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

doi:10.1007/BF00762519

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 journal › Article › peer-review

39 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 language	English (US)
Pages (from-to)	471-483
Number of pages	13
Journal	Journal of Bioenergetics and Biomembranes
Volume	21
Issue number	4
DOIs	https://doi.org/10.1007/BF00762519
State	Published - Aug 1989
Externally published	Yes

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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10.1007/BF00762519

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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.",

keywords = "Yeast VDAC, anion channel, ion channel, ion selectivity, mitochondrial outer membrane, oligonucleotide-directed mutagenesis, voltage gating",

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year = "1989",

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T1 - Probing the structure of the mitochondrial channel, VDAC, by site-directed mutagenesis

T2 - A progress report

AU - Blachly-Dyson, Elizabeth

AU - Peng, Song Zhi

AU - Colombini, Marco

AU - Forte, Michael

PY - 1989/8

Y1 - 1989/8

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AB - 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.

KW - Yeast VDAC

KW - anion channel

KW - ion channel

KW - ion selectivity

KW - mitochondrial outer membrane

KW - oligonucleotide-directed mutagenesis

KW - voltage gating

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

Abstract

Keywords

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