Journal
INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY
Volume 37, Issue 12, Pages 1262-1271Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.ibmb.2007.07.012
Keywords
diapause hormone (DH); pheromone biosynthesis activating neuropeptide (PBAN); developmental expression; Clostera anastomosis
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Using a strategy of rapid amplification of cDNA ends, the cDNA of diapause hormone (DH) and pheromone biosynthesis activating neuropeptide (PBAN) was cloned from the head of Clostera anastomosis (L.). The Cloan-DH-PBAN cDNA contains an open reading frame encoding a 196-amino acid preprohormone, from which five putative FXPRL peptides, DH, PBAN, alpha-SGNP(SGNP, suboesophageal ganglion neuropeptide), beta-SGNP and gamma-SGNP, are released. Comparing the deduced amino acid sequences from cDNAs of these five FXPRL peptides to those known from other insects, Cloan-DH shows highest similarity of 93.1% to that from Agrotis ipsilon. Cloan-PBAN 93.9% to those from Helicoverpa armigera, Helicoverpa zea and Helicoverpa assulta, which show the highest similarity to species of Noctuidae. Phylogenetic analysis revealed that the Cloan-DH-PBAN gene is relatively closely related to those from Noctuoidea, but distant from those from Tortricoidea, Yponomeutoidea and Bombycoidea species. The DNA sequence encoding Cloan-DH-PBAN was cloned by PCR, which is 3698 bp in size and comprises six exons interspersed by five introns. Developmental expression of the DH-PBAN transcripts in the head was also showed by a semi-quantitative RT-PCR method, which was relatively low in larvae and remained low in pupae of both sexes, increased sharply in adults of both sexes. (c) 2007 Elsevier Ltd. All rights reserved.
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