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Oep23 forms an ion channel in the chloroplast outer envelope
by
Goetze, Tom Alexander
, Bölter, Bettina
, Jeshen, Ingrid
, Soll, Jürgen
, Grahl, Sabine
, Patil, Manali
in
Agriculture
/ Amino Acid Sequence
/ biochemical pathways
/ Biochemistry and physiology
/ Biomedical and Life Sciences
/ cations
/ Chlorophyta
/ Chloroplast Proteins - genetics
/ Chloroplast Proteins - metabolism
/ chloroplasts
/ Chloroplasts - metabolism
/ Ion Channels - genetics
/ Ion Channels - metabolism
/ Life Sciences
/ metabolites
/ mitochondria
/ Molecular Sequence Data
/ peas
/ Pisum sativum - chemistry
/ Pisum sativum - genetics
/ Pisum sativum - metabolism
/ Pisum sativum subsp. sativum var. sativum
/ Plant Sciences
/ porins
/ potassium chloride
/ probability
/ protein transport
/ recombinant proteins
/ Recombinant Proteins - chemistry
/ Recombinant Proteins - genetics
/ Recombinant Proteins - metabolism
/ Research Article
/ Sequence Alignment
/ solutes
/ Tree Biology
2015
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Oep23 forms an ion channel in the chloroplast outer envelope
by
Goetze, Tom Alexander
, Bölter, Bettina
, Jeshen, Ingrid
, Soll, Jürgen
, Grahl, Sabine
, Patil, Manali
in
Agriculture
/ Amino Acid Sequence
/ biochemical pathways
/ Biochemistry and physiology
/ Biomedical and Life Sciences
/ cations
/ Chlorophyta
/ Chloroplast Proteins - genetics
/ Chloroplast Proteins - metabolism
/ chloroplasts
/ Chloroplasts - metabolism
/ Ion Channels - genetics
/ Ion Channels - metabolism
/ Life Sciences
/ metabolites
/ mitochondria
/ Molecular Sequence Data
/ peas
/ Pisum sativum - chemistry
/ Pisum sativum - genetics
/ Pisum sativum - metabolism
/ Pisum sativum subsp. sativum var. sativum
/ Plant Sciences
/ porins
/ potassium chloride
/ probability
/ protein transport
/ recombinant proteins
/ Recombinant Proteins - chemistry
/ Recombinant Proteins - genetics
/ Recombinant Proteins - metabolism
/ Research Article
/ Sequence Alignment
/ solutes
/ Tree Biology
2015
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Oep23 forms an ion channel in the chloroplast outer envelope
by
Goetze, Tom Alexander
, Bölter, Bettina
, Jeshen, Ingrid
, Soll, Jürgen
, Grahl, Sabine
, Patil, Manali
in
Agriculture
/ Amino Acid Sequence
/ biochemical pathways
/ Biochemistry and physiology
/ Biomedical and Life Sciences
/ cations
/ Chlorophyta
/ Chloroplast Proteins - genetics
/ Chloroplast Proteins - metabolism
/ chloroplasts
/ Chloroplasts - metabolism
/ Ion Channels - genetics
/ Ion Channels - metabolism
/ Life Sciences
/ metabolites
/ mitochondria
/ Molecular Sequence Data
/ peas
/ Pisum sativum - chemistry
/ Pisum sativum - genetics
/ Pisum sativum - metabolism
/ Pisum sativum subsp. sativum var. sativum
/ Plant Sciences
/ porins
/ potassium chloride
/ probability
/ protein transport
/ recombinant proteins
/ Recombinant Proteins - chemistry
/ Recombinant Proteins - genetics
/ Recombinant Proteins - metabolism
/ Research Article
/ Sequence Alignment
/ solutes
/ Tree Biology
2015
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Oep23 forms an ion channel in the chloroplast outer envelope
Journal Article
Oep23 forms an ion channel in the chloroplast outer envelope
2015
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Overview
Background
Metabolite, ion and protein translocation into chloroplasts occurs across two membranes, the inner and the outer envelope. Solute and metabolite channels fulfill very important functions in integrating the organelles into the metabolic network of the cell. However so far only a few have been identified. Here we describe the identification and the characterization of the outer envelope protein of 23 kDa, Oep23 from garden pea.
Results
Oep23 is found in the entire plant lineage from green algae to flowering plants. It is expressed in all organs and developmental states tested so far. The reconstituted recombinant protein Oep23 from pea forms a high conductance ion channel with a maximal conductance in the fully open state of 466 ± 14pS at a holding potential of +100 mV (in 250 mM KCl). The Oep23 channel is cation selective (P
K+
: P
Cl-
= 15 : 1) with a voltage dependent open probability of maximal V
mem
= 0 mV.
Conclusion
The data indicate that the Oep23 activity represents a single channel unit and does not assemble into a multiple pore complex like bacterial type porins or mitochondrial voltage dependent anion channel. Thus, Oep23 represents a new member of ion channels in the outer envelope of chloroplasts involved in solute exchange.
Publisher
BioMed Central,BioMed Central Ltd
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