Linked Life Data

9576772

Source:http://linkedlifedata.com/resource/pubmed/id/9576772

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pubmed-article:9576772pubmed:abstractTextPreviously we reported that oxalate oxidase activity increases in extracts of barley (Hordeum vulgare) leaves in response to the powdery mildew fungus (Blumeria [syn. Erysiphe] graminis f.sp. hordei) and proposed this as a source of H2O2 during plant-pathogen interactions. In this paper we show that the N terminus of the major pathogen-response oxalate oxidase has a high degree of sequence identity to previously characterized germin-like oxalate oxidases. Two cDNAs were isolated, pHvOxOa, which represents this major enzyme, and pHvOxOb', representing a closely related enzyme. Our data suggest the presence of only two oxalate oxidase genes in the barley genome, i.e. a gene encoding HvOxOa, which possibly exists in several copies, and a single-copy gene encoding HvOxOb. The use of 3' end gene-specific probes has allowed us to demonstrate that the HvOxOa transcript accumulates to 6 times the level of the HvOxOb transcript in response to the powdery mildew fungus. The transcripts were detected in both compatible and incompatible interactions with a similar accumulation pattern. The oxalate oxidase is found exclusively in the leaf mesophyll, where it is cell wall located. A model for a signal transduction pathway in which oxalate oxidase plays a central role is proposed for the regulation of the hypersensitive response.lld:pubmed
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pubmed-article:9576772pubmed:articleTitleMolecular characterization of the oxalate oxidase involved in the response of barley to the powdery mildew fungus.lld:pubmed
pubmed-article:9576772pubmed:affiliationPlant Pathology Section, Department of Plant Biology, The Royal Veterinary and Agricultural University, Thorvaldsensvej 40, DK-1871 Frederiksberg C, Copenhagen, Denmark.lld:pubmed
pubmed-article:9576772pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9576772pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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