Isolation and characterization of an amino acid-selective channel protein present in the chloroplastic outer envelope membrane

Autor(en): Pohlmeyer, K
Soll, J
Steinkamp, T
Hinnah, S
Wagner, R 
Stichwörter: APPARATUS; COMPONENT; FUNCTIONAL-CHARACTERIZATION; FUSION; IMPORT MACHINERY; LIGHT; Multidisciplinary Sciences; PATHWAY; Science & Technology - Other Topics; SIDE; TRANSLOCATION; VESICLES
Erscheinungsdatum: 1997
Herausgeber: NATL ACAD SCIENCES
Journal: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volumen: 94
Ausgabe: 17
Startseite: 9504
Seitenende: 9509
Zusammenfassung: 
The reconstituted pea chloroplastic outer envelope protein of 16 kDa (OEP16) forms a slightly cation-selective, high-conductance channel with a conductance of ii = 1,2 nS (in 1 M KCl), The open probability of OEP16 channel is highest at 0 mV (P-open = 0.8), decreasing exponentially with higher potentials. Transport studies using reconstituted recombinant OEP16 protein show that the OEP16 channel is selective for amino acids but excludes triosephosphates or uncharged sugars, Crosslinking indicates that OEP16 forms a homodimer in the membrane, According to its primary sequence and predicted secondary structure, OEP16 shows neither sequence nor structural homologies to classical porins. The results indicate that the intermembrane space between the two envelope membranes might not be as freely accessible as previously thought.
ISSN: 00278424
DOI: 10.1073/pnas.94.17.9504

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