An evolutionary model for the insect vitellins.
Insects can be divided into three groups based on the sizes of the polypeptide constituents of their vitellogenins and vitellins. In order to determine the relationships between these groups, antisera to the vitellins of seven insects from six taxonomic orders were used to assess immunological cross-reactivity. Antigenic relatedness was observed only between vitellins from species within the same family. Amino acid compositional data for vitellins from nine species were used to assess homology by difference matrices. The S delta Q values were similar for both intra-order and inter-order comparisons and strongly suggested relatedness. The S delta n comparisons supported the immunological data that indicated that the vitellins were evolving rapidly. For most insect vitellins there are two distinct size classes of polypeptides that seem to be derived from a single asymmetric proteolytic cleavage of a precursor. We propose a model that suggests that the different size polypeptides represent distinct domains and that in the evolution of the vitellogenin genes of the Diptera and Hymenoptera there has been domain elimination.
D000595:Amino Acid Sequence; D000818:Animals; D005075:Biological Evolution; D003429:Cross Reactions; D004175:Diptera / Q000235:genetics; D004527:Egg Proteins / Q000235:genetics* / Q000276:immunology; D005796:Genes; D006927:Hymenoptera / Q000235:genetics; D007313:Insecta / Q000235:genetics*; D008957:Models, Genetic; D010802:Phylogeny; D011499:Protein Processing, Post-Translational
D004527:Egg Proteins; C035651:vitelline membrane proteins