Molecular Cloning and Expression Analysis of the Gene Encoding DDC in the Ant Polyrhachis vicina Roger (Hymenoptera: Formicidae)

Abstract

L-3, 4-Dihydroxyphenylalanine decarboxylase (DDC) is an important enzyme which catalyses L-dopa decarboxylation to dopamine in the synthesis of catecholamine neurotransmitters and (5-HTP) to 5-hydroxytryptamine (5-HT). In this paper, a DDC homologue was isolated from Polyrhachis vicinna Roger (Hymenoptera: Formicidae). The full length cDNA of PvDDC is 1893 base pairs (bp) and contains a 5'-untranslated region of71 nucleotides and a 3'-UTR 379 bp long. The open reading frame of PvDDC encodes a deduced 480-amino acid peptide. Real-time quantitative reverse transcription polymerase chain reaction was used to compare PvDDC mRNA expression during P. vicina development in different castes. The results show that PvDDC mRNA is differentially expressed in different stages of ant development, in whole bodies and the heads of different castes. During the development, the highest expression level is in pupae. The levels also vary among castes, the highest level is in males. These investigations indicate that PvDDC mRNA possesses a function to regulate ant caste-specificity and development at the level of transcription.

Keywords

• L-3
• 4-Dihydroxyphenylalanine decarboxylase (DDC)
• Molecular Cloning
• Polyrhachis vicina Roger
• Real-time quantitative PCR