed |
| pubmed-article:10405356 | pubmed:abstractText | To study subdomain organization of the potato virus X (PVX) movement protein (MP) encoded by the first gene in the triple gene block (TGB), we mutated the 25-kDa TGBp1 protein. The N-terminal deletion of the helicase motifs I, IA, and II resulted in loss of the ATPase activity and RNA binding. A frameshift mutation truncating the C-terminal motifs V and VI gave rise to increase of the TGBp1 ATPase activity and had little effect on RNA binding in vitro. Fusions of the green fluorescent protein with 25-kDa MP and its derivative lacking motifs V-VI exhibited similar fluorescence patterns in epidermal cells of Nicotiana benthamiana leaves. Cell-to-cell movement of the 25K-deficient PVX genome was not complemented by the TGBp1 of Plantago asiatica mosaic potexvirus (PlAMV) but was efficiently complemented by a chimeric TGBp1 consisting of the N-terminal part of PlAMV protein (motifs I-IV) and the PVX-specific C-terminal part (motifs V-VI). These results suggest that NTP hydrolysis, RNA binding, and targeting to the specific cellular compartment(s) are associated with the N-terminal domain of the TGBp1 including the helicase motifs I-IV and that the C-terminal domain is involved in specific interactions with other virus proteins. | lld:pubmed |
| pubmed-article:10405356 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10405356 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10405356 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10405356 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10405356 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10405356 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10405356 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10405356 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10405356 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10405356 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:10405356 | pubmed:issn | 0042-6822 | lld:pubmed |
| pubmed-article:10405356 | pubmed:author | pubmed-author:AtabekovJ GJG | lld:pubmed |
| pubmed-article:10405356 | pubmed:author | pubmed-author:KalininaN ONO | lld:pubmed |
| pubmed-article:10405356 | pubmed:author | pubmed-author:MorozovS YSY | lld:pubmed |
| pubmed-article:10405356 | pubmed:author | pubmed-author:SchiemannJJ | lld:pubmed |
| pubmed-article:10405356 | pubmed:author | pubmed-author:FedorkinO NON | lld:pubmed |
| pubmed-article:10405356 | pubmed:author | pubmed-author:SolovyevA GAG | lld:pubmed |
| pubmed-article:10405356 | pubmed:author | pubmed-author:SamuilovaO... | lld:pubmed |
| pubmed-article:10405356 | pubmed:copyrightInfo | Copyright 1999 Academic Press. | lld:pubmed |
| pubmed-article:10405356 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10405356 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:10405356 | pubmed:volume | 260 | lld:pubmed |
| pubmed-article:10405356 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10405356 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10405356 | pubmed:pagination | 55-63 | lld:pubmed |
| pubmed-article:10405356 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:10405356 | pubmed:meshHeading | pubmed-meshheading:10405356... | lld:pubmed |
| pubmed-article:10405356 | pubmed:meshHeading | pubmed-meshheading:10405356... | lld:pubmed |
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| pubmed-article:10405356 | pubmed:meshHeading | pubmed-meshheading:10405356... | lld:pubmed |
| pubmed-article:10405356 | pubmed:meshHeading | pubmed-meshheading:10405356... | lld:pubmed |
| pubmed-article:10405356 | pubmed:meshHeading | pubmed-meshheading:10405356... | lld:pubmed |
| pubmed-article:10405356 | pubmed:meshHeading | pubmed-meshheading:10405356... | lld:pubmed |
| pubmed-article:10405356 | pubmed:meshHeading | pubmed-meshheading:10405356... | lld:pubmed |
| pubmed-article:10405356 | pubmed:meshHeading | pubmed-meshheading:10405356... | lld:pubmed |
| pubmed-article:10405356 | pubmed:meshHeading | pubmed-meshheading:10405356... | lld:pubmed |
| pubmed-article:10405356 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10405356 | pubmed:articleTitle | Evidence for two nonoverlapping functional domains in the potato virus X 25K movement protein. | lld:pubmed |
| pubmed-article:10405356 | pubmed:affiliation | A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow, 119899, Russia. | lld:pubmed |
| pubmed-article:10405356 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10405356 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10405356 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10405356 | lld:pubmed |
