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

Elizabeth Blachly-Dyson, Song Zhi Peng, Marco Colombini, Michael Forte

Research output: Contribution to journalArticle

36 Scopus citations

Abstract

The voltage-dependent anion-selective channel (VDAC) of the mitochondrial outer membrane is formed by a small (∼ 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.

Original languageEnglish (US)
Pages (from-to)471-483
Number of pages13
JournalJournal of Bioenergetics and Biomembranes
Volume21
Issue number4
DOIs
StatePublished - Aug 1 1989

Keywords

  • Yeast VDAC
  • anion channel
  • ion channel
  • ion selectivity
  • mitochondrial outer membrane
  • oligonucleotide-directed mutagenesis
  • voltage gating

ASJC Scopus subject areas

  • Physiology
  • Cell Biology

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