Vh. Nong et al., CDNA CLONING FOR A PUTATIVE CYSTEINE PROTEINASE FROM DEVELOPING SEEDSOF SOYBEAN, Biochimica et biophysica acta, N. Gene structure and expression, 1261(3), 1995, pp. 435-438
cDNA clones for a putative cysteine proteinase were isolated from deve
loping cotyledons of soybean (Glycine max.) using PCR-based techniques
. The full-length clone of 1441 bp encodes a proteinase pre-propolypep
tide of 380 amino acids. It belongs to the commonly known papain famil
y and shows the highest sequence homology (up to 53% identity) to the
protein 15A, a turgor-responsive cysteine proteinase of pea, as well a
s to several other stress inducible proteinases. Biosynthesis of the c
orresponding transcripts was shown to be developmentally controlled du
ring embryogenesis. Southern analyses revealed occurrence of one to tw
o genes in the soybean genome.