Isolation and primary structure of two sulfakinin-like peptides from the fleshfly, Neobellieria bullata.
1. Two novel insect myotropic peptides termed neosulfakinin-I (Neb-SK-I) and neosulfakinin-II (Neb-SK-II) were isolated from the heads of 42 thousand fleshflies, Neobellieria bullata (Diptera, Sarcophagidae). 2. A series of four, high-performance liquid chromatographic (HPLC), fractionations performed on columns with different characteristic features yielded two purified biologically active, hindgut motility stimulating fractions, suitable for amino acid sequence analysis. 3. The proposed sequences for the two peptides are: Phe-Asp-Asp-Tyr-Gly-His-Met-Arg-Phe-(NH2), (Neb-SK-I) and X-X-Glu-Glu-Gln-Phe-Asp-Asp-Tyr-Gly-His-Met-Arg-Phe-(NH2), (Neb-SK-II). 4. These sulfakinins exhibit very high homology to putative drosulfakinin sequences which, however, have not yet been isolated, but were deduced from a cloned Drosophila gene encoding these peptides. 5. Here we provide the first evidence for the expression of such peptides present in Dipterans. 6. Insect sulfakinins show structural identities with the hormonally-active portion of vertebrate gastrin II-, cholecystokinin- and caerulin-related peptides and they share common carboxy terminal sequences with invertebrate/vertebrate peptides of the FMRFamide peptide family.
Plant Protection Institute, Hungarian Academy of Sciences, Budapest.
A
A
Fónagy
L
L
Schoofs
P
P
Proost
J
J
Van Damme
A
A
De Loof
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D003001:Cloning, Molecular; D004175:Diptera / Q000737:chemistry*; D004330:Drosophila / Q000737:chemistry; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry / Q000302:isolation & purification*; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification*; D017386:Sequence Homology, Amino Acid
D009842:Oligopeptides; D010455:Peptides; C078373:neosulfakinin I; C078374:neosulfakinin II