| pubmed-article:15153070 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15153070 | lifeskim:mentions | umls-concept:C0699788 | lld:lifeskim |
| pubmed-article:15153070 | lifeskim:mentions | umls-concept:C0026336 | lld:lifeskim |
| pubmed-article:15153070 | lifeskim:mentions | umls-concept:C0026237 | lld:lifeskim |
| pubmed-article:15153070 | lifeskim:mentions | umls-concept:C0018873 | lld:lifeskim |
| pubmed-article:15153070 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:15153070 | lifeskim:mentions | umls-concept:C1515655 | lld:lifeskim |
| pubmed-article:15153070 | pubmed:issue | Pt 1 | lld:pubmed |
| pubmed-article:15153070 | pubmed:dateCreated | 2004-8-6 | lld:pubmed |
| pubmed-article:15153070 | pubmed:abstractText | The dual signal approach, i.e. a mitochondrial signal at the N-terminus and an ER (endoplasmic reticulum) or a peroxisomal signal at the C-terminus of EGFP (enhanced green fluorescent protein), was employed in transfected HeLa cells to test for a co-translational import model. The signal peptide from OTC (ornithine transcarbamylase) or arginase II was fused to the N-terminus of EGFP, and an ER or peroxisomal signal was fused to its C-terminus. The rationale was that if the free preprotein remained in the cytosol, it could be distributed between the two organelles by using a post-translational pathway. The resulting fusion proteins were imported exclusively into mitochondria, suggesting that co-translational import occurred. Native preALDH (precursor of rat liver mitochondrial aldehyde dehydrogenase), preOTC and rhodanese, each with the addition of a C-terminal ER or peroxisomal signal, were also translocated only to the mitochondria, again showing that a co-translational import pathway exists for these native proteins. Import of preALDH(sp)-DHFR, a fusion protein consisting of the leader sequence (signal peptide) of preALDH fused to DHFR (dihydrofolate reductase), was studied in the presence of methotrexate, a substrate analogue for DHFR. It was found that 70% of the preALDH(sp)-DHFR was imported into mitochondria in the presence of methotrexate, implying that 70% of the protein utilized the co-translational import pathway and 30% used the post-translational import pathway. Thus it appears that co-translational import is a major pathway for mitochondrial protein import. A model is proposed to explain how competition between binding factors could influence whether or not a cytosolic carrier protein, such as DHFR, uses the co- or post-translational import pathway. | lld:pubmed |
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| pubmed-article:15153070 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15153070 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15153070 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15153070 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15153070 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15153070 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:15153070 | pubmed:issn | 1470-8728 | lld:pubmed |
| pubmed-article:15153070 | pubmed:author | pubmed-author:LEEO SOSJr | lld:pubmed |
| pubmed-article:15153070 | pubmed:author | pubmed-author:MukhopadhyayA... | lld:pubmed |
| pubmed-article:15153070 | pubmed:author | pubmed-author:WeinerHenryH | lld:pubmed |
| pubmed-article:15153070 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:15153070 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:15153070 | pubmed:volume | 382 | lld:pubmed |
| pubmed-article:15153070 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15153070 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15153070 | pubmed:pagination | 385-92 | lld:pubmed |
| pubmed-article:15153070 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:15153070 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15153070 | pubmed:articleTitle | A co-translational model to explain the in vivo import of proteins into HeLa cell mitochondria. | lld:pubmed |
| pubmed-article:15153070 | pubmed:affiliation | Department of Biochemistry, Purdue University, 175 S. University Street, West Lafayette, IN 47907-2063, USA. | lld:pubmed |
| pubmed-article:15153070 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15153070 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
