Source:http://linkedlifedata.com/resource/pubmed/id/20374530
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2010-7-19
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pubmed:abstractText |
A genetic screen in Arabidopsis was developed to explore the regulation of chloroplast protein import in vivo using two independent reporters representing housekeeping and photosynthetic pre-proteins. We first used 5-enolpyruvylshikimate 3-phosphate synthase (EPSP synthase*), a key enzyme in the shikimic acid pathway, with a mutation that confers tolerance to the herbicide glyphosate. Because the EPSP synthase* pre-protein must be imported for its function, the loss of glyphosate tolerance provided an initial indication of an import deficiency. Second, the fate of GFP fused to a ferredoxin transit peptide (FD5-GFP) was determined. A class of altered chloroplast import (aci) mutants showed both glyphosate sensitivity and FD5-GFP mislocalized to nuclei. aci2-1 was selected for further study. Yellow fluorescent protein (YFP) fused to the transit peptide of EPSP synthase* or the small subunit of Rubisco was not imported into chloroplasts, but also localized to nuclei during protoplast transient expression. Isolated aci2-1 chloroplasts showed a 50% reduction in pre-protein import efficiency in an in vitro assay. Mutants did not grow photoautotrophically on media without sucrose and were small and dark green in soil. aci2-1 and two alleles code for Moco-sulfurase, which activates the aldehyde oxidases required for the biosynthesis of the plant hormones abscisic acid (ABA) and indole-acetic acid (IAA) and controls purine nucleotide (ATP and GTP) turnover and nitrogen recycling via xanthine dehydrogenase. These enzyme activities were not detected in aci2-1. ABA, IAA and/or purine turnover may play previously unrecognized roles in the regulation of chloroplast protein import in response to developmental, metabolic and environmental cues.
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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/Abscisic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Indoleacetic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Growth Regulators,
http://linkedlifedata.com/resource/pubmed/chemical/Purines,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ribulose-Bisphosphate Carboxylase,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfurtransferases,
http://linkedlifedata.com/resource/pubmed/chemical/indoleacetic acid
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1365-313X
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
63
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
44-59
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pubmed:meshHeading |
pubmed-meshheading:20374530-Abscisic Acid,
pubmed-meshheading:20374530-Arabidopsis,
pubmed-meshheading:20374530-Arabidopsis Proteins,
pubmed-meshheading:20374530-Chloroplasts,
pubmed-meshheading:20374530-Gene Expression Regulation, Plant,
pubmed-meshheading:20374530-Genes, Reporter,
pubmed-meshheading:20374530-Indoleacetic Acids,
pubmed-meshheading:20374530-Mutation,
pubmed-meshheading:20374530-Plant Growth Regulators,
pubmed-meshheading:20374530-Plants, Genetically Modified,
pubmed-meshheading:20374530-Protein Transport,
pubmed-meshheading:20374530-Purines,
pubmed-meshheading:20374530-Recombinant Fusion Proteins,
pubmed-meshheading:20374530-Ribulose-Bisphosphate Carboxylase,
pubmed-meshheading:20374530-Sulfurtransferases,
pubmed-meshheading:20374530-Transgenes
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pubmed:year |
2010
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pubmed:articleTitle |
A forward genetic screen to explore chloroplast protein import in vivo identifies Moco sulfurase, pivotal for ABA and IAA biosynthesis and purine turnover.
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pubmed:affiliation |
Department of Molecular Genetics and Cell Biology, The University of Chicago, 920 East 58th Street, Chicago, IL 60637, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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