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Intracellular localization of VDAC proteins in plants
Authors:Cathrin?Clausen,Iryna?Ilkavets,Rowena?Thomson,Katrin?Philippar,Aleksandar?Vojta,Torsten?M?hlmann,Ekkehard?Neuhaus,Hrvoje?Fulgosi,Jürgen?Soll  author-information"  >  author-information__contact u-icon-before"  >  mailto:soll@uni-muenchen.de"   title="  soll@uni-muenchen.de"   itemprop="  email"   data-track="  click"   data-track-action="  Email author"   data-track-label="  "  >Email author
Affiliation:(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 beta-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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