Translation of melittin messenger RNA in vitro yields a product terminating with glutaminylglycine rather than with glutaminamide.

Abstract

Melittin messenger RNA from queen bee venom glands has been translated in a cell-free system from wheat germ. A product larger than promelittin is formed which has the carboxy-terminal sequence-Gln-Gln-GlyCOOH. Melittin and promelittin from venom glands terminate in -Gln-GlnCONH2. The possible role of the extra glycine residue in the formation of a COOH-terminal amide via a transamidase-like reaction is discussed.