Jan 1, 1987

Purification and characterization of the voltage-dependent anion channel from the outer mitochondrial membrane of yeast

The Journal of Membrane Biology
M ForteM Colombini

Abstract

The outer mitochondrial membranes of all organisms so far examined contain a protein which forms voltage-dependent anion selective channels (VDAC) when incorporated into planar phospholipid membranes. Previous reports have suggested that the yeast (Saccharomyces cerevisiae) outer mitochondrial membrane component responsible for channel formation is a protein of 29,000 daltons which is also the major component of this membrane. In this report, we describe the purification of this 29,000-dalton protein to virtual homogeneity from yeast outer mitochondrial membranes. The purified protein readily incorporates into planar phospholipid membranes to produce ionic channels. Electrophysiological characterization of these channels has demonstrated they have a size, selectivity and voltage dependence similar to VDAC from other organisms. Biochemically, the purified protein has been characterized by determining its amino acid composition and isoelectric point (pI). In addition, we have shown that the purified protein, when reconstituted into liposomes, can bind hexokinase in a glucose-6-phosphate dependent manner, as has been shown for VDAC purified from other sources. Since physiological characterization suggests that the functional param...Continue Reading

Mentioned in this Paper

Neurospora
Tissue Membrane
Tobacco
Saccharomyces cerevisiae allergenic extract
Resting Potentials
Drosophila
Nicotiana
Hexokinase
Chloroplasts
Ion Channel

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