<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>Tomczynska, Iga</dc:creator>
  <dc:creator>Stumpe, Michael</dc:creator>
  <dc:creator>Mauch, Felix</dc:creator>
  <dc:date>2018-07-01</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">Plant pathogens of the oomycete genus Phytophthora produce virulence factors,  known as RxLR effector proteins that are transferred into host cells to suppress  disease resistance. Here, we analyse the function of the highly conserved RxLR24  effector of Phytophthora brassicae. RxLR24 was expressed early in the interaction  with Arabidopsis plants and ectopic expression in the host enhanced leaf colonization  and zoosporangia formation. Co‐immunoprecipitation (Co‐IP) experiments followed by  mass spectrometry identified different members of the RABA GTPase family as  putative RxLR24 targets. Physical interaction of RxLR24 or its homologue from the  potato pathogen Phytophthora infestans with different RABA GTPases of Arabidopsis  or potato, respectively, was confirmed by reciprocal Co‐IP. In line with the function of  RABA GTPases in vesicular secretion, RxLR24 co‐localized with RABA1a to vesicles  and the plasma membrane. The effect of RxLR24 on the secretory process was  analysed with fusion constructs of secreted antimicrobial proteins with a pH‐sensitive  GFP tag. PATHOGENESIS RELATED PROTEIN 1 (PR‐1) and DEFENSIN (PDF1.2)  were efficiently exported in control tissue, whereas in the presence of RxLR24 they  both accumulated in the endoplasmic reticulum. Together our results imply a virulence  function of RxLR24 effectors as inhibitors of RABA GTPase‐mediated vesicular  secretion of antimicrobial PR‐1, PDF1.2 and possibly other defence‐related  compounds.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://folia.unifr.ch/global/documents/307398</dc:identifier>
  <dc:identifier>https://folia.unifr.ch/documents/307398/files/mau_cre.pdf</dc:identifier>
  <dc:identifier>https://folia.unifr.ch/documents/307398/files/mau_cre_sm.pdf</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1111/tpj.13928</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:rights>License undefined</dc:rights>
  <dc:source>The Plant Journal. - 2018, vol. 95, no. 2, p. 187–203</dc:source>
  <dc:subject>info:eu-repo/classification/udc/57</dc:subject>
  <dc:title xmlns:ns1="xml" ns1:lang="en">A conserved RxLR effector interacts with host RABA-type GTPases to inhibit vesicle-mediated secretion of antimicrobial proteins</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>