C. Waldron et al., CHARACTERIZATION OF A GENOMIC SEQUENCE CODING FOR POTATO MULTICYSTATIN, AN 8-DOMAIN CYSTEINE PROTEINASE-INHIBITOR, Plant molecular biology, 23(4), 1993, pp. 801-812
A gene coding for potato multicystatin (PMC), the crystalline inhibito
r of cysteine proteases which is found in tubers, was isolated and cha
racterized. The deduced polypeptide product of this genomic sequence i
s 757 amino acids long and has a molecular mass of 86,778 Da. It consi
sts exclusively of eight closely related domains, with 53-89% identity
of residues. Each repeated unit is homologous to the cystatin superfa
mily of cysteine protease inhibitors. To date, no other member of this
family has been found to contain so many inhibitor domains in one pol
ypeptide. Eight introns are proposed in the 3.5 kb of genomic DNA codi
ng for PMC, one in each cystatin unit. There is a family of 4 to 6 suc
h large genes in potato, while in pea and maize the homologues are muc
h smaller, and probably code for single-domain cystatins. PMC transcri
pts are abundant in tubers, but scarce in undamaged leaves or stems of
field-grown potatoes. The tuber messages are derived from at least fo
ur genes (including the cloned example). The pattern of gene expressio
n, as well as the properties of the protein, suggest that PMC has a ro
le in the plant's defense system.