Title: Neuropeptide-like precursor 4 is uniquely expressed during pupal diapause in the flesh fly Authors
|Li, Aiqing - OHIO STATE UNIVERSITY|
|Denlinger, David - OHIO STATE UNIVERSITY|
Submitted to: Peptides
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: October 1, 2008
Publication Date: March 1, 2009
Repository URL: http://ddr.nal.usda.gov/bitstream/10113/42089/1/IND44382028.pdf
Citation: Li, A., Rinehart, J.P., Denlinger, D.L. 2009. Neuropeptide-like Precursor 4 is Uniquely Expressed During Pupal Diapause in the Flesh Fly. Peptides. 30(3):518-521. Interpretive Summary: Winter poses a major challenge for insects. To be successful in environments with distinct seasons, insects must grow and reproduce only for a few months during the summer and then survive the remainder of the year without feeding, while dealing with the stresses that winter brings to them. Most insects survive winter by entering diapause, a state that is characterized by developmental arrest and increased stress tolerance. It has long been known that in most cases, diapause is controlled by the brain of the insect. In insects such as the flesh fly, the brain is able to receive light, determine when winter is approaching due to shortened daylengths, and then start diapause using the insect’s hormonal system. In this study, we characterize a neuropeptide (protein found in the nervous system) that uniquely expressed during diapause of the flesh fly. Although we still do not know the function of this protein during diapause, its close association with diapause suggests that it may play a role in initiating diapause in this species.
Technical Abstract: Suppression subtractive hybridization comparing brains from diapausing and nondiapausing pupae of the flesh fly, Sarcophaga crassipalpis, suggested that the gene encoding neuropeptide-like precursor 4 (Nplp4) was uniquely expressed during diapause. We have sequenced the full-length cDNA encoding Nplp4 and used Northern blots to further evaluate linkage to diapause. The open reading frame of this cDNA encodes a 61-amino acid residue precursor protein containing a predicted 18 residue signal peptide, one 22-amino acid and one 2-amino acid propeptides, and a 19-amino acid neuropeptide. The amino acid sequence of the precursor protein shows 64% identity to Drosophila melanogaster Nplp4; homologues of this precursor protein are not known from species other than these two flies. Nplp4 mRNA levels were quite low in nondiapausing (long day) pupae, but in contrast the gene was highly upregulated in diapausing (short day) pupae. Expression increased at the onset of diapause, remained high throughout diapause, and then decreased 2 days after diapause was terminated. Although the function of this precursor protein and the neuropeptide it yields remain unknown, this close association with diapause suggests a potential role for Nplp4 in initiating and maintaining diapause in the flesh fly.