<oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:creator>Jaquenoud, Malika</dc:creator>
  <dc:creator>Pagac, Martin</dc:creator>
  <dc:creator>Signorell, Aita</dc:creator>
  <dc:creator>Benghezal, Mohammed</dc:creator>
  <dc:creator>Jelk, Jennifer</dc:creator>
  <dc:creator>Bütikofer, Peter</dc:creator>
  <dc:creator>Conzelmann, Andreas</dc:creator>
  <dc:date>2007-12-07</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">Glycosylphosphatidylinositol (GPI) lipids of &lt;i&gt;Trypanosoma brucei&lt;/i&gt; undergo lipid remodelling, whereby longer fatty acids on the glycerol are replaced by myristate (C14:0). A similar process occurs on GPI proteins of &lt;i&gt;Saccharomyces cerevisiae&lt;/i&gt; where Per1p first deacylates, Gup1p subsequently reacylates the anchor lipid, thus replacing a shorter fatty acid by C26:0. Heterologous expression of the &lt;i&gt;GUP1&lt;/i&gt; homologue of &lt;i&gt;T. bruce&lt;/i&gt;i in &lt;i&gt;gup1&lt;/i&gt;Δ yeast cells partially normalizes the &lt;i&gt;gup1&lt;/i&gt;Δ phenotype and restores the transfer of labelled fatty acids from Coenzyme A to &lt;i&gt;lyso&lt;/i&gt;-GPI proteins in a newly developed microsomal assay. In this assay, the Gup1p from &lt;i&gt;T. brucei&lt;/i&gt; (tbGup1p) strongly prefers C14:0 and C12:0 over C16:0 and C18:0, whereas yeast Gup1p strongly prefers C16:0 and C18:0. This acyl specificity of tbGup1p closely matches the reported specificity of the reacylation of free &lt;i&gt;lyso&lt;/i&gt;-GPI lipids in microsomes of &lt;i&gt;T. brucei&lt;/i&gt;. Depletion of tbGup1p in trypanosomes by RNAi drastically reduces the rate of myristate incorporation into the &lt;i&gt;sn&lt;/i&gt;-2 position of &lt;i&gt;lyso&lt;/i&gt;-GPI lipids. Thus, tbGup1p is involved in the addition of myristate to &lt;i&gt;sn&lt;/i&gt;-2 during GPI remodelling in &lt;i&gt;T. brucei&lt;/i&gt; and can account for the fatty acid specificity of this process. tbGup1p can act on GPI proteins as well as on GPI lipids.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://folia.unifr.ch/global/documents/300683</dc:identifier>
  <dc:identifier>https://folia.unifr.ch/documents/300683/files/conzelmann_ght.pdf</dc:identifier>
  <dc:identifier>https://folia.unifr.ch/documents/300683/files/conzelmann_ght_sm.pdf</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1111/j.1365-2958.2007.06043.x</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:rights>License undefined</dc:rights>
  <dc:source>Molecular Microbiology. - 2008, vol. 67, no. 1, p. 202-212</dc:source>
  <dc:subject>info:eu-repo/classification/udc/57</dc:subject>
  <dc:title xmlns:ns1="xml" ns1:lang="en">The &lt;i&gt;Gup1&lt;/i&gt; homologue of &lt;i&gt;Trypanosoma brucei&lt;/i&gt; is a GPI glycosylphosphatidylinositol remodelase</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>
