Detection of small GTP-binding proteins in the outer envelope membrane of pea chloroplasts.
We found small GTP-binding proteins in the outer envelope membrane of pea chloroplasts. The proteins in this membrane were separated by SDS-PAGE, transferred to a nitrocellulose filter, and incubated with [alpha-32P]GTP. Three GTP-binding proteins with the molecular weight of 24,000 were found. Binding was prevented by 10(-8)-10(-7) M GTP or by 10(-7) M guanosine 5'-[gamma-thio]triphosphate or GDP; binding was unaffected by 10(-8)-10(-6) M ATP. Thermolysin treatment of intact chloroplasts resulted in the loss of GTP-binding activity, suggesting that these proteins were in the cytosolic side of the outer envelope membrane.
Sasaki
Y
Y
Department of Food Science and Technology, Faculty of Agriculture, Kyoto University, Japan.
Sekiguchi
K
K
Nagano
Y
Y
Matsuno
R
R
D001667:Binding, Competitive; D002736:Chloroplasts / Q000737:chemistry* / Q000187:drug effects; D004591:Electrophoresis, Polyacrylamide Gel; D007887:Fabaceae; D019204:GTP-Binding Proteins / Q000032:analysis* / Q000187:drug effects; D008565:Membrane Proteins / Q000737:chemistry* / Q000187:drug effects; D008970:Molecular Weight; D010940:Plant Proteins / Q000737:chemistry* / Q000187:drug effects; D010946:Plants, Medicinal; D013820:Thermolysin / Q000494:pharmacology
D008565:Membrane Proteins; D010940:Plant Proteins; D013820:Thermolysin; D019204:GTP-Binding Proteins