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

Songzhi Peng, Elizabeth Blachly-Dyson, Marco Colombini, Michael Forte

Research output: Contribution to journalArticle

41 Scopus citations

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 107. These findings favor the hypothesis that each functional VDAC channel is composed of a single 30-kDa polypeptide chain.

Original languageEnglish (US)
Pages (from-to)27-31
Number of pages5
JournalJournal of Bioenergetics and Biomembranes
Volume24
Issue number1
DOIs
StatePublished - Feb 1 1992

Keywords

  • Mitochondrion
  • hybrid
  • outer membrane
  • site-directed mutations
  • voltage-gated channel
  • yeast

ASJC Scopus subject areas

  • Physiology
  • Cell Biology

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