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dc.contributor.authorChen, Mingjieeng
dc.contributor.authorMooney, Brian P.eng
dc.contributor.authorHajduch, Martineng
dc.contributor.authorJoshi, Trupti, 1977-eng
dc.contributor.authorZhou, Mingyieng
dc.contributor.authorXu, Dong, 1965-eng
dc.contributor.authorThelen, Jay J.eng
dc.date.issued2009eng
dc.description.abstractEmbryo-specific overexpression of biotin carboxyl carrier protein 2 (BCCP2) inhibited plastid acetyl-coenzyme A carboxylase (ACCase), resulting in altered oil, protein, and carbohydrate composition in mature Arabidopsis (Arabidopsis thaliana) seed. To characterize gene and protein regulatory consequences of this mutation, global microarray, two-dimensional difference gel electrophoresis, iTRAQ, and quantitative immunoblotting were performed in parallel. These analyses revealed that (1) transgenic overexpression of BCCP2 did not affect the expression of three other ACCase subunits; (2) four subunits to plastid pyruvate dehydrogenase complex were 25% to 70% down-regulated at protein but not transcript levels; (3) key glycolysis and de novo fatty acid/lipid synthesis enzymes were induced; (4) multiple storage proteins, but not cognate transcripts, were up-regulated; and (5) the biotin synthesis pathway was up-regulated at both transcript and protein levels. Biotin production appears closely matched to endogenous BCCP levels, since overexpression of BCCP2 produced mostly apo-BCCP2 and the resulting ACCase-compromised, low-oil phenotype. Differential expression of glycolysis, plastid pyruvate dehydrogenase complex, fatty acid, and lipid synthesis activities indicate multiple, complex regulatory responses including feedback as well as futile "feed-forward" elicitation in the case of fatty acid and lipid biosynthetic enzymes. Induction of storage proteins reveals that oil and protein synthesis share carbon intermediate(s) and that reducing malonyl-coenzyme A flow into fatty acids diverts carbon into amino acid and protein synthesis.eng
dc.identifier.citationPlant Physiology 150:27-41 (2009)eng
dc.identifier.issn1532-2548eng
dc.identifier.urihttp://hdl.handle.net/10355/3239eng
dc.languageEnglisheng
dc.publisherAmerican Society of Plant Biologistseng
dc.relation.ispartofProteomics Center publications (MU)eng
dc.relation.ispartofcommunityUniversity of Missouri-Columbia. Christopher S. Bond Life Sciences Center. Proteomics Centereng
dc.rightsOpenAccesseng
dc.rights.licenseThis work is licensed under a Creative Commons Attribution-NonCommerical-NoDerivs 3.0 License.
dc.subjectembyroeng
dc.subjectoileng
dc.subjectproteineng
dc.subjectseedeng
dc.subjectcarbohydrateseng
dc.subject.disciplineLife scienceseng
dc.subject.lcshArabidopsis thaliana -- Seedseng
dc.subject.lcshTwo-dimensional electrophoresiseng
dc.subject.lcshImmunoblottingeng
dc.subject.lcshFatty acids -- Synthesiseng
dc.subject.lcshPlant proteomicseng
dc.titleSystem analysis of an Arabidopsis mutant altered in de novo fatty acid synthesis reveals diverse changes in seed composition and metabolismeng
dc.typeArticleeng


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