Source:http://linkedlifedata.com/resource/pubmed/id/20876333
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
15
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pubmed:dateCreated |
2010-10-18
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pubmed:abstractText |
Hydrogen peroxide (H(2)O(2)) is an important signal molecule involved in plant development and environmental responses. Changes in H(2)O(2) availability can result from increased production or decreased metabolism. While plants contain several types of H(2)O(2)-metabolizing proteins, catalases are highly active enzymes that do not require cellular reductants as they primarily catalyse a dismutase reaction. This review provides an update on plant catalase genes, function, and subcellular localization, with a focus on recent information generated from studies on Arabidopsis. Original data are presented on Arabidopsis catalase single and double mutants, and the use of some of these lines as model systems to investigate the outcome of increases in intracellular H(2)O(2) are discussed. Particular attention is paid to interactions with cell thiol-disulphide status; the use of catalase-deficient plants to probe the apparent redundancy of reductive H(2)O(2)-metabolizing pathways; the importance of irradiance and growth daylength in determining the outcomes of catalase deficiency; and the induction of pathogenesis-related responses in catalase-deficient lines. Within the context of strategies aimed at understanding and engineering plant stress responses, the review also considers whether changes in catalase activities in wild-type plants are likely to be a significant part of plant responses to changes in environmental conditions or biotic challenge.
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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 |
Oct
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pubmed:issn |
1460-2431
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
61
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4197-220
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pubmed:meshHeading |
pubmed-meshheading:20876333-Amino Acid Sequence,
pubmed-meshheading:20876333-Arabidopsis,
pubmed-meshheading:20876333-Catalase,
pubmed-meshheading:20876333-Models, Biological,
pubmed-meshheading:20876333-Molecular Sequence Data,
pubmed-meshheading:20876333-Mutation,
pubmed-meshheading:20876333-Oxidation-Reduction,
pubmed-meshheading:20876333-Stress, Physiological
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pubmed:year |
2010
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pubmed:articleTitle |
Catalase function in plants: a focus on Arabidopsis mutants as stress-mimic models.
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pubmed:affiliation |
Institut de Biologie des Plantes, UMR CNRS 8618, Université de Paris sud, F-91405 Orsay cedex, France.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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