| pubmed-article:1281544 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1281544 | lifeskim:mentions | umls-concept:C0596286 | lld:lifeskim |
| pubmed-article:1281544 | lifeskim:mentions | umls-concept:C1274040 | lld:lifeskim |
| pubmed-article:1281544 | lifeskim:mentions | umls-concept:C1148846 | lld:lifeskim |
| pubmed-article:1281544 | lifeskim:mentions | umls-concept:C1704332 | lld:lifeskim |
| pubmed-article:1281544 | lifeskim:mentions | umls-concept:C1880352 | lld:lifeskim |
| pubmed-article:1281544 | lifeskim:mentions | umls-concept:C1707798 | lld:lifeskim |
| pubmed-article:1281544 | lifeskim:mentions | umls-concept:C0123921 | lld:lifeskim |
| pubmed-article:1281544 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:1281544 | pubmed:dateCreated | 1993-1-19 | lld:pubmed |
| pubmed-article:1281544 | pubmed:abstractText | The translation of ferritin mRNA and degradation of transferrin receptor mRNA are regulated by the interaction of an RNA-binding protein, the iron-responsive element binding protein (IRE-BP), with RNA stem-loop structures known as iron-responsive elements (IREs) contained within these transcripts. IRE-BP produced in iron-replete cells has aconitase (EC 4.2.1.3) activity. The protein shows extensive sequence homology with mitochondrial aconitase, and sequences of peptides prepared from cytosolic aconitase are identical with peptides of IRE-BP. As an active aconitase, IRE-BP is expected to have an Fe-S cluster, in analogy to other aconitases. This Fe-S cluster has been implicated as the region of the protein that senses intracellular iron levels and accordingly modifies the ability of the IRE-BP to interact with IREs. Expression of the IRE-BP in cultured cells has revealed that the IRE-BP functions either as an active aconitase, when the cells are iron-replete, or as an active RNA-binding protein, when the cells are iron-depleted. We compare properties of purified authentic cytosolic aconitase from beef liver with those of IRE-BP from tissue culture cells and establish that characteristics of the physiologically relevant form of the protein from iron-depleted cells resemble those of cytosolic aconitase apoprotein. We demonstrate that loss of the labile fourth iron atom of the Fe-S cluster results in loss of aconitase activity, but that more extensive cluster alteration is required before the IRE-BP acquires the capacity to bind RNA with the affinity seen in vivo. These results are consistent with a model in which the cubane Fe-S cluster is disassembled when intracellular iron is depleted. | lld:pubmed |
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| pubmed-article:1281544 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1281544 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1281544 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1281544 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1281544 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:1281544 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:1281544 | pubmed:author | pubmed-author:BeinertHH | lld:pubmed |
| pubmed-article:1281544 | pubmed:author | pubmed-author:HarfordJ BJB | lld:pubmed |
| pubmed-article:1281544 | pubmed:author | pubmed-author:KlausnerR DRD | lld:pubmed |
| pubmed-article:1281544 | pubmed:author | pubmed-author:BlondinG AGA | lld:pubmed |
| pubmed-article:1281544 | pubmed:author | pubmed-author:KennedyM CMC | lld:pubmed |
| pubmed-article:1281544 | pubmed:author | pubmed-author:RouaultT ATA | lld:pubmed |
| pubmed-article:1281544 | pubmed:author | pubmed-author:HaileD JDJ | lld:pubmed |
| pubmed-article:1281544 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1281544 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:1281544 | pubmed:volume | 89 | lld:pubmed |
| pubmed-article:1281544 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1281544 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1281544 | pubmed:pagination | 11735-9 | lld:pubmed |
| pubmed-article:1281544 | pubmed:dateRevised | 2010-9-7 | lld:pubmed |
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| pubmed-article:1281544 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1281544 | pubmed:articleTitle | Cellular regulation of the iron-responsive element binding protein: disassembly of the cubane iron-sulfur cluster results in high-affinity RNA binding. | lld:pubmed |
| pubmed-article:1281544 | pubmed:affiliation | Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892. | lld:pubmed |
| pubmed-article:1281544 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1281544 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:1281544 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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