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Plant Cell, Vol. 10, 1207-1216, July 1998, Copyright © 1998, American Society of Plant Physiologists
A High-Conductance Solute Channel in the Chloroplastic Outer Envelope from Pea
Kai Pohlmeyera,
Jürgen Solla,
Rudolf Grimmb,
Kerstin Hillc, and
Richard Wagnerc
a Botanisches Institut, Universität Kiel, D-24098 Kiel, Germany
b Hewlett Packard, D-76337 Waldbronn, Germany
c Fachbereich Biologie/Chemie, Universität Osnabrück, D-49034 Osnabrück, Germany
Correspondence to:
Jürgen Soll, jsoll{at}bot.uni-kiel.de (E-mail), 49-431-880-4222 (fax).
The pea chloroplastic outer envelope protein OEP24 can function as a general solute channel. OEP24 is present in chloroplasts, etioplasts, and non-green root plastids. The heterologously expressed protein forms a voltage-dependent, high-conductance ( = 1.3 nS in 1 M KCl), and slightly cation-selective ion channel in reconstituted proteoliposomes. The highest open probability (Popen  0.8) is at 0 mV, which is consistent with the absence of a transmembrane potential across the chloroplastic outer envelope. The OEP24 channels allow the flux of triosephosphate, dicarboxylic acids, positively or negatively charged amino acids, sugars, ATP, and Pi. Structure prediction algorithms and circular dichroism spectra indicate that OEP24 contains seven amphiphilic ß strands. The primary structure of OEP24 shows no homologies to mitochondrial or bacterial porins on a primary sequence basis, and OEP24 is functionally not inhibited by cadaverine, which is a potent inhibitor of bacterial porins. We conclude that OEP24 represents a new type of solute channel in the plastidic outer envelope.
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