CYP83A1 is required for metabolic compatibility of Arabidopsis with the adapted powdery mildew fungus Erysiphe cruciferarum. Issue 4 (6th March 2014)

• Record Type: Journal Article
• Authors: Weis, Corina; Hildebrandt, Ulrich; Hoffmann, Thomas; Hemetsberger, Christoph; Pfeilmeier, Sebastian; König, Constanze; Schwab, Wilfried; Eichmann, Ruth; Hückelhoven, Ralph
• Is Part Of: New phytologist. Volume 202:Issue 4(2014)
• Page Start: 1310
• Page End: 1319
• Publication Date: 2014-03-06
• Subjects: Botany -- Periodicals; 580
• DOI: 10.1111/nph.12759
• Languages: English
• ISSNs: 0028-646X

Abstract

<abstract abstract-type="main" id="nph12759-abs-0001"> <title>Summary</title> <p> <list id="nph12759-list-0001" list-type="bullet"> <list-item> <p>Aliphatic glucosinolates function in the chemical defense of Capparales. The cytochrome P450 83A1 monooxygenase (CYP83A1) catalyzes the initial conversion of methionine‐derived aldoximes to thiohydroximates in the biosynthesis of glucosinolates, and thus <italic>cyp83a1</italic> mutants have reduced levels of aliphatic glucosinolates.</p> </list-item> <list-item> <p>Loss of CYP83A1 function leads to dramatically reduced parasitic growth of the biotrophic powdery mildew fungus <italic>Erysiphe cruciferarum</italic> on <italic>Arabidopsis thaliana</italic>. The <italic>cyp83a1</italic> mutants support less well the germination and appressorium formation of <italic>E. cruciferarum</italic> on the leaf surface and post‐penetration conidiophore formation by the fungus. By contrast, a <italic>myb28‐1 myb29‐1</italic> double mutant, which totally lacks aliphatic glucosinolates, shows a wild‐type level of susceptibility to <italic>E. cruciferarum</italic>.</p> </list-item> <list-item> <p>The <italic>cyp83a1</italic> mutants also lack very‐long‐chain aldehydes on their leaf surface. Such aldehydes support appressorium formation by <italic>E. cruciferarum in vitro</italic>. In addition, when chemically complemented with the C26 aldehyde <italic>n</italic>‐hexacosanal, <italic>cyp83a1</italic> mutants can again support appressorium formation. The mutants further accumulate 5‐methylthiopentanaldoxime, the potentially toxic substrate of CYP83A1.</p> </list-item> <list-item> <p>Loss of powdery mildew susceptibility by <italic>cyp83a1</italic> may be explained by a reduced supply of the fungus with inductive signals from the host and an accumulation of potentially fungitoxic metabolites.</p> </list-item> </list> </p> </abstract>