Source:http://linkedlifedata.com/resource/pubmed/id/10052358
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1999-4-13
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pubmed:databankReference | |
pubmed:abstractText |
Transgenic tobacco plants that synthesize alfalfa ferritin in vegetative tissues--either in its processed form in chloroplasts or in the cytoplasmic nonprocessed form--retained photosynthetic function upon free radical toxicity generated by iron excess or paraquat treatment. Progeny of transgenic plants accumulating ferritin in their leaves exhibited tolerance to necrotic damage caused by viral (tobacco necrosis virus) and fungal (Alternaria alternata, Botrytis cinerea) infections. These transformants exhibited normal photosynthetic function and chlorophyll content under greenhouse conditions. We propose that by sequestering intracellular iron involved in generation of the very reactive hydroxyl radicals through a Fenton reaction, ferritin protects plant cells from oxidative damage induced by a wide range of stresses.
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pubmed:commentsCorrections | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1087-0156
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
17
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
192-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10052358-Alternaria,
pubmed-meshheading:10052358-Base Sequence,
pubmed-meshheading:10052358-Botrytis,
pubmed-meshheading:10052358-DNA Primers,
pubmed-meshheading:10052358-Ferritins,
pubmed-meshheading:10052358-Iron,
pubmed-meshheading:10052358-Medicago sativa,
pubmed-meshheading:10052358-Molecular Sequence Data,
pubmed-meshheading:10052358-Oxidative Stress,
pubmed-meshheading:10052358-Paraquat,
pubmed-meshheading:10052358-Plants, Genetically Modified,
pubmed-meshheading:10052358-Plants, Toxic,
pubmed-meshheading:10052358-Tobacco
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pubmed:year |
1999
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pubmed:articleTitle |
Plants ectopically expressing the iron-binding protein, ferritin, are tolerant to oxidative damage and pathogens.
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pubmed:affiliation |
Institute of Plant Biology, Biological Research Center of the Hungarian Academy of Sciences, Szeged.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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