A novel property of a mitochondrial presequence. Its ability to induce cardiolipin-specific interbilayer contacts which are dissociated by a transmembrane potential.
A new property of the presequence of the mitochondrial precursor protein cytochrome oxidase subunit IV is presented. This mitochondrial presequence induces interbilayer contacts between large unilamellar vesicles consisting of phosphatidylcholine and cardiolipin. The presequence-vesicle aggregates can be dissociated by applying a membrane potential across the bilayers (negative inside). These effects require the presence of cardiolipin and are not observed for other negatively charged phospholipids. We propose a role for the presequence in the formation and dissociation of mitochondrial contact sites.
Department of Biochemistry of Membranes, University of Utrecht, The Netherlands.
J M
JM
Leenhouts
J
J
de Gier
B
B
de Kruijff
D000595:Amino Acid Sequence; D000818:Animals; D002308:Cardiolipins / Q000378:metabolism*; D003576:Electron Transport Complex IV / Q000378:metabolism*; D007425:Intracellular Membranes / Q000378:metabolism*; D008564:Membrane Potentials; D008863:Microspheres; D008928:Mitochondria / Q000201:enzymology*; D008969:Molecular Sequence Data; D010713:Phosphatidylcholines / Q000378:metabolism*; D011498:Protein Precursors / Q000378:metabolism*; D021382:Protein Sorting Signals / Q000378:metabolism*
D002308:Cardiolipins; D010713:Phosphatidylcholines; D011498:Protein Precursors; D021382:Protein Sorting Signals; D003576:Electron Transport Complex IV