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Plant Cell ; 8(4): 701-11, 1996 Apr.
Article in English | MEDLINE | ID: mdl-8624442

ABSTRACT

Plant cell membrane anion channels participate in basic physiological functions, such as cell volume regulation and signal transduction. However, nothing is known about their molecular structure. Using a polymerase chain reaction strategy, we have cloned a tobacco cDNA (CIC-Nt1) encoding a 780-amino acid protein with several putative transmembrane domains. CIC-Nt1 displays 24 to 32% amino acid identity with members of the animal voltage-dependent chloride channel (CIC) family, whose archetype is CIC-0 from the Torpedo marmorata electric organ. Injection of CIC-Nt1 complementary RNA into Xenopus oocytes elicited slowly activating inward currents upon membrane hyperpolarization more negative than -120 mV. These currents were carried mainly by anions, modulated by extracellular anions, and totally blocked by 10 mM extracellular calcium. The identification of CIC-Nt1 extends the CIC family to higher plants and provides a molecular probe for the study of voltage-dependent anion channels in plants.


Subject(s)
Chloride Channels/genetics , Nicotiana/genetics , Plants, Toxic , Amino Acid Sequence , Animals , Base Sequence , Chlorides/physiology , Cloning, Molecular , DNA Primers/chemistry , DNA, Complementary/genetics , Ion Channel Gating/physiology , Membrane Potentials , Molecular Sequence Data , Plant Proteins/genetics , Sequence Alignment , Sequence Homology, Amino Acid , Xenopus laevis
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