Endonuclease Activity of Phenol Oxidase From Musca domestica Larvae
Endonuclease Activity of Phenol Oxidase From Musca domestica Larvae
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DOI:
10.2307/25470688
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发表时间:
2008-08
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通讯作者:
Shaoguang Sun;Weiquan Liu;Jigui Wang;Shu-Yan Yang;Ling Gu;Yan Hong;Dan-Dan Shang-Dan;B. Wang;Xiaoming Su;S. Qi
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文献类型:
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作者:
Shaoguang Sun;Weiquan Liu;Jigui Wang;Shu-Yan Yang;Ling Gu;Yan Hong;Dan-Dan Shang-Dan;B. Wang;Xiaoming Su;S. Qi
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° 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.