Mc. Gonzalez et al., EXPRESSION AND LOCALIZATION OF PHOSPHOENOLPYRUVATE CARBOXYLASE IN DEVELOPING AND GERMINATING WHEAT GRAINS, Plant physiology, 116(4), 1998, pp. 1249-1258
Phosphoenolpyruvate carboxylase (PEPC) activity and corresponding mRNA
levels were investigated in developing and germinating wheat (Triticu
m aestivum) grains. During grain development PEPC activity increased t
o reach a maximum 15 d postanthesis. Western-blot experiments detected
two main PEPC polypeptides with apparent molecular masses of 108 and
103 kD. The most abundant 103-kD PEPC subunit remained almost constant
throughout the process of grain development and in the scutellum and
aleurone layer of germinating grains. The less-abundant 108-kD polypep
tide progressively disappeared during the second half of grain develop
ment and was newly synthesized in the scutellum and aleurone layer of
germinating grains. PEPC mRNA was detected throughout the process of g
rain development; however, in germinating grains PEPC mRNA accumulated
transiently in the scutellum and aleurone layer, showing a sharp maxi
mum 24 h after imbibition. Immunolocalization studies revealed the pre
sence of the enzyme in tissues with a high metabolic activity, as well
as in the vascular tissue of the crease area of developing grains. A
clear increase in PEPC was observed in the scutellar epithelium of gra
ins 24 h after imbibition. The data suggest that the transiently forme
d PEPC mRNA in the scutellar epithelium encodes the 108-kD PEPC subuni
t.