Abstract
Voltage-dependent anion channels (VDACs) are conserved proteins of the mitochondria. We have functionally compared Arabidopsis VDACs using Saccharomyces cerevisiae Δpor1 and M3 yeast system. VDAC (1, 2, and 4) were able to restore Δpor1 growth in elevated temperature, in oxidative and salt stresses, whereas VDAC3 only partially rescued Δpor1 in these conditions. The ectopic expression of VDAC (1, 2, 3, and 4) in mutant yeast recapitulated the mitochondrial membrane potential thus, enabled it to maintain reactive oxygen species homeostasis. Overexpression of these VDACs (AtVDACs) in M3 strain did not display any synergistic or antagonistic activity with the native yeast VDAC1 (ScVDAC1). Collectively, our data suggest that Arabidopsis VDACs are involved in regulating respiration, reactive oxygen species homeostasis, and stress tolerance in yeast.
Highlights
Voltage-dependent anion channels (VDACs) are highly conserved protein, present in all eukaryotic species examined so far (Colombini, 2012)
We demonstrate the role of Arabidopsis VDAC proteins in respiration, maintaining mitochondrial membrane potential (MMP), reactive oxygen species (ROS) homeostasis, and stress
In our methyl viologen (MV) stress treatment, we observed that VDAC2 and VDAC4 were upregulated than control, especially VDAC4, which was highly upregulated
Summary
Voltage-dependent anion channels (VDACs) are highly conserved protein, present in all eukaryotic species examined so far (Colombini, 2012). These are thought to regulate metabolite transport between mitochondria and the cytoplasm in both physiological and pathological conditions (Kroemer et al, 2007). VDACs are b-barrel proteins of a single subunit of the molecular mass of 30 kDa. VDACs are b-barrel proteins of a single subunit of the molecular mass of 30 kDa They possess a conserved structure as well as similar biophysical properties across species (Colombini et al, 1996). Two genes encode VDAC isoforms (ScVDAC1 and ScVDAC2) whereas in mammals, including mice and human have three isoforms (Kusano et al, 2009).
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