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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1992-4-7
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pubmed:abstractText |
In this study, we have investigated the protein/lipid interactions of two mitochondrial precursor proteins, apocytochrome c and pCOX IV-DHFR, which exhibit mitochondrial import pathways with different characteristics. In-vitro-synthesized apocytochrome c was found to bind efficiently and specifically to liposomes composed of negatively charged phospholipids and showed a (at least partial) translocation across a lipid bilayer, as reported previously for the chemically prepared precursor protein [Rietveld, A. & de Kruijff, B. (1984) J. Biol. Chem. 259, 6704-6707; Dumont, M. E. & Richards, F. M. (1984) J. Biol. Chem. 259, 4147-4156]. Negatively charged liposomes were shown to efficiently compete with mitochondria for import of in-vitro-synthesized apocytochrome c into the organelle, suggesting an important role for negatively charged phospholipids in the initial binding of apocytochrome c to mitochondria. In contrast, the purified and in-vitro-synthesized precursor fusion protein pCOX IV-DHFR, consisting of the presequence of yeast cytochrome oxidase subunit IV fused to mouse dihydrofolate reductase was unable to translocate across a pure lipid bilayer. The data indicate that the ability of apocytochrome c to spontaneously translocate across the bilayer is not shared by all mitochondrial precursor proteins. The implications of the special protein/lipid interaction of apocytochrome c for import into mitochondria will be discussed.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Apoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome c Group,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochromes c,
http://linkedlifedata.com/resource/pubmed/chemical/Lipid Bilayers,
http://linkedlifedata.com/resource/pubmed/chemical/Liposomes
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
204
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
841-6
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:1311682-Animals,
pubmed-meshheading:1311682-Apoproteins,
pubmed-meshheading:1311682-Autoradiography,
pubmed-meshheading:1311682-Binding Sites,
pubmed-meshheading:1311682-Biological Transport,
pubmed-meshheading:1311682-Cytochrome c Group,
pubmed-meshheading:1311682-Cytochromes c,
pubmed-meshheading:1311682-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1311682-Lipid Bilayers,
pubmed-meshheading:1311682-Liposomes,
pubmed-meshheading:1311682-Mitochondria, Heart,
pubmed-meshheading:1311682-Neurospora crassa,
pubmed-meshheading:1311682-Protein Biosynthesis,
pubmed-meshheading:1311682-Transcription, Genetic
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pubmed:year |
1992
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pubmed:articleTitle |
Bilayer-penetrating properties enable apocytochrome c to follow a special import pathway into mitochondria.
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pubmed:affiliation |
Centre for Biomembranes and Lipid Enzymology, Department of Biochemistry of Membranes, University of Utrecht, The Netherlands.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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