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Journal of Bioenergetics and Biomembranes

, Volume 21, Issue 4, pp 471–483 | Cite as

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 Articles: Mitochondrial Membrane Channels

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 genein 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.

Key Words

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

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Copyright information

© Plenum Publishing Corporation 1989

Authors and Affiliations

  • Elizabeth Blachly-Dyson
    • 1
  • Song Zhi Peng
    • 2
  • Marco Colombini
    • 2
  • Michael Forte
    • 1
  1. 1.Vollum Institute for Advanced Biomedical ResearchOregon Health Sciences UniversityPortland
  2. 2.Department of ZoologyUniversity of MarylandCollege Park

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