Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 2 de 2
Filter
Add more filters










Database
Language
Publication year range
1.
New Phytol ; 202(4): 1310-1319, 2014 Jun.
Article in English | MEDLINE | ID: mdl-24602105

ABSTRACT

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 cyp83a1 mutants have reduced levels of aliphatic glucosinolates. Loss of CYP83A1 function leads to dramatically reduced parasitic growth of the biotrophic powdery mildew fungus Erysiphe cruciferarum on Arabidopsis thaliana. The cyp83a1 mutants support less well the germination and appressorium formation of E. cruciferarum on the leaf surface and post-penetration conidiophore formation by the fungus. By contrast, a myb28-1 myb29-1 double mutant, which totally lacks aliphatic glucosinolates, shows a wild-type level of susceptibility to E. cruciferarum. The cyp83a1 mutants also lack very-long-chain aldehydes on their leaf surface. Such aldehydes support appressorium formation by E. cruciferarum in vitro. In addition, when chemically complemented with the C26 aldehyde n-hexacosanal, cyp83a1 mutants can again support appressorium formation. The mutants further accumulate 5-methylthiopentanaldoxime, the potentially toxic substrate of CYP83A1. Loss of powdery mildew susceptibility by cyp83a1 may be explained by a reduced supply of the fungus with inductive signals from the host and an accumulation of potentially fungitoxic metabolites.


Subject(s)
Arabidopsis Proteins/genetics , Arabidopsis/enzymology , Ascomycota/physiology , Cytochrome P-450 Enzyme System/genetics , Glucosinolates/metabolism , Host-Pathogen Interactions , Aldehydes/pharmacology , Arabidopsis/genetics , Arabidopsis/microbiology , Arabidopsis Proteins/metabolism , Ascomycota/drug effects , Chlorophyll/metabolism , Cytochrome P-450 Enzyme System/metabolism , Mutation , Plant Leaves/enzymology , Plant Leaves/genetics , Plant Leaves/microbiology , Spores, Fungal
2.
Phys Rev Lett ; 97(1): 018105, 2006 Jul 07.
Article in English | MEDLINE | ID: mdl-16907414

ABSTRACT

We use dibutyl phosphate to simulate the behavior of the phosphate group in DNA towards the attack of low energy electrons. We find that the compound undergoes effective dissociative electron attachment within a low energy resonant feature at 1 eV and a further resonance peaking at 8 eV. The dissociative electron attachment (DEA) reactions are associated with the direct cleavage of the C-O and the P-O bond but also the excision of the PO-, PO3-, H2PO3- units. For the phosphate group coupled in the DNA network these reactions represent single strand breaks. We hence propose that the most direct mechanism of single strand breaks occurring in DNA at subexcitation energies (< 4 eV) is due to DEA directly to the phosphate group.


Subject(s)
DNA Breaks, Single-Stranded/radiation effects , DNA/chemistry , DNA/radiation effects , Electrons , Models, Chemical , Organophosphates/chemistry , Organophosphates/radiation effects , Computer Simulation , Dose-Response Relationship, Radiation , Models, Molecular , Radiation Dosage
SELECTION OF CITATIONS
SEARCH DETAIL
...