cDNA cloning of the housefly pigment‐dispersing factor (PDF) precursor protein and its peptide comparison among the insect circadian neuropeptides

Mar 5, 2004Journal of peptide science : an official publication of the European Peptide Society

Cloning the housefly’s pigment-dispersing factor protein and comparing it to other insect daily rhythm peptides

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Abstract

An isolated clone of 527 bp from the housefly Musca domestica encodes a PDF precursor protein of ordinary length.

Musca PDF shows 78%-94% sequence identity and 89%-100% similarity to PDFs from other insects and crustaceans.
A single amino acid difference exists between Musca PDF and Drosophila PDF, with Ser in Musca and Asn in Drosophila at position 14.
The presence of a characteristic Ser10 in Musca indicates a unique structural profile shared with Drosophila PDFs.
Musca and Drosophila PDFs likely belong to a single structurally evolved group based on sequence analyses.
The primary structures of the PAP regions suggest that Musca PDF precursor is related to Drosophila PDF precursor.

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Pigment-dispersing factor (PDF), an 18-amino acid neuropeptide, is a principal circadian neurotransmitter for the circadian rhythms of the locomotor activity in flies. Recently, two completely different types of PDF precursor were clarified; that of the cricket Gryllus bimaculatus and that of the last-summer cicada Meimuna opalifera. The G. bimaculatus PDF precursor is extraordinarily short and comprises a nuclear localization signal (NLS), while the M. opalifera PDF precursor is of ordinary length, comparable to that seen for the precursors of crustacean beta-PDH homologues. Although their PDF peptide regions were exactly the same, the regions containing a signal peptide combined with a PDF-associated peptide (PAP) were remarkably different from each other. Such a grouping suggested a fundamental role for the PAP peptide in the circadian clock, perhaps associated with PDF function. In the present study, the cDNA cloning of PDF from the adult brains of the housefly Musca domestica was carried out and it was found that an isolated clone (527 bp) encodes a PDF precursor protein of ordinary length. The PDF peptide shows a high sequence identity (78%-94%) and similarity (89%-100%) to insect PDFs and also to the crustacean beta-PDH peptides. In particular, there is only a single amino acid difference between the PDFs of Musca and Drosophila; at position 14 Ser for Musca PDF and Asn for Drosophila PDF. A characteristic Ser10 in Drosophila was retained in Musca, indicating the presence of a structural profile unique to these PDFs. The results of sequence analyses suggest that Musca and Drosophila PDFs are to be considered members of a single group that has evolved structurally. When the primary structure of the PAP regions was compared, the Musca PDF precursor also belonged to the same group as that to which the Drosophila PDF precursor belongs.

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cDNA cloning of the housefly pigment‐dispersing factor (PDF) precursor protein and its peptide comparison among the insect circadian neuropeptides

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