Amino acid sequence of honeybee prepromelittin synthesized in vitro.

Abstract
Translation of melittin mRNA from queen bee venom glands in a cell-free system from wheat germ yielded prepromelittin. Sequence analysis of the labeled in vitro product was performed by automatic Edman degradation of the intact polypeptide and by analysis of some of its proteolytic fragments. Prepomelittin was composed of 70 amino acids, 2 of which were not identified. The sequence of melittin is located in the COOH-terminal third of the polypeptide chain (residues 44-69). Prepromelittin starts with a very hydrophobic pre-region, probably 21 residues long, followed by a pro-part of unusual sequence, containing only alanine proline and acidic residues. At least 3 post-translational reactions are required to convert prepromelittin to melittin.