Functional identification of the DNA packaging terminase from Pseudomonas aeruginosa phage PaP3.

Functional identification of the DNA packaging terminase from Pseudomonas aeruginosa phage PaP3.
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铜绿假单胞菌噬菌体 PaP3 DNA 包装终止酶的功能鉴定

DOI:
10.1007/s00705-012-1409-5
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发表时间:
2012-11
影响因子:
2.7
通讯作者:
Hu, Fuquan
Hu, Fuquan
中科院分区:
医学4区
文献类型:
--
作者:
Shen, Xiaodong;Li, Ming;Zeng, Yijun;Hu, Xiaomei;Tan, Yinling;Rao, Xiancai;Jin, Xiaolin;Li, Shu;Zhu, Junmin;Zhang, Kebin;Hu, Fuquan

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终止酶蛋白负责DNA识别和DNA包装的启动。我们以前报道了温和的铜绿假单胞菌噬菌体,PaP3的基因组序列,并确定其在宿主细菌染色体的精确整合位点。在这项研究中,我们提出了一个详细的功能鉴定噬菌体PaP3的DNA包装末端酶。纯化的大亚基p03被证明具有ATP酶和核酸酶活性,以及在未组装时结合特异性DNA的能力。此外,还发现了一种新型的小末端酶亚基(p01),它能特异性地与含cos的DNA结合,并能刺激p03的cos切割和ATP酶活性。这里提出的结果表明,PaP3利用一个典型的COS网站的DNA包装机制,并提供了第一步了解PaP3 DNA包装反应的分子机制。
Terminase proteins are responsible for DNA recognition and initiation of DNA packaging in phages. We previously reported the genomic sequence of a temperate Pseudomonas aeruginosa phage, PaP3, and determined its precise integration site in the host bacterial chromosome. In this study, we present a detailed functional identification of the DNA packaging terminase for phage PaP3. The purified large subunit p03 was demonstrated to possess ATPase and nuclease activities, as well as the ability to bind to specific DNA when it is unassembled. In addition, a small terminase subunit (p01) of a new type was found and shown to bind specifically to cos-containing DNA and stimulate the cos-cleavage and ATPase activities of p03. The results presented here suggest that PaP3 utilizes a typical cos site mechanism for DNA packaging and provide a first step towards understanding the molecular mechanism of the PaP3 DNA packaging reaction.
DOI: 10.1021/bi052284b
发表时间: 2006-04-25
期刊: BIOCHEMISTRY
影响因子: 2.9
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通讯作者: Catalano, CE
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