Amino acid sequence of honeybee prepromelittin synthesized in vitro

Translation of melittin messenger RNA 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 as well as by analysis of some of its proteolytic f...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1978-02, Vol.75 (2), p.701-704
Main Authors: Suchanek, G, Kreil, G, Hermodson, M.A
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Animal glands
Apis mellifera
Bee Venoms - metabolism
Bees
Biochemistry
Cell free system
Electrophoresis
In Vitro Techniques
Material degradation
Melitten - metabolism
Messenger RNA
Neutral amino acids
Protein Biosynthesis
Protein Precursors - biosynthesis
RNA
Venoms
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Summary:Translation of melittin messenger RNA 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 as well as by analysis of some of its proteolytic fragments. Prepromelittin was shown to be composed of 70 amino acids, two of which have not been 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 three post-translational reactions are required to convert prepromelittin to melittin.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.75.2.701