Amino acid sequence of honeybee prepromelittin synthesized in vitro.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 75 ·No. 2 ·1978-02-00 ·Pages 701-4

Suchanek G, Kreil G, Hermodson MA

Abstract

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 mellitin.

MeSH Terms

Amino Acid Sequence Bee Venoms/metabolism Bees Cell-Free System In Vitro Techniques Melitten/metabolism Protein Biosynthesis Protein Precursors/biosynthesis

Chemicals

Bee Venoms Protein Precursors Melitten prepromelittin

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Suchanek G

Kreil G

Hermodson M A

References (22)

22 references, click to expand

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Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.75.2.701

Published

1978-02-00

Pages

701-4

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC411324

Subset

External Links

PubMed source DOI: 10.1073/pnas.75.2.701 PMC Full Text View journal details

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Amino acid sequence of honeybee prepromelittin synthesized in vitro.

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