title: Probing the structure of the mitochondrial channel, VDAC, by site-directed mutagenesis: a progress report.
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.
authors: Vollum Institute for Advanced Biomedical Research, Oregon Health Sciences University, Portland 97201.
authors: E
authors: E
authors: Blachly-Dyson
authors: S Z
authors: SZ
authors: Peng
authors: M
authors: M
authors: Colombini
authors: M
authors: M
authors: Forte
mesh_terms: D000595:Amino Acid Sequence; D007473:Ion Channels / Q000378:metabolism / Q000648:ultrastructure; D008565:Membrane Proteins / Q000235:genetics* / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism / Q000648:ultrastructure; D008969:Molecular Sequence Data; D009154:Mutation; D009492:Neurospora crassa / Q000235:genetics; D018272:Porins; D012441:Saccharomyces cerevisiae / Q000235:genetics; D050994:Voltage-Dependent Anion Channels
chemical_list: D007473:Ion Channels; D008565:Membrane Proteins; D018272:Porins; D050994:Voltage-Dependent Anion Channels