Accumulation of a glycoprotein that is homologous to a seed storage protein in mung bean hypocotyls at the late stage of tissue elongation.

Physiological changes were examined in the amount of a 50-kDa glycoprotein (gp50) that was recovered in a nuclear fraction from hypocotyls of mung bean (Vigna radiata) seedlings. Immunoblot analysis indicated that the glycoprotein was present in hypocotyls and epicotyls from 4- and 5-day-old seedlings but not in hypocotyls from 2-day-old seedlings. The glycoprotein was not detected in leaves or roots. When we divided hypocotyls of 3-day-old seedlings into elongating region (0 to 1.5 cm below the cotyledon) and the mature region, we found gp50 in the mature region only. The results suggest that the 50-kDa glycoprotein is synthesized de novo and accumulates at the late stage during elongation of cells in the hypocotyl. Furthermore, an antibody specific to gp50 reacted with a major 50-kDa protein in cotyledons, which is known as a storage protein in mung bean cotyledon. Eighteen amino acid residues among 22 amino-terminal residues of gp50 were identical to those of the storage protein from cotyledon. A peptide map of the glycoprotein after digestion with V8 protease was similar to that of the storage protein. Overall, our findings suggest that the glycoprotein recovered in the nuclear fraction is an isoform of the seed storage protein that is expressed only in the mature cells of hypocotyls and epicotyls.