J. Taipalensuu et al., MYROSINASE-BINDING PROTEINS ARE DERIVED FROM A LARGE WOUND-INDUCIBLE AND REPETITIVE TRANSCRIPT, European journal of biochemistry, 243(3), 1997, pp. 605-611
Several non-myrosinase proteins have been found in association with so
me of the myrosinases extracted from rape (Brassica napus) seed. Most
of these proteins seemed to belong to a large family of proteins rangi
ng in size over approximately 30-110 kDa, namely the myrosinase-bindin
g protein (MBP) family. Potentially all of these MBPs might be derived
from a single large precursor, encoded by a 3.3-kb transcript. This t
ranscript coded for a 99-kDa glycine-rich protein with a highly repeti
tive structure. The mature 50-kDa and 52-kDa MBP amino-terminal was lo
cated 255 amino acids from the putative initiation methionine. Also, a
more divergently related transcript, the protein product of which was
unknown, has been cloned. However, the largest open reading frame sug
gested a proline-rich protein. While this transcript seemed to be expr
essed predominantly in seeds, the MBP transcripts were expressed in se
veral tissues and also exhibited a responsiveness to wounding and meth
yl jasmonate. Both proteins exhibited significant similarities to lect
ins from Artocarpus integer and from Maclura pomifera.