Selectivity changes in site-directed mutants of the VDAC ion channel: Structural implications

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

Research output: Contribution to journalArticlepeer-review

113 Scopus citations


The gene encoding the yeast mitochondrial outer membrane channel VDAC was subjected to site-directed mutagenesis to change amino acids at 29 positions to residues differing in charge from the wild-type sequence. The mutant genes were then expressed in yeast, and the physiological consequences of single and multiple amino acid changes were assessed after isolation and insertion of mutant channels into phospholipid bilayers. Selectivity changes were observed at 14 sites distributed throughout the length of the molecule. These sites are likely to define the position of the protein walls lining the aqueous pore and hence, the transmembrane segments. These results have been used to develop a model of the open state of the channel in which each polypeptide contributes 12 β strands and one a helix to form the aqueous transmembrane pathway.

Original languageEnglish (US)
Pages (from-to)1233-1236
Number of pages4
Issue number4947
StatePublished - 1990
Externally publishedYes

ASJC Scopus subject areas

  • General


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