<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>Gamir, Jordi</dc:creator>
  <dc:creator>Darwiche, Rabih</dc:creator>
  <dc:creator>Hof, Pieter van't</dc:creator>
  <dc:creator>Choudhary, Vineet</dc:creator>
  <dc:creator>Stumpe, Michael</dc:creator>
  <dc:creator>Schneiter, Roger</dc:creator>
  <dc:creator>Mauch, Felix</dc:creator>
  <dc:date>2017-02-01</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">Pathogenesis-related proteins played a pioneering role 50 years ago in the discovery  of plant innate immunity as a set of proteins that accumulated upon pathogen  challenge. The most abundant of these proteins, PATHOGENESIS-RELATED 1 (PR-1)  encodes a small antimicrobial protein that has become, as a marker of plant immune  signaling, one of the most referred to plant proteins. The biochemical activity and mode  of action of PR-1 proteins has remained elusive, however. Here, we provide genetic  and biochemical evidence for the capacity of PR-1 proteins to bind sterols, and  demonstrate that the inhibitory effect on pathogen growth is caused by the  sequestration of sterol from pathogens. In support of our findings, sterol-auxotroph  pathogens such as the oomycete Phytophthora are particularly sensitive to PR-1,  whereas sterol-prototroph fungal pathogens become highly sensitive only when sterol  biosynthesis is compromised. Our results are in line with previous findings showing  that plants with enhanced PR-1 expression are particularly well protected against  oomycete pathogens.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://folia.unifr.ch/global/documents/305452</dc:identifier>
  <dc:identifier>https://folia.unifr.ch/documents/305452/files/mau_sba.pdf</dc:identifier>
  <dc:identifier>https://folia.unifr.ch/documents/305452/files/mau_sba_sm.pdf</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1111/tpj.13398</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:rights>License undefined</dc:rights>
  <dc:source>The Plant Journal. - 2017, vol. 89, no. 3, p. 502–509</dc:source>
  <dc:subject xmlns:ns1="xml" ns1:lang="en">PR-1</dc:subject>
  <dc:subject xmlns:ns2="xml" ns2:lang="en">CAP protein</dc:subject>
  <dc:subject xmlns:ns3="xml" ns3:lang="en">antimicrobial protein</dc:subject>
  <dc:subject xmlns:ns4="xml" ns4:lang="en">Phytophthora</dc:subject>
  <dc:subject xmlns:ns5="xml" ns5:lang="en">sterol binding</dc:subject>
  <dc:subject xmlns:ns6="xml" ns6:lang="en">plant immunity</dc:subject>
  <dc:subject>info:eu-repo/classification/udc/57</dc:subject>
  <dc:title xmlns:ns7="xml" ns7:lang="en">The sterol-binding activity of PATHOGENESIS-RELATED PROTEIN 1 reveals the mode of action of an antimicrobial protein</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>
