Source:http://linkedlifedata.com/resource/pubmed/id/12354789
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
21
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pubmed:dateCreated |
2002-9-30
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pubmed:abstractText |
Friedreich's ataxia is caused by a deficit in frataxin, a small mitochondrial protein of unknown function that has been conserved during evolution. Previous studies have pointed out a role for frataxin in mitochondrial iron-sulfur (Fe-S) metabolism. Here, we have analyzed the incorporation of Fe-S clusters into yeast ferredoxin imported into isolated energized mitochondria from cells grown in the presence of glycerol, an obligatory respiratory carbon source. Similar amounts of apo-ferredoxin precursor were imported into mitochondria and processed in wild-type and yfh1-deleted (delta YF111) strains. However, the incorporation of Fe-S clusters into apo-ferredoxin was significantly reduced in delta YFH1 mitochondria. The newly assembled ferredoxin was stable, excluding the possibility that the decreased incorporation was a result of increased oxidative damage. When delta YFH1 cells were grown in raffinose medium, the formation of holo-ferredoxin was low, as a consequence of the decrease in ferredoxin precursor import into mitochondria. However, the decrease in the conversion rate of apo- into holo-ferredoxin was in the same range as for glycerol-grown cells, indicating that the extent of the defect in Fe-S protein assembly is similar under different physiological conditions. These data show that frataxin is not essential for Fe-S protein assembly, but improves the efficiency of the process. The large variations observed in the activity of Fe-S cluster proteins under different physiological conditions result from secondary defects in the physiology of delta YFH1 cells.
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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/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Iron-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Iron-Sulfur Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfur Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/frataxin
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0964-6906
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2635-43
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12354789-Cysteine,
pubmed-meshheading:12354789-Iron-Binding Proteins,
pubmed-meshheading:12354789-Iron-Sulfur Proteins,
pubmed-meshheading:12354789-Mitochondria,
pubmed-meshheading:12354789-Protein Transport,
pubmed-meshheading:12354789-Saccharomyces cerevisiae,
pubmed-meshheading:12354789-Sulfur Radioisotopes
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pubmed:year |
2002
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pubmed:articleTitle |
A non-essential function for yeast frataxin in iron-sulfur cluster assembly.
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pubmed:affiliation |
Unité de Biochimie Physiologique, Université Catholique de Louvain, Croix du Sud 2-20, B-1348 Louvain-la-Neuve, Belgium.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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