STRUCTURAL ORGANIZATION OF THE HELICOVERPA-ZEA GENE ENCODING THE PRECURSOR PROTEIN FOR PHEROMONE BIOSYNTHESIS-ACTIVATING NEUROPEPTIDE AND OTHER NEUROPEPTIDES
Pwk. Ma et al., STRUCTURAL ORGANIZATION OF THE HELICOVERPA-ZEA GENE ENCODING THE PRECURSOR PROTEIN FOR PHEROMONE BIOSYNTHESIS-ACTIVATING NEUROPEPTIDE AND OTHER NEUROPEPTIDES, Proceedings of the National Academy of Sciences of the United Statesof America, 91(14), 1994, pp. 6506-6510
Sex pheromone biosynthesis in a number of moth species is induced by a
conserved 33-amino acid amidated neuropeptide PBAN (pheromone biosynt
hesis-activating neuropeptide). We have isolated and characterized the
Helicoverpa zea PBAN cDNA corresponding to a 766-nucleotide mRNA that
is expressed in the subesophageal ganglion of adult moths. This mRNA
is encoded on a transcription unit comprising 6 exons. The longest ope
n reading frame of the cDNA encodes a 194-amino acid precursor protein
that contains the PBAN peptide sequence. Proteolytic processing of th
is protein, which has structural features consistent with its being a
preprohormone, is predicted to generate Hez-PBAN and four additional n
europeptides having a common C-terminal pentapeptide motif, Phe-Xaa-Pr
o-(Arg or Lys)-Leu (Xaa = Gly, Ser, or Thr), which is also found in in
sect pyrokinin and myotropin peptide families.