Assembly and intracellular transport of phaseolin, the major storage protein of Phaseolus vulgaris L.

Phaseolin is a trimeric glycoprotein that accumulates in the protein storage vacuoles of common bean
(Phaseolus vulgaris 1.) seeds. The resistance to proteolytic degradation is likely to be an important feature
of native phaseolin, allowing its stable accumulation in the protein storage vacuoles. Acquisition of a protease-
resistant structure is linked to the assembly of phaseolin subunits into trimers, a rapid and efficient
process occurring in the endoplasmic reticulum. In bean cotyledonary cells phaseolin trimerization is
likely to be assisted by cellular factors and occurs also in the presence of inhibitors of N-linked glycosylation.
A mechanism devoted to the retention of unassembled subunits and of assembly intermediates in an
early compartment of the secretory pathway would guarantee that only the protease-resistant form of
the protein is transported to the storage vacuoles, contributing to the overall efficiency of storage protein
accumulation.