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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
1990-11-15
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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.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-16453466,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-16453467,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-2166740,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-2404612,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-2406905,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-2557158,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-2645524,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-2674724,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-2684653,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-2834388,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-2842866,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-2884042,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-2905264,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-2967109,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-3016548,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-3034898,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-3056099,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-3058716,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-30693,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-3282178,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-3308450,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-6091052,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-6098467,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-6215406,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-6228704,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-6235522,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-6290489,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-6321150,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-6365533,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-6396085,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-6526014,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-6544882,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2170106-6656640
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3191-200
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pubmed:dateRevised |
2010-9-10
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pubmed:meshHeading |
pubmed-meshheading:2170106-Cytochromes c1,
pubmed-meshheading:2170106-Fungal Proteins,
pubmed-meshheading:2170106-Immunoglobulin G,
pubmed-meshheading:2170106-Kinetics,
pubmed-meshheading:2170106-Membrane Proteins,
pubmed-meshheading:2170106-Microscopy, Immunoelectron,
pubmed-meshheading:2170106-Mitochondria,
pubmed-meshheading:2170106-Mitochondrial Membrane Transport Proteins,
pubmed-meshheading:2170106-Models, Biological,
pubmed-meshheading:2170106-Proton-Translocating ATPases,
pubmed-meshheading:2170106-Saccharomyces cerevisiae,
pubmed-meshheading:2170106-Saccharomyces cerevisiae Proteins
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pubmed:year |
1990
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pubmed:articleTitle |
Protein import into yeast mitochondria is accelerated by the outer membrane protein MAS70.
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pubmed:affiliation |
Biocenter, University of Basel, Switzerland.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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