10859201

Source:http://linkedlifedata.com/resource/pubmed/id/10859201

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0009015, umls-concept:C0010798, umls-concept:C0017262, umls-concept:C0025519, umls-concept:C0063100, umls-concept:C0102216, umls-concept:C0185117, umls-concept:C0242772, umls-concept:C1956100, umls-concept:C2911684
pubmed:issue	2
pubmed:dateCreated	2000-9-7
pubmed:abstractText	Allene oxide synthase (AOS) and fatty acid hydroperoxide lyase (HPL) are plant-specific cytochrome P450s that commit fatty acid hydroperoxides to different branches of oxylipin metabolism. Here we report the cloning and characterization of AOS (LeAOS) and HPL (LeHPL) cDNAs from tomato (Lycopersicon esculentum). Functional expression of the cDNAs in Escherichia coli showed that LeAOS and LeHPL encode enzymes that metabolize 13- but not 9-hydroperoxide derivatives of C(18) fatty acids. LeAOS was active against both 13S-hydroperoxy-9(Z),11(E),15(Z)-octadecatrienoic acid (13-HPOT) and 13S-hydroperoxy-9(Z),11(E)-octadecadienoic acid, whereas LeHPL showed a strong preference for 13-HPOT. These results suggest a role for LeAOS and LeHPL in the metabolism of 13-HPOT to jasmonic acid and hexenal/traumatin, respectively. LeAOS expression was detected in all organs of the plant. In contrast, LeHPL expression was predominant in leaves and flowers. Damage inflicted to leaves by chewing insect larvae led to an increase in the local and systemic expression of both genes, with LeAOS showing the strongest induction. Wound-induced expression of LeAOS also occurred in the def-1 mutant that is deficient in octadecanoid-based signaling of defensive proteinase inhibitor genes. These results demonstrate that tomato uses genetically distinct signaling pathways for the regulation of different classes of wound responsive genes.
pubmed:commentsCorrections	http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-10036774, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-10103020, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-10420644, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-10462435, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-10545469, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-10708853, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-11607285, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-11607420, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-11607534, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-11607536, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-1594598, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-16660762, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-16665806, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-16668490, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-1876834, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-1909580, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-2666279, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-7672118, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-7721745, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-7753776, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-7857301, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-8323283, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-8378325, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-8420948, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-8506358, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-8539290, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-8754681, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-8756596, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-8914325, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-8925919, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-8953771, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-8989885, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-9232884, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-9484484, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-9648747, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-9680973, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-9701595, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-9736997, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-9764311, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-9778849, http://linkedlifedata.com/resource/pubmed/commentcorrection/10859201-9870900
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/0401224
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Aldehyde-Lyases, http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 Enzyme System, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary, http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers, http://linkedlifedata.com/resource/pubmed/chemical/Intramolecular Oxidoreductases, http://linkedlifedata.com/resource/pubmed/chemical/Linoleic Acids, http://linkedlifedata.com/resource/pubmed/chemical/hydroperoxide isomerase, http://linkedlifedata.com/resource/pubmed/chemical/hydroperoxide lyase
pubmed:status	MEDLINE
pubmed:month	Jun
pubmed:issn	0032-0889
pubmed:author	pubmed-author:DeRocherA EAE, pubmed-author:FOXR ARA, pubmed-author:HoweG AGA, pubmed-author:ItorKK, pubmed-author:LORR
pubmed:issnType	Print
pubmed:volume	123
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	711-24
pubmed:dateRevised	2010-9-14
pubmed:meshHeading	pubmed-meshheading:10859201-Aldehyde-Lyases, pubmed-meshheading:10859201-Amino Acid Sequence, pubmed-meshheading:10859201-Base Sequence, pubmed-meshheading:10859201-Cytochrome P-450 Enzyme System, pubmed-meshheading:10859201-DNA, Complementary, pubmed-meshheading:10859201-DNA Primers, pubmed-meshheading:10859201-Escherichia coli, pubmed-meshheading:10859201-Gene Expression Regulation, Enzymologic, pubmed-meshheading:10859201-Gene Expression Regulation, Plant, pubmed-meshheading:10859201-Intramolecular Oxidoreductases, pubmed-meshheading:10859201-Linoleic Acids, pubmed-meshheading:10859201-Lycopersicon esculentum, pubmed-meshheading:10859201-Molecular Sequence Data, pubmed-meshheading:10859201-Sequence Homology, Amino Acid, pubmed-meshheading:10859201-Signal Transduction
pubmed:year	2000
pubmed:articleTitle	Cytochrome P450-dependent metabolism of oxylipins in tomato. Cloning and expression of allene oxide synthase and fatty acid hydroperoxide lyase.
pubmed:affiliation	Department of Energy-Plant Research Laboratory, Michigan State University, East Lansing 48824, USA. howeg@msu.edu
pubmed:publicationType	Journal Article, Research Support, U.S. Gov't, Non-P.H.S.

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