pubmed-article:9250670 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9250670 | lifeskim:mentions | umls-concept:C0699788 | lld:lifeskim |
pubmed-article:9250670 | lifeskim:mentions | umls-concept:C0521449 | lld:lifeskim |
pubmed-article:9250670 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
pubmed-article:9250670 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:9250670 | lifeskim:mentions | umls-concept:C1511625 | lld:lifeskim |
pubmed-article:9250670 | lifeskim:mentions | umls-concept:C0521451 | lld:lifeskim |
pubmed-article:9250670 | lifeskim:mentions | umls-concept:C0243041 | lld:lifeskim |
pubmed-article:9250670 | lifeskim:mentions | umls-concept:C1427202 | lld:lifeskim |
pubmed-article:9250670 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:9250670 | lifeskim:mentions | umls-concept:C1709634 | lld:lifeskim |
pubmed-article:9250670 | pubmed:issue | 14 | lld:pubmed |
pubmed-article:9250670 | pubmed:dateCreated | 1997-9-2 | lld:pubmed |
pubmed-article:9250670 | pubmed:abstractText | We have reconstituted the early steps of precursor targeting to mitochondria in a defined and soluble system consisting of the cytosolic domains of the yeast mitochondrial import receptors Tom20 and Tom70, precursor to bovine adrenal adrenodoxin (which has a cleavable targeting signal) and rat liver cytosolic chaperones hsp70 and mitochondrial import-stimulating factor (MSF). The Tom70 domain only bound the precursor in the presence of MSF, yielding a precursor-MSF-Tom70 complex; ATP hydrolysis by MSF released MSF and generated a precursor-Tom70 complex whose formation was inhibited by an excess of a functional presequence peptide, but not by 150 mM NaCl. In the presence of the Tom20 domain, ATP caused transfer of the precursor from the precursor-MSF-Tom70 complex to Tom20. The Tom20 domain alone only bound the precursor in the presence of hsp70; hsp70 itself was not incorporated into the resulting complex. Formation of the Tom20-precursor complex was inhibited by excess presequence peptide or by 150 mM NaCl. Similar results were obtained with the ADP/ATP carrier and porin precursors, which both lack a cleaved targeting signal. Correct targeting of a precursor to mitochondrial import receptors thus requires cytosolic chaperones, irrespective of the presence or absence of a cleavable presequence. | lld:pubmed |
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pubmed-article:9250670 | pubmed:language | eng | lld:pubmed |
pubmed-article:9250670 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9250670 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9250670 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:9250670 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9250670 | pubmed:month | Jul | lld:pubmed |
pubmed-article:9250670 | pubmed:issn | 0261-4189 | lld:pubmed |
pubmed-article:9250670 | pubmed:author | pubmed-author:MiharaKK | lld:pubmed |
pubmed-article:9250670 | pubmed:author | pubmed-author:SchatzGG | lld:pubmed |
pubmed-article:9250670 | pubmed:author | pubmed-author:KomiyaTT | lld:pubmed |
pubmed-article:9250670 | pubmed:author | pubmed-author:RospertSS | lld:pubmed |
pubmed-article:9250670 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9250670 | pubmed:day | 16 | lld:pubmed |
pubmed-article:9250670 | pubmed:volume | 16 | lld:pubmed |
pubmed-article:9250670 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9250670 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9250670 | pubmed:pagination | 4267-75 | lld:pubmed |
pubmed-article:9250670 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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pubmed-article:9250670 | pubmed:year | 1997 | lld:pubmed |