Protein phosphorylation stimulates the rate of malate uptake across the peribacteroid membrane of soybean nodules.
Incubation of intact isolated symbiosomes with [gamma-32P]ATP, followed by isolation of the peribacteroid membrane and polypeptide analysis, showed that a single major polypeptide at 26 kDa was labelled. Antibodies raised against nodulin 26 reacted with a similar sized polypeptide. Incubation of the symbiosomes with alkaline phosphatase removed the label from this polypeptide. Pre-incubation with ATP stimulated malate accumulation by isolated symbiosomes, but only slightly (10-30%). Pre-treatment of symbiosomes with alkaline phosphatase inhibited malate uptake substantially and this inhibition was completely relieved by addition of ATP. The ATP stimulation of malate uptake was not affected by ATPase inhibitors. It is suggested that the rate of malate uptake across the peribacteroid membrane is controlled by phosphorylation of nodulin 26.
Ouyang
L J
LJ
Division of Biochemistry and Molecular Biology, Australian National University, Canberra, ACT.
Whelan
J
J
Weaver
C D
CD
Roberts
D M
DM
Day
D A
DA
D000469:Alkaline Phosphatase / Q000494:pharmacology; D001692:Biological Transport; D007700:Kinetics; D008293:Malates / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism; D009586:Nitrogen Fixation; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D010940:Plant Proteins / Q000378:metabolism*; D012230:Rhizobiaceae; D013025:Glycine max; D013559:Symbiosis
D008293:Malates; D008565:Membrane Proteins; D010750:Phosphoproteins; D010940:Plant Proteins; C030298:malic acid; D000469:Alkaline Phosphatase