| pubmed-article:2170106 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2170106 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
| pubmed-article:2170106 | lifeskim:mentions | umls-concept:C0025252 | lld:lifeskim |
| pubmed-article:2170106 | lifeskim:mentions | umls-concept:C0026237 | lld:lifeskim |
| pubmed-article:2170106 | lifeskim:mentions | umls-concept:C1167331 | lld:lifeskim |
| pubmed-article:2170106 | lifeskim:mentions | umls-concept:C1326471 | lld:lifeskim |
| pubmed-article:2170106 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:2170106 | pubmed:dateCreated | 1990-11-15 | lld:pubmed |
| pubmed-article:2170106 | pubmed:abstractText | The yeast mitochondrial outer membrane contains a major 70 kd protein with an amino-terminal hydrophobic membrane anchor and a hydrophilic 60 kd domain exposed to the cytosol. We now show that this protein (which we term MAS70) accelerates the mitochondrial import of many (but not all) precursor proteins. Anti-MAS70 IgGs or removal of MAS70 from the mitochondria by either mild trypsin treatment or by disrupting the nuclear MAS70 gene inhibits import of the F1-ATPase beta-subunit, the ADP/ATP translocator, and of several other precursors into isolated mitochondria by up to 75%, but has little effect on the import of porin. Intact cells of a mas70 null mutant import the F1-ATPase alpha-subunit and beta-subunits, cytochrome c1 and other precursors at least several fold more slowly than wild-type cells. Removal of MAS70 from wild-type mitochondria inhibits binding of the ADP/ATP translocator to the mitochondrial surface, indicating that MAS70 mediates one of the earliest import steps. Several precursors are thus imported by a pathway in which MAS70 functions as a receptor-like component. MAS70 is not essential for import of these precursors, but only accelerates this process. | lld:pubmed |
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| pubmed-article:2170106 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2170106 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2170106 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2170106 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2170106 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:2170106 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:2170106 | pubmed:author | pubmed-author:SchatzGG | lld:pubmed |
| pubmed-article:2170106 | pubmed:author | pubmed-author:HorstmannHH | lld:pubmed |
| pubmed-article:2170106 | pubmed:author | pubmed-author:BrandtAA | lld:pubmed |
| pubmed-article:2170106 | pubmed:author | pubmed-author:GriffithsGG | lld:pubmed |
| pubmed-article:2170106 | pubmed:author | pubmed-author:HinesVV | lld:pubmed |
| pubmed-article:2170106 | pubmed:author | pubmed-author:BrütschHH | lld:pubmed |
| pubmed-article:2170106 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2170106 | pubmed:volume | 9 | lld:pubmed |
| pubmed-article:2170106 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2170106 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2170106 | pubmed:pagination | 3191-200 | lld:pubmed |
| pubmed-article:2170106 | pubmed:dateRevised | 2010-9-10 | lld:pubmed |
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| pubmed-article:2170106 | pubmed:meshHeading | pubmed-meshheading:2170106-... | lld:pubmed |
| pubmed-article:2170106 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2170106 | pubmed:articleTitle | Protein import into yeast mitochondria is accelerated by the outer membrane protein MAS70. | lld:pubmed |
| pubmed-article:2170106 | pubmed:affiliation | Biocenter, University of Basel, Switzerland. | lld:pubmed |
| pubmed-article:2170106 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2170106 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2170106 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:2170106 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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