ATP-released large subunits participate in the assembly of RuBP carboxylase.
Preincubation of 35S-methionine-labeled chloroplast extracts with ATP at 0 degree C potentiates the subsequent assembly of labeled large subunits into RuBPCase . This is correlated with the dissociation of newly synthesized large subunits from the 29S large subunit binding protein complex. These released large subunits then assemble into RuBPCase in a second, nucleotide-stimulated reaction. The data demonstrate that the 29S complex can play an active role in the assembly of RuBPCase .
D000255:Adenosine Triphosphate / Q000502:physiology*; D002736:Chloroplasts / Q000378:metabolism; D003720:Densitometry; D004591:Electrophoresis, Polyacrylamide Gel; D010940:Plant Proteins / Q000096:biosynthesis; D010944:Plants / Q000378:metabolism*; D012273:Ribulose-Bisphosphate Carboxylase / Q000378:metabolism*
D010940:Plant Proteins; D000255:Adenosine Triphosphate; D012273:Ribulose-Bisphosphate Carboxylase