Endonuclease activity of phenol oxidase from Musca domestica larvae |
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Authors: | Sun Shaoguang Liu Weiquan Wang Jigui Yang Shuyan Gu Ling Hong Yan Shang Dan Wang Benxu Su Xiaoming Qi Shunzhang |
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Institution: | Department of Biochemistry and Molecular Biology, China Agricultural University, Beijing 100094, China. |
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Abstract: | Phenol oxidase (PO), a copper-containing enzyme with oxygenase activity, can convert mono- or diphenol into quinone and plays an important role in the arthropod melanization reaction. Here, we report a new property of PO from Musca domestica larvae: a thermotolerant endonuclease activity, by which PO can degrade plasmid DNA even after being heated to 80 degrees C for 20 min. We cloned PO cDNA, constructed the expression vector pVAX1-PO, and expressed it in HeLa cells. The expression product showed the same properties as purified PO. Our data indicate that PO is a bifunctional enzyme, exhibiting both oxygenase and endonuclease activity, suggesting new roles for this important molecule in the innate responses of M. domestica. |
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