Cloning and functional expression of a plant voltage-dependent chloride channel.
AUTOR(ES)
Lurin, C
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=161130Documentos Relacionados
- Voltage-dependent inactivation of a calcium channel.
- Primary structure and functional expression of the human cardiac tetrodotoxin-insensitive voltage-dependent sodium channel.
- Voltage-dependent gating of an asymmetric gramicidin channel.
- Voltage-dependent behavior of a "ball-and-chain" gramicidin channel.
- Mapping of residues forming the voltage sensor of the voltage-dependent anion-selective channel.