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The voltage-dependent anion-selective channel (VDAC) in
mitochondrial outer membranes is formed by a polypeptide (M
Volume 270,
Number 28,
Issue of July 14, pp. 16694-16700, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
31,000) coded by a nuclear gene whose cDNA
sequence is known for several organisms. Antibodies have been raised
against synthetic peptides corresponding to four different regions in
the predicted sequence of the VDAC polypeptide of the fungus Neurospora crassa (residues 1-20, amino terminus;
195-210, 251-268, and 272-283, carboxyl terminus).
Specificity of the antibodies has been characterized in terms of
binding to peptides or fungal mitochondria on microtiter plates and
binding to mitochondrial proteins of several species in Western blots.
Reactivity of three of the four antibodies with fungal mitochondria in
suspension increases with lysis of outer membranes, indicating that the
respective epitopes (including those near the amino and carboxyl
termini) are exposed on the surface of the outer membrane that faces
inside the mitochondrion. Preincubation of mitochondria with a
polyanion that modulates VDAC voltage dependence strongly inhibits
binding of the antibody against residues 251-268, whose epitopes
are on the outer mitochondrial surface.
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