Expression and processing of a hormonally regulated beta-expansin from soybean.

Abstract

Expansin proteins are essential components of acid-induced cell wall loosening in plants. Beta-expansins, which constitute a subfamily of related expansin proteins, include the group I grass pollen allergens. To provide a better description of beta-expansin expression, we have characterized a cytokinin-inducible beta-expansin from soybean (Glycine max cv Mandarin) called Cim1. Our results demonstrate that the hormones cytokinin and auxin act synergistically to induce the accumulation and proteolytic processing of Cim1. Carboxyl terminal truncation of a 35-kD form of Cim1 is predicted to remove the putative cellulose binding domain from the amino terminal cysteine-rich domain, resulting in a 20-kD form of the protein. Furthermore, the identical amino termini of the 35- and 20-kD forms of Cim1 correspond to a position 11 amino acids downstream of the predicted signal sequence cleavage site, suggesting proteolysis of a short amino terminal propeptide after removal of the signal peptide. This propeptide fragment contains a consensus site for N-glycosylation and our data suggest that it is glycosylated by a tunicamycin-sensitive mechanism in cultured soybean cells. The onset of Cim1 expression correlates with increased growth of soybean cultures. Ultimately, Cim1 is rapidly and specifically proteolyzed as soybean cultures reach stationary phase. These findings are consistent with the hypothesis that beta-expansin proteins are extensively modified by post-translational N-glycosylation and proteolysis.