Feb 1, 1992

Determination of the number of polypeptide subunits in a functional VDAC channel from Saccharomyces cerevisiae

Journal of Bioenergetics and Biomembranes
S PengM Forte

Abstract

Genes encoding VDAC proteins containing specific site-directed amino acid alterations were introduced into wild-type Saccharomyces cerevisiae. The mutant VDAC proteins form channels with ion selectivities very different from that of the wild-type channel. Therefore, the resulting yeast strains express two different genes capable of coding for functional, yet distinct, VDAC channels. If VDAC were an oligomeric channel, analysis of VDAC from these strains should have revealed not only the presence of channels with wild-type or mutant selectivity but also channels with intermediate selectivities. While channels with wild-type and mutant selectivities were observed with approximately equal frequency, no channels with intermediate selectivity were observed. Sufficient observations were performed with two different mutant genes K61E.K65E and K19E.K61E) that the likelihood of having missed hybrid channels was less than 1 in 10(7). These findings favor the hypothesis that each functional VDAC channel is composed of a single 30-kDa polypeptide chain.

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  • Citations19

Citations

Mentioned in this Paper

Saccharomyces cerevisiae allergenic extract
Resting Potentials
Ion Channel
Mitochondria
Voltage-Dependent Anion Channels
Pore Proteins
Mutant
Yeast Proteins
Cell Surface Proteins
Saccharomyces cerevisiae

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