A 28 kDa mitochondrial protein is radiolabelled by crosslinking with a 125I-labelled presequence.
A 13-residue peptide containing the first 12 amino acids of the N-terminal part of the signal sequence of yeast cytochrome c oxidase subunit IV is shown by chemical crosslinking to interact with a mitochondrial protein. This result is obtained with mitochondria from four different origins. Submitochondrial localization experiments suggest that the 28 kDa labelled component is present on the outer face of the inner membrane. Since such addressing peptides are imported into mitochondria through the same machinery as protein precursors, the 28 kDa protein might be a component of the translocation apparatus.
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Laboratoire de Biologie et de Technologie des Membranes du CNRS, Villeurbanne, France.
Goldschmidt
D
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Chich
J F
JF
Thieffry
M
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Henry
J P
JP
Gautheron
D C
DC
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003432:Cross-Linking Reagents; D004591:Electrophoresis, Polyacrylamide Gel; D007457:Iodine Radioisotopes; D008928:Mitochondria / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D021382:Protein Sorting Signals / Q000378:metabolism; D011817:Rabbits; D051381:Rats; D013367:Submitochondrial Particles / Q000378:metabolism; D014357:Trypsin
D003432:Cross-Linking Reagents; D007457:Iodine Radioisotopes; D021382:Protein Sorting Signals; D014357:Trypsin