Solute pores, ion channels, and metabolite transporters in the outer and inner envelope membranes of higher plant plastids

Autor(en): Neuhaus, HE
Wagner, R 
Stichwörter: 2-OXOGLUTARATE MALATE TRANSLOCATOR; ADENINE-NUCLEOTIDE; ARABIDOPSIS-THALIANA L; Biochemistry & Molecular Biology; Biophysics; CAULIFLOWER FLORAL BUDS; channel; CHLOROPLAST ENVELOPE; FATTY-ACID SYNTHESIS; PEA ROOT PLASTIDS; PHOSPHATE TRANSLOCATOR; PISUM-SATIVUM-L; plastid envelope membrane; porin; SPINACH-CHLOROPLASTS; transport protein
Erscheinungsdatum: 2000
Herausgeber: ELSEVIER
Journal: BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volumen: 1465
Ausgabe: 1-2
Startseite: 307
Seitenende: 323
Zusammenfassung: 
All plant cells contain plastids. Various reactions are located exclusively within these unique organelles, requiring the controlled exchange of a wide range of solutes, ions, and metabolites. In recent years, several proteins involved in import and/or export of these compounds have been characterized using biochemical and electrophysiological approaches, and in addition have been identified at the molecular level. Several solute channels have been identified in the outer envelope membrane. These porin-like proteins in the outer envelope membrane were formerly thought to be quite unspecific, but have now been shown to exhibit significant substrate specificity and to be highly regulated. Therefore, the inter-envelope membrane space is not as freely accessible as previously thought. Transport proteins in the inner envelope membrane have been characterized in more detail. It has been proved unequivocally that a family of proteins (including triose phosphate-/phosphoenolpyruvate-, and glucose 6-phosphate-specific transporters) permit the exchange of inorganic phosphate and phosphorylated intermediates. A new type of plastidic 2-oxoglutarate/malate transporter has been identified and represents the first carrier with 12 putative transmembrane domains, to be located in the inner envelope membrane. The plastidic ATP/ADP transporter also contains 12 putative transmembrane domains and possesses striking structural similarity to ATP/ADP transporters found in intracellular, human pathogenic bacteria. (C) 2000 Published by Elsevier Science B.V. All rights reserved.
ISSN: 00052736
DOI: 10.1016/S0005-2736(00)00146-2

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