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
期刊:
The Biological Bulletin
影响因子:
--
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
Shaoguang Sun;Weiquan Liu;Jigui Wang;Shu-Yan Yang;Ling Gu;Yan Hong;Dan-Dan Shang-Dan;B. Wang;Xiaoming Su;S. Qi
中科院分区:
其他
文献类型:
--
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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酚氧化酶(PO)是一种具有加氧酶活性的含铜酶,可以将单酚或二酚转化为醌,在节肢动物的黑化反应中发挥重要作用。本文报道了家蝇幼虫PO的一个新特性:具有耐热性内切酶活性,即使在80° C下加热20 min,PO仍能降解质粒DNA。表达产物与纯化的PO具有相同的性质。我们的数据表明PO是一种双功能酶,同时表现出加氧酶和核酸内切酶活性,这表明这种重要分子在M的先天反应中发挥了新的作用。南极洲
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.