As Dictyostelium discoideum amoebae differentiate from the noncohesive to the mutually cohesive state, they synthesize two galactose-binding lectins--discoidins I and II--which have been implicated as obligatory components of the morphogenetic cell-cell recognition and cohesion system. These proteins have been shown to have similar amino acid compositions and subunit Mr and overlapping but distinct carbohydrate recognition specificities. We have performed extensive immunochemical and biochemical analyses to study the structural relationships between these two molecules and to eventually identify structural and functional domains. Antisera raised against highly purified preparations of discoidin I and discoidin II were tested for their reactivities against each protein by both immunoprecipitation and double diffusion analyses. The patterns of crossreactivity indicated the presence of shared as well as unique antigenic determinants. This interpretation was supported by two-dimensional thin-layer peptide map analysis and by studies with purified peptides. Of approximately 10-12 peptides observed after exhaustive tryptic digestion of each radioiodinated lectin, 3 appeared to be common to both. These putative common peptides were purified, and the corresponding peptides from discoidins I and II were found to behave identically by two-dimensional thin-layer analysis, gel filtration, and susceptibility to chymotrypsin. The finding of common and unique regions in discoidins I and II suggests analogies with other families of recognition proteins and may have important functional implications for these cell-cell recognition molecules
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