Molecular genetics of the VDAC ion channel: Structural model and sequence analysis

Michael Forte; H. Robert Guy; Carmen A. Mannella

doi:10.1007/BF00768537

Molecular genetics of the VDAC ion channel: Structural model and sequence analysis

Michael Forte, H. Robert Guy, Carmen A. Mannella

Vollum Institute

Research output: Contribution to journal › Article › peer-review

96 Scopus citations

Abstract

The voltage-dependent anion-selective channel of the outer mitochondrial membrane provides a unique system in which to study the molecular basis of voltage gating of ion flow. We have cloned and sequenced a cDNA coding for this protein in yeast. From the derived amino acid sequence, we have generated a preliminary model for the secondary structure of the protein which suggests that the protein forms a "β-barrel" type structure. Comparison of the VDAC amino acid sequence with that of the bacterial porins has indicated that the two classes of molecules appear to be unrelated.

Original language	English (US)
Pages (from-to)	341-350
Number of pages	10
Journal	Journal of Bioenergetics and Biomembranes
Volume	19
Issue number	4
DOIs	https://doi.org/10.1007/BF00768537
State	Published - Aug 1 1987

Keywords

Yeast VDAC
bacterial porins
gene cloning
secondary structure
sequence homology

ASJC Scopus subject areas

Physiology
Cell Biology

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10.1007/BF00768537

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N2 - The voltage-dependent anion-selective channel of the outer mitochondrial membrane provides a unique system in which to study the molecular basis of voltage gating of ion flow. We have cloned and sequenced a cDNA coding for this protein in yeast. From the derived amino acid sequence, we have generated a preliminary model for the secondary structure of the protein which suggests that the protein forms a "β-barrel" type structure. Comparison of the VDAC amino acid sequence with that of the bacterial porins has indicated that the two classes of molecules appear to be unrelated.

AB - The voltage-dependent anion-selective channel of the outer mitochondrial membrane provides a unique system in which to study the molecular basis of voltage gating of ion flow. We have cloned and sequenced a cDNA coding for this protein in yeast. From the derived amino acid sequence, we have generated a preliminary model for the secondary structure of the protein which suggests that the protein forms a "β-barrel" type structure. Comparison of the VDAC amino acid sequence with that of the bacterial porins has indicated that the two classes of molecules appear to be unrelated.

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KW - bacterial porins

KW - gene cloning

KW - secondary structure

KW - sequence homology

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Molecular genetics of the VDAC ion channel: Structural model and sequence analysis

Abstract

Keywords

ASJC Scopus subject areas

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