Immunocytochemical analysis of protein body formation in seeds of Sorghum bicolor

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Abstract
Electrophoretic analysis of sorghum (Sorghum bicolor (L.) Moench) seed prolamines in the presence of sodium dodecyl sulfate reveals major proteins of 27 and 25 kDa and two other proteins of 18 and 12 kDa. Antibodies were raised against this prolamine fraction and used to examine the subcellular distribution of the proteins in developing sorghum seeds. Protein bodies in the starchy endosperm and subaleurone cells usually are round in cross section and contain darkly staining materials arranged in concentric rings. Protein bodies in the first two layers beneath the aleurone layer are irregular in shape and contain discrete pockets of light and dark staining inclusions. Prolamines were detected in both types of protein bodies by immunolabeling. Other oganelles, including Golgi complexes, mitochondria, and amyloplasts, were not labeled. The protein bodies, which have ribosomes attached to their surfaces, are directly connected to the rough endoplasmic reticulum. In some instances, this endoplasmic reticulum was specifically labeled with protein A – gold particles. Based on these observations, we suggest that the rough endoplasmic reticulum serves as the site of both synthesis and accumulation of sorghum prolamines.

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