| dc.contributor.author |
DEMOPOULOS, VP |
en |
| dc.contributor.author |
ZIOGAS, BN |
en |
| dc.date.accessioned |
2014-06-06T06:42:36Z |
|
| dc.date.available |
2014-06-06T06:42:36Z |
|
| dc.date.issued |
1994 |
en |
| dc.identifier.issn |
0048-3575 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/712 |
|
| dc.subject.classification |
Biochemistry & Molecular Biology |
en |
| dc.subject.classification |
Entomology |
en |
| dc.subject.classification |
Physiology |
en |
| dc.subject.other |
ERGOSTEROL BIOSYNTHESIS |
en |
| dc.subject.other |
PENICILLIUM-ITALICUM |
en |
| dc.subject.other |
USTILAGO-MAYDIS |
en |
| dc.subject.other |
WILD-TYPE |
en |
| dc.subject.other |
FUNGICIDES |
en |
| dc.subject.other |
CYTOCHROME-P-450 |
en |
| dc.subject.other |
INHIBITORS |
en |
| dc.subject.other |
MUTANT |
en |
| dc.subject.other |
14-ALPHA-DEMETHYLATION |
en |
| dc.subject.other |
DEMETHYLATION |
en |
| dc.title |
STUDIES ON THE MECHANISM OF EXPRESSION OF A MAJOR GENE MUTATION FOR RESISTANCE TO TRIADIMENOL IN THE FILAMENTOUS PHYTOPATHOGENIC ASCOMYCETE NECTRIA-HAEMATOCOCCA VAR CUCURBITAE |
en |
| heal.type |
journalArticle |
en |
| heal.language |
English |
en |
| heal.publicationDate |
1994 |
en |
| heal.abstract |
The chromosomal major gene mutation at tri-1 locus gives high resistance to triadimenol and low resistance to other triazoles. The same mutation has no effect on sensitivity to nontriazole sterol biosynthesis inhibitors or even increases the sensitivity to certain imidazole derivatives. The tri-1 gene reduces mainly the fungitoxicity of diastereoisomer A of triadimenol (res. factor 58) and has little effect on sensitivity to diastereoisomer B (res. factor 5.5), indicating stereospecificity of the mutation to triadimenol A. There was a low reduction of the ergosterol content in total nonsaponifiable lipids with triadimenol concentrations highly inhibitory to growth of the mutant strain. The higher sensitivity of tri-1 strains to certain imidazoles was correlated with higher inhibition of the 14 alpha-demethylation step of the ergosterol biosynthetic pathway. Electrophoretic profiles of microsomal fractions from a wild-type and a tri-1 strain showed the presence of one hemoprotein band with a molecular weight in the region of 125 kDa and an isoelectric point of 4.4. The connection of the heme with the apoprotein was found more unstable in the case of the enzyme from the mutant strain. Moreover, the peroxidase activity of electrophoresed mutant microsomes was greatly reduced after long storing at a low temperature. The presence of triadimefon in the growth medium increased the intensity of the hemoprotein band to the same extent in both wild-type and mutant strain. From the above results it may be concluded that a structural change in the cytochrome P450(14DM) is probably responsible for the resistance of tri-1 strains to triazoles with no effect on 14 alpha-demethylation ability of the enzyme. (C) 1994 Academic Press, Inc. |
en |
| heal.publisher |
ACADEMIC PRESS INC JNL-COMP SUBSCRIPTIONS |
en |
| heal.journalName |
PESTICIDE BIOCHEMISTRY AND PHYSIOLOGY |
en |
| dc.identifier.issue |
2 |
en |
| dc.identifier.volume |
50 |
en |
| dc.identifier.isi |
ISI:A1994PT65900006 |
en |
| dc.identifier.spage |
159 |
en |
| dc.identifier.epage |
170 |
en |