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Mol. Cells 2009; 27(3): 321-327

Published online March 31, 2009

https://doi.org/10.1007/s10059-009-0041-z

© The Korean Society for Molecular and Cellular Biology

Pathogen Inducible Voltage-Dependent Anion Channel (AtVDAC) Isoforms Are Localized to Mitochondria Membrane in Arabidopsis

Sang Min Lee, My Hanh Thi Hoang, Hay Ju Han, Ho Soo Kim, Kyunghee Lee, Kyung Eun Kim, Doh Hoon Kim, Sang Yeol Lee, and Woo Sik Chung

Received: October 6, 2008; Revised: December 6, 2008; Accepted: December 18, 2008

Abstract

Voltage-dependent anion channels (VDACs) are reported to be porin-type, ?-barrel diffusion pores. They are prominently localized in the outer mitochondrial membrane and are involved in metabolite exchange between the organelle and the cytosol. In this study, we have investigated a family of VDAC isoforms in Arabidopsis thaliana (AtVDAC). We have shown that the heterologous expression of AtVDAC proteins can functionally complement a yeast mutant lacking the endogenous mitochondrial VDAC gene. AtVDACs tagged with GFP were localized to mitochondria in both yeast and plant cells. We also looked at the response of AtVDACs to biotic and abiotic stresses and found that four AtVDAC transcripts were rapidly up-regulated in response to a bacterial pathogen.

Keywords Arabidopsis, mitochondria, outer membrane, pathogen, voltage-dependent anion channel

Article

Research Article

Mol. Cells 2009; 27(3): 321-327

Published online March 31, 2009 https://doi.org/10.1007/s10059-009-0041-z

Copyright © The Korean Society for Molecular and Cellular Biology.

Pathogen Inducible Voltage-Dependent Anion Channel (AtVDAC) Isoforms Are Localized to Mitochondria Membrane in Arabidopsis

Sang Min Lee, My Hanh Thi Hoang, Hay Ju Han, Ho Soo Kim, Kyunghee Lee, Kyung Eun Kim, Doh Hoon Kim, Sang Yeol Lee, and Woo Sik Chung

Received: October 6, 2008; Revised: December 6, 2008; Accepted: December 18, 2008

Abstract

Voltage-dependent anion channels (VDACs) are reported to be porin-type, ?-barrel diffusion pores. They are prominently localized in the outer mitochondrial membrane and are involved in metabolite exchange between the organelle and the cytosol. In this study, we have investigated a family of VDAC isoforms in Arabidopsis thaliana (AtVDAC). We have shown that the heterologous expression of AtVDAC proteins can functionally complement a yeast mutant lacking the endogenous mitochondrial VDAC gene. AtVDACs tagged with GFP were localized to mitochondria in both yeast and plant cells. We also looked at the response of AtVDACs to biotic and abiotic stresses and found that four AtVDAC transcripts were rapidly up-regulated in response to a bacterial pathogen.

Keywords: Arabidopsis, mitochondria, outer membrane, pathogen, voltage-dependent anion channel

Mol. Cells
May 31, 2022 Vol.45 No.5, pp. 273~352
COVER PICTURE
Fe2+ ion depletion-induced expression of BΔGFP at the early stage of leaf development (Choi et al., pp. 294-305).

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