Molecular Heterogeneity of TIME-EA4, a Timer Protein in Silkworm Diapause Eggs

Pitchayawasin-Thapphasaraphong, Suthasinee; Tani, Naoki; Isobe, Mitsuaki; Huang, Kai; Kurahashi, Takuya; Katô, Junko; Trisunan, Saikwan

doi:10.1271/bbb.90066

Cited by 1 publication

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“…Studies of time interval measuring enzyme-esterase A4 (TIME-EA4) from diapause eggs of the silkworm Bombyx mori (B.mori) show that the protein is a time-dependent ATPase that may regulate the diapause duration of B.mori eggs [13] . TIME-EA4, which also named diapause bio-clock protein or TIME, had been identified as an esterase, acting as a single, transitory activation burst for the termination of the B.mori diapause two weeks after eggs had been chilled at 5°C [14] .…”

Section: Introductionmentioning

confidence: 99%

Diapause-Associated Protein3 Functions as Cu/Zn Superoxide Dismutase in the Chinese Oak Silkworm (Antheraea pernyi)

Yang

et al. 2014

PLoS ONE

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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 constructed a prokaryotic expression vector by inserting the coding region sequence into plasmid pET-28a (+) and obtained the purified rHIS-DAP3 fusion protein by Ni-NTA affinitive column. Importantly, we found the SOD activity of DAP3 fusion protein was approximately 0.6674 U/µg. To further confirm the SOD activity of DAP3 in vivo, we induced the oxidative stress model of pupae by UV irradiation. The results showed that both the mRNA and protein level of DAP3 significantly increased by UV irradiation. Furthermore, the SOD activity of the total lysate of pupae increased significantly at 10 min post UV irradiation and transiently returned to normal level afterwards. These results suggested that DAP3 might be a novel protein with SOD activity getting involved in regulation of diapause in A.pernyi.

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Section: Introductionmentioning

confidence: 99%

Diapause-Associated Protein3 Functions as Cu/Zn Superoxide Dismutase in the Chinese Oak Silkworm (Antheraea pernyi)

Yang

et al. 2014

PLoS ONE

View full text Add to dashboard Cite

show abstract

Molecular Heterogeneity of TIME-EA4, a Timer Protein in Silkworm Diapause Eggs

Cited by 1 publication

References 10 publications

Diapause-Associated Protein3 Functions as Cu/Zn Superoxide Dismutase in the Chinese Oak Silkworm (Antheraea pernyi)

Diapause-Associated Protein3 Functions as Cu/Zn Superoxide Dismutase in the Chinese Oak Silkworm (Antheraea pernyi)

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