Source:http://linkedlifedata.com/resource/pubmed/id/16146525
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2005-9-8
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pubmed:abstractText |
The Arabidopsis acyl-CoA oxidase (ACX) family comprises isozymes with distinct fatty acid chain-length specificities that together catalyse the first step of peroxisomal fatty acid beta-oxidation. We have isolated and characterized T-DNA insertion mutants in the medium to long-chain (ACX1) and long-chain (ACX2) acyl-CoA oxidases, and show that the corresponding endogenous activities are decreased in the mutants. Lipid catabolism during germination and early post-germinative growth was unaltered in the acx1-1 mutant, but slightly delayed in the acx2-1 mutant, with 3-day-old acx2-1 seedlings accumulating long-chain acyl-CoAs. In acx1-1 and acx2-1, seedling growth and establishment in the absence of an exogenous supply of sucrose was unaffected. Seedlings of the double mutant acx1-1 acx2-1 were unable to catabolize seed storage lipid, and accumulated long-chain acyl-CoAs. The acx1-1 acx2-1 seedlings were also unable to establish photosynthetic competency in the absence of an exogenous carbon supply, a phenotype that is shared with a number of other Arabidopsis mutants disrupted in storage lipid breakdown. Germination frequency of the double mutant was significantly reduced compared with wild-type seeds. This was unaffected by the addition of exogenous sucrose, but was improved by dormancy-breaking treatments such as cold stratification and after-ripening. We show that the acx1-1, acx2-1 and acx1-2 acx2-1 double mutants and the ketoacyl-CoA thiolase-2 (kat2) mutant exhibit a sucrose-independent germination phenotype comparable with that reported for comatose (cts-2), a mutant in a peroxisomal ABC transporter which exhibits enhanced dormancy. This demonstrates an additional role beyond that of carbon provision for the beta-oxidation pathway during germination or in dormant seeds.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ACX1 protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Acyl Coenzyme A,
http://linkedlifedata.com/resource/pubmed/chemical/Acyl-CoA Oxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclopentanes,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Oxylipins,
http://linkedlifedata.com/resource/pubmed/chemical/Sucrose,
http://linkedlifedata.com/resource/pubmed/chemical/jasmonic acid
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0960-7412
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
43
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
861-72
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:16146525-Acyl Coenzyme A,
pubmed-meshheading:16146525-Acyl-CoA Oxidase,
pubmed-meshheading:16146525-Arabidopsis,
pubmed-meshheading:16146525-Arabidopsis Proteins,
pubmed-meshheading:16146525-Cyclopentanes,
pubmed-meshheading:16146525-Fatty Acids,
pubmed-meshheading:16146525-Germination,
pubmed-meshheading:16146525-Mutation,
pubmed-meshheading:16146525-Oxylipins,
pubmed-meshheading:16146525-Peroxisomes,
pubmed-meshheading:16146525-Seedling,
pubmed-meshheading:16146525-Sucrose,
pubmed-meshheading:16146525-Time Factors
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pubmed:year |
2005
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pubmed:articleTitle |
Sucrose rescues seedling establishment but not germination of Arabidopsis mutants disrupted in peroxisomal fatty acid catabolism.
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pubmed:affiliation |
CNAP, Department of Biology, University of York, PO Box 373, York YO10 5YW, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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