Isolation, characterization and molecular cloning of the bark lectins from Maackia amurensis.
A detailed study was made of the bark lectins of the legume tree Maackia amurensis using a combination of protein purification and cDNA cloning. The lectins, which are the most abundant bark proteins, are a complex mixture of isoforms composed of two types of subunits of 32 and 37 kDa, respectively. Isolation and characterization of the homotetrameric isoforms indicated that the 32 kDa subunit exhibits a 100-fold stronger haemagglutinating activity than the 37 kDa subunit. Molecular cloning confirmed that the two lectin subunits are encoded by different genes. The 32 kDa subunit is apparently encoded by a single gene, whereas two highly homologous genes encode the 37 kDa subunit. A comparison of the deduced amino acid sequences of the bark lectin cDNAs and the previously described cDNA encoding the seed haemagglutinin demonstrated that they are encoded by different genes.
Van Damme
E J
EJ
Laboratory for Phytopathology and Plant Protection, Katholieke Universiteit Leuven, Belgium.
Van Leuven
F
F
Peumans
W J
WJ
D000595:Amino Acid Sequence; D015152:Blotting, Northern; D015139:Blotting, Southern; D002852:Chromatography, Ion Exchange; D003001:Cloning, Molecular; D018076:DNA, Complementary; D004591:Electrophoresis, Polyacrylamide Gel; D007887:Fabaceae / Q000737:chemistry*; D037102:Lectins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D010802:Phylogeny; D037121:Plant Lectins; D010946:Plants, Medicinal; D017386:Sequence Homology, Amino Acid
D018076:DNA, Complementary; D037102:Lectins; D037121:Plant Lectins