Immunochemical characterization of seed proteins of some species of the genusArachis L.

Relationships between seed protein patterns of 16 species ofArachis were studied by means of immunochemical methods (immunoelectrophoresis and double diffusion). The broad similarity of these patterns suggests that protein patterns are conservative in this genus from an evolutionary viewpoint. The differences which have evolved support recent schemes for classifying the genus, particularly the breakdown into sections. It also suggests thatA. villosa andA. correntina should probably be recognized as distinct species. The strong relationship indicated betweenA. hypogaea andA. batizocoi supports the hypothesis that the latter may be source of one of the genomes ofA. hypogaea. The possibility thatA. cardenasii might be the source of the other genome did not receive such strong positive support.     

The anther-specific protein encoded by the Brassica napus and Arabidopsis thaliana A6 gene displays similarity to β-1,3-glucanases

An anther-specific Brassica napus cDNA, A6, and two corresponding Arabidopsis thaliana genes have been isolated. Sequence analyses of A6 revealed similarity to β-1,3-glucanases. The deduced A6 protein differs from other β-1,3-glucanases in the possession of a long C-terminus. Immunoblotting using an antibody raised to the A6 protein detects a temporal 60 kDa protein in B. napus buds, suggesting that the long C-terminal region is present in the mature protein. A6 promoter—GUS and RNase fusions demonstrate that the A6 gene is tapetum-specific and temporally expressed with a peak in activity when the plant normally expresses callase (a complex of endo- and exo-β-1,3-glucanase activities). The sequence similarity of A6 to other β-1,3-glucanases, coupled with the temporal and spatial expression data, suggests that A6 may be part of the callase enzyme complex.