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@prefix dc: .
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@prefix diseaseontology: .
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@prefix drug: .
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pubmed-article:18208519 a pubmed:Citation ;
lifeskim:mentions umls-concept:C0025252 , umls-concept:C0230839 , umls-concept:C0008266 , umls-concept:C0026882 , umls-concept:C0001721 , umls-concept:C1563744 ;
pubmed:issue "1" ;
pubmed:dateCreated "2008-3-20" ;
pubmed:abstractText "Lipid biosynthesis in plant cells is associated with various organelles, and maintenance of cell lipid homeostasis requires nimble regulation and coordination. In plants, environmental cues such as phosphate limitation require readjustment of the lipid biosynthetic machinery to substitute phospholipids by non-phosphorous glycolipids. Biosynthesis of the galactoglycerolipids predominant in plants proceeds by a constitutive and an alternative pathway that is known to be induced in response to phosphate deprivation. Plant lipid galactosyltransferases involved in both pathways are associated with the plastid envelope membranes and are encoded by nuclear genes. To identify mechanisms governing the activity of the alternative galactoglycerolipid pathway, a genetic suppressor screen was conducted in the background of the digalactolipid-deficient dgd1 mutant of Arabidopsis. A suppressor line that partially restored digalactoglycerolipid content in the dgd1 background carries a point mutation in a mitochondrial protein, which was tentatively designated DGD1 SUPPRESSOR 1 (DGS1). Presumed orthologs of this protein are present in plants, algae and fungi, but its molecular function is not yet known. In the dgd1 dgs1 double mutant, expression of nuclear genes encoding enzymes of the alternative galactoglycerolipid pathway is increased and hydrogen peroxide levels are elevated. This increase in hydrogen peroxide is proposed to be the reason for activation of the alternative pathway in the dgd1 dgs1 double mutant. Accordingly, hydrogen peroxide and treatments producing reactive oxygen also activate the alternative pathway in the wild-type. These results likely implicate the production of reactive oxygen in the regulation of the alternative galactoglycerolipid pathway in plants." ;
pubmed:language "eng" ;
pubmed:journal ;
pubmed:citationSubset "IM" ;
pubmed:chemical , , , , , ;
pubmed:status "MEDLINE" ;
pubmed:month "Apr" ;
pubmed:issn "1365-313X" ;
pubmed:author pubmed-author:BenningChristophC , pubmed-author:XuChangchengC , pubmed-author:FanJilianJ , ;
pubmed:issnType "Electronic" ;
pubmed:volume "54" ;
pubmed:owner "NLM" ;
pubmed:authorsComplete "Y" ;
pubmed:pagination "163-75" ;
pubmed:meshHeading pubmed-meshheading:18208519-Chloroplasts , pubmed-meshheading:18208519-Lipids , pubmed-meshheading:18208519-Mutation , , , pubmed-meshheading:18208519-Phylogeny , , , pubmed-meshheading:18208519-Galactosyltransferases , pubmed-meshheading:18208519-Arabidopsis , , , ;
pubmed:year "2008" ;
pubmed:articleTitle "Mutation of a mitochondrial outer membrane protein affects chloroplast lipid biosynthesis." ;
pubmed:affiliation "Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA." ;
pubmed:publicationType "Journal Article" , "Research Support, U.S. Gov't, Non-P.H.S." .