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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
26
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pubmed:dateCreated |
1995-2-2
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pubmed:abstractText |
In the bacterium Alcaligenes eutrophus, three genes encode the enzymes necessary to catalyze the synthesis of poly[(R)-(-)-3-hydroxybutyrate] (PHB) from acetyl-CoA. In order to target these enzymes into the plastids of higher plants, the genes were modified by addition of DNA fragments encoding a pea chloroplast transit peptide, a constitutive plant promoter, and a poly(A) addition sequence. Each of the modified bacterial genes was introduced into Arabidopsis thaliana by Agrobacterium-mediated transformation, and plants containing all three genes were obtained by sexual crosses. These plants accumulated PHB up to 14% of the dry weight as 0.2- to 0.7-micron granules within plastids. In contrast to earlier experiments in which expression of the PHB biosynthetic pathway in the cytoplasm led to a deleterious effect on growth, expression of the PHB biosynthetic pathway in plastids had no obvious effect on the growth or fertility of the transgenic plants and resulted in a 100-fold increase in the amount of PHB that accumulated. We conclude that there does not appear to be any biological barrier to high-level production of PHB in higher plants. The high level of PHB accumulation also suggests that the synthesis of plastid acetyl-CoA is regulated by a mechanism which responds to metabolic demand.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809117-1015943,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809117-1366894,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809117-14135548,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809117-16346184,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809117-16664354,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809117-16666863,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809117-17787950,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809117-2046547,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809117-4723225,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809117-6086332,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809117-8219042
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
91
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pubmed:geneSymbol |
phbA,
phbB,
phbC
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12760-4
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pubmed:dateRevised |
2010-9-13
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pubmed:meshHeading |
pubmed-meshheading:7809117-Acyltransferases,
pubmed-meshheading:7809117-Aldehyde Oxidoreductases,
pubmed-meshheading:7809117-Amino Acid Sequence,
pubmed-meshheading:7809117-Arabidopsis,
pubmed-meshheading:7809117-Cell Compartmentation,
pubmed-meshheading:7809117-Molecular Sequence Data,
pubmed-meshheading:7809117-Plants, Genetically Modified,
pubmed-meshheading:7809117-Plastids,
pubmed-meshheading:7809117-Polyesters,
pubmed-meshheading:7809117-Recombinant Proteins
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pubmed:year |
1994
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pubmed:articleTitle |
Targeting of the polyhydroxybutyrate biosynthetic pathway to the plastids of Arabidopsis thaliana results in high levels of polymer accumulation.
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pubmed:affiliation |
Department of Plant Biology, Carnegie Institution of Washington, Stanford, CA 94305.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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