Diapause-associated protein3 functions as Cu/Zn superoxide dismutase in the Chinese oak silkworm (Antheraea pernyi).

ABSTRACT: To better understand the molecular mechanism underlying of diapause in Antheraea pernyi (A. pernyi), we cloned a novel diapause-associated protein 3 (DAP3) gene from A. pernyi by reverse transcription-polymerase chain reaction (RT-PCR) and studied the biological functions. Sequence analysis revealed that this gene encodes 171 amino acids and has a conserved domain of Copper/Zinc superoxide dismutase (Cu/Zn-SOD). Western blot and qRT-PCR results showed that DAP3 was mainly expressed in the pupal stage, and gradually decreased as diapause development. DAP3 was also expressed in 1st and 5th instar larvae of A. pernyi. In tissues of 5th instar larvae of A. pernyi, DAP3 was mainly expressed in the epidermis, followed by the head, hemolymph and fat body. To identify the SOD activity of DAP3, we

SUBMITTER: Bi Z 

PROVIDER: S-EPMC3948625 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature