| pubmed-article:19684283 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19684283 | lifeskim:mentions | umls-concept:C0017535 | lld:lifeskim |
| pubmed-article:19684283 | lifeskim:mentions | umls-concept:C0016192 | lld:lifeskim |
| pubmed-article:19684283 | lifeskim:mentions | umls-concept:C1704448 | lld:lifeskim |
| pubmed-article:19684283 | lifeskim:mentions | umls-concept:C0001383 | lld:lifeskim |
| pubmed-article:19684283 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
| pubmed-article:19684283 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
| pubmed-article:19684283 | lifeskim:mentions | umls-concept:C1554184 | lld:lifeskim |
| pubmed-article:19684283 | lifeskim:mentions | umls-concept:C1709450 | lld:lifeskim |
| pubmed-article:19684283 | lifeskim:mentions | umls-concept:C1551359 | lld:lifeskim |
| pubmed-article:19684283 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:19684283 | pubmed:dateCreated | 2009-10-5 | lld:pubmed |
| pubmed-article:19684283 | pubmed:abstractText | A Giardia-specific protein family denominated as alpha-giardins, represents the major protein component, besides tubulin, of the cytoskeleton of the human pathogenic parasite Giardia lamblia. One of its members, alpha19-giardin, carries an N-terminal sequence extension of MGCXXS, which in many proteins serves as a target for dual lipid conjugation: myristoylation at the glycine residue after removal of the methionine and palmitoylation at the cysteine residue. As the first experimental evidence of a lipid modification, we found alpha19-giardin to be associated with the membrane fraction of disrupted trophozoites. After heterologous coexpression of alpha19-giardin with giardial N-myristoyltransferase (NMT) in Escherichia coli, we found the protein in a myristoylated form. Additionally, after heterologous expression together with the palmitoyl transferase Pfa3 in Saccharomyces cerevisiae, alpha19-giardin associates with the membrane of the main vacuole. Immunocytochemical colocalization studies on wild-type Giardia trophozoites with tubulin provide evidence that alpha19-giardin exclusively localizes to the ventral pair of the giardial flagella. A mutant in which the putatively myristoylated N-terminal glycine residue was replaced by alanine lost this specific localization. Our findings suggest that the dual lipidation of alpha19-giardin is responsible for its specific flagellar localization. | lld:pubmed |
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| pubmed-article:19684283 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19684283 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19684283 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19684283 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19684283 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19684283 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:19684283 | pubmed:issn | 1535-9786 | lld:pubmed |
| pubmed-article:19684283 | pubmed:author | pubmed-author:HehlAdrian... | lld:pubmed |
| pubmed-article:19684283 | pubmed:author | pubmed-author:ScholzeHennin... | lld:pubmed |
| pubmed-article:19684283 | pubmed:author | pubmed-author:VahrmannAnkeA | lld:pubmed |
| pubmed-article:19684283 | pubmed:author | pubmed-author:SaricMirelaM | lld:pubmed |
| pubmed-article:19684283 | pubmed:author | pubmed-author:NieburDaniela... | lld:pubmed |
| pubmed-article:19684283 | pubmed:author | pubmed-author:KluempersVere... | lld:pubmed |
| pubmed-article:19684283 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19684283 | pubmed:volume | 8 | lld:pubmed |
| pubmed-article:19684283 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19684283 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19684283 | pubmed:pagination | 1567-74 | lld:pubmed |
| pubmed-article:19684283 | pubmed:dateRevised | 2010-9-27 | lld:pubmed |
| pubmed-article:19684283 | pubmed:meshHeading | pubmed-meshheading:19684283... | lld:pubmed |
| pubmed-article:19684283 | pubmed:meshHeading | pubmed-meshheading:19684283... | lld:pubmed |
| pubmed-article:19684283 | pubmed:meshHeading | pubmed-meshheading:19684283... | lld:pubmed |
| pubmed-article:19684283 | pubmed:meshHeading | pubmed-meshheading:19684283... | lld:pubmed |
| pubmed-article:19684283 | pubmed:meshHeading | pubmed-meshheading:19684283... | lld:pubmed |
| pubmed-article:19684283 | pubmed:meshHeading | pubmed-meshheading:19684283... | lld:pubmed |
| pubmed-article:19684283 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19684283 | pubmed:articleTitle | Dual acylation accounts for the localization of {alpha}19-giardin in the ventral flagellum pair of Giardia lamblia. | lld:pubmed |
| pubmed-article:19684283 | pubmed:affiliation | Faculty of Biology/Chemistry, Barbarastrasse 13, D-49069 Osnabrueck, Germany. | lld:pubmed |
| pubmed-article:19684283 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19684283 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:5697719 | entrezgene:pubmed | pubmed-article:19684283 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:19684283 | lld:entrezgene |
