rdf:type |
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lifeskim:mentions |
umls-concept:C0004755,
umls-concept:C0016832,
umls-concept:C0069713,
umls-concept:C0319635,
umls-concept:C0871261,
umls-concept:C1095831,
umls-concept:C1314939,
umls-concept:C1521991,
umls-concept:C1704632,
umls-concept:C1706817,
umls-concept:C1880022,
umls-concept:C2911692
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pubmed:issue |
1
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pubmed:dateCreated |
1998-8-31
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pubmed:databankReference |
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pubmed:abstractText |
Previously 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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9576772-16668394,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9576772-1668186,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9576772-6546423,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9576772-8012045,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9576772-8044704,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9576772-8143935,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9576772-8159797,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9576772-8400378,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9576772-8509360,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9576772-8723347,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9576772-8736791,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9576772-9049263,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9576772-9484466
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0032-0889
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
117
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
33-41
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pubmed:dateRevised |
2010-9-13
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pubmed:meshHeading |
pubmed-meshheading:9576772-Amino Acid Sequence,
pubmed-meshheading:9576772-Base Sequence,
pubmed-meshheading:9576772-Genes, Plant,
pubmed-meshheading:9576772-Hordeum,
pubmed-meshheading:9576772-Isoenzymes,
pubmed-meshheading:9576772-Molecular Sequence Data,
pubmed-meshheading:9576772-Oxidoreductases,
pubmed-meshheading:9576772-Plant Diseases,
pubmed-meshheading:9576772-Plant Leaves,
pubmed-meshheading:9576772-Plant Proteins,
pubmed-meshheading:9576772-Sequence Alignment,
pubmed-meshheading:9576772-Sequence Homology, Amino Acid,
pubmed-meshheading:9576772-Transcription, Genetic
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pubmed:year |
1998
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pubmed:articleTitle |
Molecular characterization of the oxalate oxidase involved in the response of barley to the powdery mildew fungus.
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pubmed:affiliation |
Plant Pathology Section, Department of Plant Biology, The Royal Veterinary and Agricultural University, Thorvaldsensvej 40, DK-1871 Frederiksberg C, Copenhagen, Denmark.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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