Aug 1, 1989

Probing the structure of the mitochondrial channel, VDAC, by site-directed mutagenesis: a progress report

Journal of Bioenergetics and Biomembranes
E Blachly-DysonM Forte

Abstract

The voltage-dependent anion-selective channel (VDAC) of the mitochondrial outer membrane is formed by a small (approximately 30 kDa) polypeptide, but shares with more complex channels the properties of voltage-dependent gating and ion selectivity. Thus, it is a useful model for studying these properties. The molecular biology techniques available in yeast allow us to construct mutant versions of the cloned yeast VDAC gene in vitro, using oligonucleotide-directed mutagenesis, and to express the mutant genes in yeast cells in the absence of wild-type VDAC. We find that one substitution mutation (lys 61 to glu) alters the selectivity of VDAC.

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Citations

Mentioned in this Paper

Neurospora crassa
Oligonucleotide-Directed Mutagenesis
Exploration With a Probe
Mutagenesis, Site-Directed
Ion Channel
Mitochondria
Voltage-Dependent Anion Channels
Pore Proteins
Mutant
Molecular Biology

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