| pubmed-article:11060020 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11060020 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:11060020 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:11060020 | lifeskim:mentions | umls-concept:C1383501 | lld:lifeskim |
| pubmed-article:11060020 | lifeskim:mentions | umls-concept:C0026237 | lld:lifeskim |
| pubmed-article:11060020 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
| pubmed-article:11060020 | lifeskim:mentions | umls-concept:C1158193 | lld:lifeskim |
| pubmed-article:11060020 | pubmed:issue | 21 | lld:pubmed |
| pubmed-article:11060020 | pubmed:dateCreated | 2000-11-29 | lld:pubmed |
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| pubmed-article:11060020 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11060020 | pubmed:abstractText | Iron-sulfur (Fe-S) clusters are cofactors found in many proteins that have important redox, catalytic or regulatory functions. In mammalian cells, almost all known Fe-S proteins are found in the mitochondria, but at least one is found in the cytosol. Here we report cloning of the human homologs to IscU and NifU, iron-binding proteins that play a critical role in Fe-S cluster assembly in bacteria. In human cells, alternative splicing of a common pre-mRNA results in synthesis of two proteins that differ at the N-terminus and localize either to the cytosol (IscU1) or to the mitochondria (IscU2). Biochemical analyses demonstrate that IscU proteins specifically associate with IscS, a cysteine desulfurase that is proposed to sequester inorganic sulfur for Fe-S cluster assembly. Protein complexes containing IscU and IscS can be found in the mitochondria as well as in the cytosol, implying that Fe-S cluster assembly takes place in multiple subcellular compartments in mammalian cells. The possible roles of the IscU proteins in mammalian cells and the potential implications of compartmentalization of Fe-S cluster assembly are discussed. | lld:pubmed |
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| pubmed-article:11060020 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11060020 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11060020 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11060020 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:11060020 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:11060020 | pubmed:author | pubmed-author:RouaultTT | lld:pubmed |
| pubmed-article:11060020 | pubmed:author | pubmed-author:TongW HWH | lld:pubmed |
| pubmed-article:11060020 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11060020 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:11060020 | pubmed:volume | 19 | lld:pubmed |
| pubmed-article:11060020 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11060020 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11060020 | pubmed:pagination | 5692-700 | lld:pubmed |
| pubmed-article:11060020 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:11060020 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:11060020 | pubmed:articleTitle | Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells. | lld:pubmed |
| pubmed-article:11060020 | pubmed:affiliation | National Institute of Child Health and Human Development, Cell Biology and Metabolism Branch, Bethesda, MD 20892, USA. trou@helix.nih.gov | lld:pubmed |
| pubmed-article:11060020 | pubmed:publicationType | Journal Article | lld:pubmed |
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