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Intracellular localization of VDAC proteins in plants |
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| Authors: | Cathrin?Clausen Iryna?Ilkavets Rowena?Thomson Katrin?Philippar Aleksandar?Vojta Torsten?M?hlmann Ekkehard?Neuhaus Hrvoje?Fulgosi |
| Institution: | (1) Department Biologie I, Ludwig-Maximilians-Universität München, Menzingerstr. 67, 80638 München, Germany;(2) Fachbereich Biologie, Universität Kaiserslautern, Erwin-Schrödinger-Straße, 67663 Kaiserslautern, Germany;(3) Present address: Biochemisches Institut, Universität Kiel, Olshausenstr. 40, 24098 Kiel, Germany;(4) Present address: Department of Molecular Genetics, Ruder Boskovic Institute, University of Zagreb, Bijenicka 54, 10000 Zagreb, Croatia |
| Abstract: | Voltage-dependent anion channels (VDACs) are porin-type  -barrel diffusion pores. They are prominent in the outer membrane of mitochondria and facilitate metabolite exchange between the organelle and the cytosol. Here we studied the subcellular distribution of a plant VDAC-like protein between plastids and mitochondria in green and non-green tissue. Using in vitro studies of dual-import into mitochondria and chloroplasts as well as transient expression of fluorescence-labeled polypeptides, it could be clearly demonstrated that this VDAC isoform targets exclusively to mitochondria and not to plastids. Our results support the idea that plastids evolved a concept of solute exchange with the cytosol different from that of mitochondria.Abbreviations AOX Alternative oxidase - p Precursor form - POM36 Putative outer mitochondrial membrane proteins of 36 kDa - SSU Small subunit of ribulose-1,5-bisphosphate carboxylase-oxygenase (Rubisco) - VDAC Voltage-dependent anion channel |
| Keywords: | Envelope membrane Mitochondrion Pisum Plastid Solute transport Voltage-dependent anion channel |
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